细胞信号通路大全

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细胞信号通路大全

1PPAR信号通路：过氧化物酶体增殖物激活受体(PPARs)是与维甲酸、类固醇和甲状腺激素受体相关的配体激活转录因子超家族核激素受体成员。

它们作为脂肪传感器调节脂肪代谢酶的转录。

PPARs由PPARα、PPARβ和PPARγ3种亚型组成。

PPARα主要在脂肪酸代谢水平高的组织，如：肝、棕色脂肪、心、肾和骨骼肌表达。

他通过调控靶基因的表达而调节机体许多生理功能包括能量代谢、生长发育等。

另外，他还通过调节脂质代谢的生物感受器而调节细胞生长、分化与凋亡。

PPARa同时也是一种磷酸化蛋白，他受多种磷酸化酶的调节包括丝裂原激活蛋白激酶(ERK-和p38．MAPK)，蛋白激酶A和C(PKA，PKC)，AMPK和糖原合成酶一3(GSK3)等调控。

调控PPARa生长信号的酶报道有MAPK、PKA和GSK3。

PPARβ广泛表达于各种组织，而PPARγ主要局限表达在血和棕色脂肪，其他组织如骨骼肌和心肌有少量表达。

PPAR-γ在诸如炎症、动脉粥样硬化、胰岛素抵抗和糖代谢调节，以及肿瘤和肥胖等方面均有着举足轻重的作用，而其众多生物学效应则是通过启动或参与的复杂信号通路予以实现。

鉴于目前人们对PPAR—γ信号通路尚不甚清，PPARs通常是通过与9-cis维甲酸受体(RXR)结合实现其转录活性的。

2MAPK信号通路:mapk简介:丝裂原激活蛋白激酶（mitogen—activatedproteinkinase，MAPK）是广泛存在于动植物细胞中的一类丝氨酸/苏氨酸蛋白激酶。

作用主要是将细胞外刺激信号转导至细胞及其核内，并引起细胞的生物化学反应（增殖、分化、凋亡、应激等）。

MAPKs家族的亚族:ERKs（extracellularsignalregulatedkinase) ：包括ERK1、ERK2。

生长因子、细胞因子或激素激活此通路，介导细胞增殖、分化。

JNKs(c-JunN-terminalkinase)包括JNK1、JNK2、JNK3。

细胞信号通路大全

1 PPAR信号通路：过氧化物酶体增殖物激活受体( PPARs) 是与维甲酸、类固醇和甲状腺激素受体相关的配体激活转录因子超家族核激素受体成员。

它们作为脂肪传感器调节脂肪代谢酶的转录。

PPARs由PPARα、PPARβ和PPARγ 3种亚型组成。

PPARα主要在脂肪酸代谢水平高的组织，如：肝、棕色脂肪、心、肾和骨骼肌表达。

他通过调控靶基因的表达而调节机体许多生理功能包括能量代谢、生长发育等。

另外，他还通过调节脂质代谢的生物感受器而调节细胞生长、分化与凋亡。

PPARa同时也是一种磷酸化蛋白，他受多种磷酸化酶的调节包括丝裂原激活蛋白激酶( ERK-和p38．M APK) ，蛋白激酶A和C( PKA，PKC) ，AM PK和糖原合成酶一3( G SK3) 等调控。

调控PPARa生长信号的酶报道有M APK、PKA和G SK3。

PPARβ广泛表达于各种组织，而PPAR γ主要局限表达在血和棕色脂肪，其他组织如骨骼肌和心肌有少量表达。

鉴于目前人们对PPAR—γ信号通路尚不甚清，PPARs 通常是通过与9-cis维甲酸受体( RXR)结合实现其转录活性的。

2 MAPK信号通路:mapk简介:丝裂原激活蛋白激酶（mitogen—activated protein kinase，MAPK）是广泛存在于动植物细胞中的一类丝氨酸/苏氨酸蛋白激酶。

作用主要是将细胞外刺激信号转导至细胞及其核内，并引起细胞的生物化学反应（增殖、分化、凋亡、应激等）。

MAPKs家族的亚族 :ERKs（extracellular signal regulated kinase)：包括ERK1、ERK2。

生长因子、细胞因子或激素激活此通路，介导细胞增殖、分化。

JNKs(c-Jun N-terminal kinase)包括JNK1、JNK2、JNK3。

细胞信号通路大全

信号通路与免疫系统疾病
自身免疫疾病
自身免疫疾病患者体内免疫细胞信号通路异常激活，如T细胞、B细胞等信号通路，导致自身免疫反应过度。
炎症性疾病
炎症性疾病患者体内炎症细胞信号通路异常激活，如NF-κB、MAPK等信号通路，导致炎症反应过度或持续。
感染性疾病
感染性疾病患者体内病原微生物通过干扰免疫细胞信号通路，如细菌、病毒等，逃避免疫细胞的攻击。
PI3K-Akt信号通路
PI3K-Akt信号通路是细胞生存和增殖的关键信号转导途径。
PI3K-Akt信号通路在细胞生长、代谢、存活和凋亡等过程中发挥重要作用。当细胞受到生长因子、激素等刺激时，PI3K被激活，进而催化生成PIP3，后者与Akt结合并使其磷酸化，从而激活Akt。Akt可以进一步调控下游的靶蛋白，参与细胞增殖、迁移、代谢等过程。
JAK-STAT信号通路
JAK-STAT信号通路是细胞因子信号转导的重要途径之一。
JAK-STAT信号通路在细胞因子信号转导中发挥关键作用。当细胞因子与受体结合后，JAK被激活并催化受体酪氨酸磷酸化，进而招募并磷酸化STAT蛋白。STAT蛋白形成二聚体并进入细胞核，调控靶基因的表达，参与细胞生长、分化、免疫调节等过程。
信号通路的自调节
信号通路的正反馈调节
自调节的一种形式是正反馈调节，它通过增加某个关键信号分子的数量或活性，进一步增强自身的信号传递。例如，某些生长因子可以诱导自身受体的表达，形成一个正反馈环路，不断放大信号传递。
信号通路的负反馈调节
另一种自调节形式是负反馈调节，它通过降低某个关键信号分子的数量或活性，来抑制自身的信号传递。例如，某些激素可以通过诱导产生拮抗性激素或受体，从而抑制自身的信号传递。

细胞信号通路

Cell Signalling Pathways--Michael J. Berridge--module 2 胞内信号通路可分为两类，大多数的信号通路受细胞表面的胞外信号刺激，通常以化学信号的形式，如神经递质、激素及生长因子等；其他类的信号通路是由细胞内产生的信号激活的。

胞内信号主要来自内质网或代谢物。

一、环腺苷酸信号通路（Cyclic AMP signalling pathway）环腺苷酸是广泛存在的一种第二信使，其形成依赖于GPCR的活化，GPCR通过异质三聚体激活放大器AC（腺苷酸环化酶）。

cAMP的信号效应器有PKA、EPACs等可激活小GTP连接蛋白Rap1及环核苷酸门控通道（CNGCs），这些效应器负责进行cAMP信号功能。

cAMP 的许多功能取决于PKA的准确定位，而A激酶锚定蛋白（AKAPs）家族约定了PKA及其他许多信号组分的细胞定位。

Cyclic AMP formation环腺苷酸的形成可被许多细胞刺激活化，主要是神经递质和激素，这些刺激可被G蛋白偶联受体通过异质三聚体G蛋白检测到。

在腺苷酸环化酶刺激下，外部刺激结合到G蛋白偶联受体上，作为鸟苷酸交换因子（GEF）用GTP替代GDP，从而使得异质三聚体G蛋白分裂成Gβᵞ和Gα亚基。

Gα亚基和GTP的复合体激活腺苷酸环化酶，然而抑制性GαGTP 抑制AC。

Ｇα亚基具有GTP酶活性，可水解GTP成GDP，因而停止其对AC的作用。

Adenylyl cyclase (AC)AC家族由十个亚型组成，前九个为膜结合的，另外一个是水溶性的。

AC1-9的域结构具有两个含六个转膜区的区域。

大的细胞浆域C1和C2含有催化区，形成异质二聚体使得ATP 转化成AMP。

Cyclic AMP signalling effectorsEPACs、CNGCs等，cAMP的大多数作用都是通过PKA发挥作用的。

Protein kinase A (PKA)PKA由两个调节亚基（R）和两个催化亚基（C）组成。

细胞信号通路大全

1 PPAR信号通路：过氧化物酶体增殖物激活受体( PPARs) 是与维甲酸、类固醇和甲状腺激素受体相关的配体激活转录因子超家族核激素受体成员。

它们作为脂肪传感器调节脂肪代谢酶的转录。

PPARs由PPARα、PPARβ和PPARγ 3种亚型组成。

PPARα主要在脂肪酸代谢水平高的组织，如：肝、棕色脂肪、心、肾和骨骼肌表达。

他通过调控靶基因的表达而调节机体许多生理功能包括能量代谢、生长发育等。

另外，他还通过调节脂质代谢的生物感受器而调节细胞生长、分化与凋亡。

PPARa同时也是一种磷酸化蛋白，他受多种磷酸化酶的调节包括丝裂原激活蛋白激酶( ERK-和p38．M APK) ，蛋白激酶A和C( PKA，PKC) ，AM PK和糖原合成酶一3( G SK3) 等调控。

调控PPARa生长信号的酶报道有M APK、PKA和G SK3。

PPARβ广泛表达于各种组织，而PPAR γ主要局限表达在血和棕色脂肪，其他组织如骨骼肌和心肌有少量表达。

鉴于目前人们对PPAR—γ信号通路尚不甚清，PPARs 通常是通过与9-cis维甲酸受体( RXR)结合实现其转录活性的。

2 MAPK信号通路:mapk简介:丝裂原激活蛋白激酶（mitogen—activated protein kinase，MAPK）是广泛存在于动植物细胞中的一类丝氨酸/苏氨酸蛋白激酶。

作用主要是将细胞外刺激信号转导至细胞及其核内，并引起细胞的生物化学反应（增殖、分化、凋亡、应激等）。

MAPKs家族的亚族 :ERKs（extracellular signal regulated kinase)：包括ERK1、ERK2。

生长因子、细胞因子或激素激活此通路，介导细胞增殖、分化。

JNKs(c-Jun N-terminal kinase)包括JNK1、JNK2、JNK3。

专题二常见的细胞信号转导通路

２、螺旋结构域：位于135~315位氨基酸残基之间，由4个螺旋组成，主要负责STAT蛋白与其它蛋白的相互作用。
3、DNA结合结构域：位于320~490位氨基酸残基之间，含有几个β-折叠结构，与靶基因的启动子结合，启动靶基因的转录。不同的STAT蛋白具有不同的DNA结合特异性。
JAK-STAT信号通路
NF-κB信号通路
• NF-κB信号通路分为的经典信号通路和非经典信号通路
• 在NF-κB经典信号通路中， IκB蛋白的降解使 NF-κB二聚体得到释放
• 在NF-κB非经典信号通路中，则是通过P100到 P52的加工处理，是信号通路激活
NF-κB信号通路
IκB激酶复合物
• IKKα • IKKβ • 调节亚基NEMO
另外，TRAF2-7的N-末端存在一个RING指结构，其可以作为E3 泛素连接酶起作用，即将泛素转移到目的蛋白上。RING 指结构后还有5 到7 个锌指结构域
NF-κB信号通路
TRAFs的功能
通过TRADD，TRAF2和 TNF-α 的受体TNFR1结合，向下传递信号，激活IKK。在此过程中，其RING指区域作为E3连接酶是必须的。但是其具体作用机制还需要深入研究。
JAK-STAT信号通路
• 受体的二聚化可以是同源的也可以是异源的。在发生同源受体二聚化时，只有JAK2被激活；相反，由不同亚基组成的异源受体二聚化，却可以激活多种JAK。一旦被激活，JAK便磷酸化受体的亚基以及其他底物。
JAK-STAT信号通路
酪氨酸激酶JAK（Janus kinase）
• 每个成员N端都有一个高度保守的Rel同源结构域（RHD ），由约300个氨基酸组成，包含结合特异性DNA序列的基序；蛋白二聚化的基序；一个核定位基序。

细胞信号通路大全

细胞信号通路⼤全1 PPAR信号通路：过氧化物酶体增殖物激活受体( PPARs) 是与维甲酸、类固醇和甲状腺激素受体相关的配体激活转录因⼦超家族核激素受体成员。

它们作为脂肪传感器调节脂肪代谢酶的转录。

PPARs由PPARα、PPARβ和PPARγ 3种亚型组成。

PPARα主要在脂肪酸代谢⽔平⾼的组织，如：肝、棕⾊脂肪、⼼、肾和⾻骼肌表达。

他通过调控靶基因的表达⽽调节机体许多⽣理功能包括能量代谢、⽣长发育等。

另外，他还通过调节脂质代谢的⽣物感受器⽽调节细胞⽣长、分化与凋亡。

PPARa同时也是⼀种磷酸化蛋⽩，他受多种磷酸化酶的调节包括丝裂原激活蛋⽩激酶( ERK-和p38．M APK) ，蛋⽩激酶A和C( PKA，PKC) ，AM PK和糖原合成酶⼀3( G SK3) 等调控。

调控PPARa⽣长信号的酶报道有M APK、PKA和G SK3。

PPARβ⼴泛表达于各种组织，⽽PPAR γ主要局限表达在⾎和棕⾊脂肪，其他组织如⾻骼肌和⼼肌有少量表达。

PPAR-γ在诸如炎症、动脉粥样硬化、胰岛素抵抗和糖代谢调节，以及肿瘤和肥胖等⽅⾯均有着举⾜轻重的作⽤，⽽其众多⽣物学效应则是通过启动或参与的复杂信号通路予以实现。

鉴于⽬前⼈们对PPAR—γ信号通路尚不甚清，PPARs通常是通过与9-cis维甲酸受体( RXR)结合实现其转录活性的。

2 MAPK信号通路:mapk简介:丝裂原激活蛋⽩激酶（mitogen—activated protein kinase，MAPK）是⼴泛存在于动植物细胞中的⼀类丝氨酸/苏氨酸蛋⽩激酶。

作⽤主要是将细胞外刺激信号转导⾄细胞及其核内，并引起细胞的⽣物化学反应（增殖、分化、凋亡、应激等）。

MAPKs家族的亚族 :ERKs（extracellular signal regulated kinase)：包括ERK1、ERK2。

⽣长因⼦、细胞因⼦或激素激活此通路，介导细胞增殖、分化。

JNKs(c-Jun N-terminal kinase)包括JNK1、JNK2、JNK3。

细胞信号通路大全.pdf

1 PPAR信号通路：过氧化物酶体增殖物激活受体( PPARs) 是与维甲酸、类固醇和甲状腺激素受体相关的配体激活转录因子超家族核激素受体成员。

它们作为脂肪传感器调节脂肪代谢酶的转录。

PPARs由PPARα、PPARβ和PPARγ 3种亚型组成。

PPARα主要在脂肪酸代谢水平高的组织，如：肝、棕色脂肪、心、肾和骨骼肌表达。

他通过调控靶基因的表达而调节机体许多生理功能包括能量代谢、生长发育等。

另外，他还通过调节脂质代谢的生物感受器而调节细胞生长、分化与凋亡。

PPARa同时也是一种磷酸化蛋白，他受多种磷酸化酶的调节包括丝裂原激活蛋白激酶( ERK-和p38．M APK) ，蛋白激酶A和C( PKA，PKC) ，AM PK和糖原合成酶一3( G SK3) 等调控。

调控PPARa生长信号的酶报道有M APK、PKA和G SK3。

PPARβ广泛表达于各种组织，而PPAR γ主要局限表达在血和棕色脂肪，其他组织如骨骼肌和心肌有少量表达。

鉴于目前人们对PPAR—γ信号通路尚不甚清，PPARs 通常是通过与9-cis维甲酸受体( RXR)结合实现其转录活性的。

2 MAPK信号通路:mapk简介:丝裂原激活蛋白激酶（mitogen—activated protein kinase，MAPK）是广泛存在于动植物细胞中的一类丝氨酸/苏氨酸蛋白激酶。

作用主要是将细胞外刺激信号转导至细胞及其核内，并引起细胞的生物化学反应（增殖、分化、凋亡、应激等）。

：包括ERK1、MAPKs家族的亚族 :ERKs（extracellular signal regulated kinase)ERK2。

生长因子、细胞因子或激素激活此通路，介导细胞增殖、分化。

JNKs(c-Jun N-terminal kinase)包括JNK1、JNK2、JNK3。

细胞常见信号通路图片合集

•·NGF信号通路(2004-8-16)•·TGF beta 信号转导(2004-8-16)•·细胞凋亡信号(2004-8-16)•·线粒体输入信号(2004-8-16)•·ROS信号(2004-8-16)•·Toll-Like 受体家族(2004-8-16)•·Toll-Like 受体(2004-8-16)•·actin肌丝(2004-8-16)•·Wnt/LRP6 信号(2004-8-16)•·WNT信号转导(2004-8-16)•·West Nile 西尼罗河病毒(2004-8-16)•·Vitamin C 维生素C在大脑中的作用(2004-8-16)•·视觉信号转导(2004-8-16)•·VEGF，低氧(2004-8-16)•·TSP-1诱导细胞凋亡(2004-8-16)•·Trka信号转导(2004-8-16)•·dbpb调节mRNA (2004-8-16)•·CARM1甲基化(2004-8-16)•·CREB转录因子(2004-8-16)•·TPO信号通路(2004-8-16)•·Toll-Like 受体(2004-8-16)•·TNFR2 信号通路(2004-8-16)•·TNFR1信号通路(2004-8-16)•·TNF/Stress相关信号(2004-8-16)•·IGF-1受体(2004-8-16)•·共刺激信号(2004-8-16)•·Th1/Th2 细胞分化(2004-8-16)•·TGF beta 信号转导(2004-8-16)•·端粒、端粒酶与衰老(2004-8-16)•·TACI和BCMA调节B细胞免疫(2004-8-16)•·T辅助细胞的表面受体(2004-8-16)•·T细胞受体信号通路(2004-8-16)•·T细胞受体和CD3复合物(2004-8-16)•·Cardiolipin的合成(2004-8-16)•·Synaptic突触连接中的蛋白(2004-8-16)•·HSP在应激中的调节的作用(2004-8-16)•·Stat3 信号通路(2004-8-16)•·SREBP控制脂质合成(2004-8-16)•·酪氨酸激酶的调节(2004-8-16)•·Sonic Hedgehog (SHH)受体ptc1调节细胞周期(2004-8-16)•·Sonic Hedgehog (Shh) 信号(2004-8-16)•·SODD/TNFR1信号(2004-8-16)•·AKT/mTOR在骨骼肌肥大中的作用(2004-8-16)•·G蛋白信号转导(2004-8-16)•·肝细胞生长因子受体信号(2004-8-16)•·IL1受体信号转导(2004-8-16)•·acetyl从线粒体到胞浆过程(2004-8-16)•·趋化因子chemokine在T细胞极化中的选择性表(2004-8-16)•·SARS冠状病毒蛋白酶(2004-8-16)•·Parkin在泛素-蛋白酶体中的作用(2004-8-16)•·nicotinic acetylcholine受体在凋亡中的作用(2004-8-16)•·线粒体在细胞凋亡中的作用(2004-8-16)•·MEF2D在T细胞凋亡中的作用(2004-8-16)•·Erk5和神经元生存(2004-8-16)•·ERBB2信号转导(2004-8-16)•·GPCRs调节EGF受体(2004-8-16)•·BRCA1调节肿瘤敏感性(2004-8-16)•·Rho细胞运动的信号(2004-8-16)•·Leptin能逆转胰岛素抵抗(2004-8-16)•·转录因子DREAM调节疼敏感(2004-8-16)•·PML调节转录(2004-8-16)•·p27调节细胞周期(2004-8-16)•·MAPK信号调节(2004-8-16)•·细胞因子调节造血细胞分化(2004-8-16)•·eIF4e和p70 S6激酶调节(2004-8-16)•·eIF2调节(2004-8-16)•·谷氨酸受体调节ck1/cdk5 (2004-8-16)•·plk3在细胞周期中的作用(2004-8-1)•·BAD磷酸化调节(2004-8-1)•·Reelin信号通路(2004-8-1)•·RB肿瘤抑制和DNA破坏(2004-8-1)•·NK细胞介导的细胞毒作用(2004-8-1)•·Ras信号通路(2004-8-1)•·Rac 1细胞运动信号(2004-8-1)•·PTEN依赖的细胞生长抑制和细胞凋亡(2004-8-1)•·notch信号通路(2004-8-1)•·蛋白激酶A（PKA）在中心粒中的作用(2004-8-1)•·蛋白酶体Proteasome复合物(2004-8-1)•·Prion朊病毒的信号通路(2004-8-1)•·早老素Presenilin在notch和wnt信号中的作用(2004-8-1)•·mRNA的poly(A)形成(2004-8-1)•·淀粉样蛋白前体信号(2004-8-1)•·PKC抑制myosin磷酸化(2004-8-1)•·磷脂酶C（PLC）信号(2004-8-1)•·巨噬细胞Pertussis toxin不敏感的CCR5信号通(2004-8-1)•·Pelp1调节雌激素受体的活性(2004-8-1)•·PDGF信号通路(2004-8-1)•·p53信号通路(2004-8-1)•·p38MAPK信号通路(2004-8-1)•·Nrf2是氧化应激基本表达的关键基因(2004-8-1)•·OX40信号通路(2004-8-1)•·hTerc转录调节活性图(2004-8-1)•·hTert转录因子的调节作用(2004-8-1)•·AIF在细胞凋亡中的作用(2004-8-1)•·Omega氧化通路(2004-8-1)•·核受体在脂质代谢和毒性中的作用(2004-8-1)•·NK细胞中NO2依赖的IL-12信号通路(2004-8-1)•·TOR信号通路(2004-8-1)•·NO信号通路(2004-8-1)•·NF-kB信号转导通路(2004-8-1)•·NFAT与心肌肥厚的示意图(2004-8-1)•·神经营养素及其表面分子(2004-8-1)•·神经肽VIP和PACAP防止活化T细胞凋亡图(2004-8-1)•·神经生长因子信号图(2004-8-1)•·线虫和哺乳动物的MAPK信号比较(2004-7-17)•·细胞内信号总论(2004-7-17)•·细胞凋亡信号通路(2004-7-17)•·MAPK级联通路(2004-7-17)•·MAPK信号通路图(2004-7-17)•·BCR信号通路(2004-7-17)•·蛋白质乙酰化示意图(2004-7-17)•·wnt信号通路(2004-7-17)•·胰岛素受体信号通路(2004-7-17)•·细胞周期在G2/M期的调控机理图(2004-7-17)•·细胞周期G1/S检查点调控机理图(2004-7-17)•·Jak-STAT关系总表(2004-7-17)•·Jak/STAT 信号(2004-7-17)•·TGFbeta信号(2004-7-17)•·NFkappaB信号(2004-7-17)•·p38 MAPK信号通路(2004-7-17)•·SAPK/JNK 信号级联通路(2004-7-17)•·从G蛋白偶联受体到MAPK (2004-7-17)•·MAPK级联信号图(2004-7-17)•·eIF-4E和p70 S6激酶调控蛋白质翻译(2004-7-17)•·eif2蛋白质翻译(2004-7-17)•·蛋白质翻译示意图(2004-7-17)•·线粒体凋亡通路(2004-7-17)•·死亡受体信号通路(2004-7-17)•·凋亡抑制通路(2004-7-17)•·细胞凋亡综合示意图(2004-7-17)•·Akt/Pkb信号通路(2004-7-17)•·MAPK/ERK信号通路(2004-7-17)•·哺乳动物MAPK信号通路(2004-7-17)•·Pitx2多步调节基因转录(2004-7-17)•·IGF-1R导致BAD磷酸化的多个凋亡路径(2004-7-17)•·多重耐药因子(2004-7-17)•·mTOR信号通路(2004-7-17)•·Msp/Ron受体信号通路(2004-7-17)•·单核细胞和其表面分子(2004-7-17)•·线粒体的肉毒碱转移酶（CPT）系统(2004-7-17)•·METS影响巨噬细胞的分化(2004-7-17)•·Anandamide，内源性大麻醇的代谢(2004-7-17)•·黑色素细胞（Melanocyte）发育和信号(2004-7-17)•·DNA甲基化导致转录抑制的机理图(2004-7-17)•·蛋白质的核输入信号图(2004-7-17)•·PPARa调节过氧化物酶体的增殖(2004-7-17)•·对乙氨基酚（Acetaminophen）的活性和毒性机(2004-7-17)•·mCalpain在细胞运动中的作用(2004-7-17)•·MAPK信号图(2004-7-17)•·MAPK抑制SMRT活化(2004-7-17)•·苹果酸和天门冬酸间的转化(2004-7-17)•·低密度脂蛋白（LDL）在动脉粥样硬化中的作用(2004-7-17)•·LIS1基因在神经细胞的发育和迁移中的作用图(2004-7-17)•·Pyk2与Mapk相连的信号通路(2004-7-17)•·galactose代谢通路(2004-7-17)•·Lectin诱导补体的通路(2004-7-17)•·Lck和Fyn在TCR活化中的作用(2004-7-17)•·乳酸合成图(2004-7-17)•·Keratinocyte分化图(2004-7-17)•·离子通道在心血管内皮细胞中的作用(2004-7-17)•·离子通道和佛波脂（Phorbal Esters）信号(2004-7-17)•·内源性Prothrombin激活通路(2004-7-17)•·Ribosome内化通路(2004-7-17)•·整合素（Integrin）信号通路(2004-7-17)•·胰岛素（Insulin）信号通路(2004-7-17)•·Matrix Metalloproteinases (2004-7-17)•·组氨酸去乙酰化抑制剂抑制Huntington病(2004-7-17)•·Gleevec诱导细胞增殖(2004-7-17)•·Ras和Rho在细胞周期的G1/S转换中的作用(2004-7-17)•·DR3，4，5受体诱导细胞凋亡(2004-7-17)•·AKT调控Gsk3图(2004-7-17)•·IL-7信号转导(2004-7-17)•·IL22可溶性受体信号转导图(2004-7-17)•·IL-2活化T细胞图(2004-7-17)•·IL12和Stat4依赖的TH1细胞发育信号通路(2004-7-17)•·IL-10信号通路(2004-7-17)•·IL 6信号通路(2004-7-17)•·IL 5信号通路(2004-7-17)•·IL 4信号通路(2004-7-17)•·IL 3信号通路(2004-7-17)•·IL 2 信号通路(2004-7-17)•·IL 18信号通路(2004-7-17)•·IL 17信号通路(2004-7-17)•·IGF-1信号通路(2004-7-17)•·IFN gamma信号通路(2004-7-17)•·INF信号通路(2004-7-17)•·低氧诱导因子（HIF）在心血管中的作用(2004-7-17)•·低氧和P53在心血管系统中的作用(2004-7-17)•·人类巨细胞病毒和MAP信号通路(2004-7-17)•·孕酮如何促进卵细胞成熟？(2004-7-17)•·How does salmonella hijack a cell (2004-7-17)•·Hop通路在心脏发育中的作用(2004-7-17)•·HIV-I Nef:负性调节fas和TNF (2004-7-17)•·HIV-1防止宿主细胞耐受的机理(2004-7-17)•·HIV诱导T细胞凋亡图(2004-7-17)•·血红素的伴侣分子(2004-7-17)•·g-Secretase介导ErbB4信号通路(2004-7-17)•·生物激素信号(2004-7-17)•·Granzyme A介导的凋亡信号通路(2004-7-17)•·G蛋白偶联信号需要Tubby支持(2004-7-17)•·糖酵解通路(2004-7-17)•·Ghrelin：食物吸收和能量平衡的调控者(2004-7-17)•·PS1能产生beta淀粉样蛋白导致老年性痴呆(2004-7-17)•·GATA3部分参与TH2细胞因子基因的表达(2004-7-17)•·GABA受体的代谢图(2004-7-17)•·FXR和LXR调节胆固醇代谢(2004-7-17)•·SLRP在骨骼中的作用(2004-7-17)•·自由基诱导细胞凋亡信号(2004-7-17)•·FOSB与药物成瘾(2004-7-17)•·fMLP诱导趋化因子基因表达(2004-7-17)•·Fibrinolysis通路(2004-7-17)•·糖酵解通路(2004-7-17)•·Fc Epsilon Receptor I信号(2004-7-17)•·FAS信号通路(2004-7-17)•·外源性Prothrombin激活通路(2004-7-17)•·真核细胞蛋白质翻译示意图(2004-7-17)•·雌激素反应蛋白EFP控制乳腺癌细胞的细胞周期(2004-7-17)•·EPO介导神经保护作用与NF-kB相关(2004-7-17)•·Erythrocyte分化通路(2004-7-17)•·Erk1/Erk2 Mapk 信号通路(2004-7-17)•·Erk和PI-3K在细胞外间质中的作用(2004-7-17)•·内质网相关的蛋白质降解通路示意图(2004-7-17)•·EPO售转导机制图(2004-7-17)•·血小板凝聚示意图(2004-7-17)•·NDK动力学(2004-7-17)•·线粒体的电子传递链示意图(2004-7-17)•·Eicosanoid代谢(2004-7-17)•·EGF信号通路(2004-7-17)•·calcineurin对Keratinocyte分化的影响(2004-7-17)•·E2F1信号通路(2004-7-17)•·MTA-3在雌激素不敏感性乳腺癌中下调(2004-7-17)•·双链RNA诱导基因表达示意图(2004-7-17)•·Dicer信号通路（RNAi机理）(2004-7-17)•·CDK5在老年性痴呆中的调节作用(2004-7-17)•·树突状细胞调节TH1和TH2发育示意图(2004-7-17)•·RAR和RXR被蛋白酶体降解通路(2004-7-17)•·D4-GDI信号通路示意图(2004-7-17)•·细胞因子和炎症反应示意图(2004-7-9)•·细胞因子网络调控图(2004-7-9)•·CFTR和beta 2肾上腺素受体通路(2004-7-9)•·Cyclin和细胞周期调控图(2004-7-9)•·Ran核质循环转运图(2004-7-9)•·Cyclin E降解通路图(2004-7-9)•·CXCR4信号通路图(2004-7-9)•·CTL介导的免疫反应图(2004-7-9)•·CTCF：第一个多价核因子(2004-7-9)•·皮质激素和心脏保护(2004-7-9)•·骨骼肌的成肌信号图(2004-7-9)•·VitD调控基因表达信号图(2004-7-9)•·补体信号通路(2004-7-9)•·线粒体和过氧化物酶体中β氧化的比较图(2004-7-9)•·经典的补体信号通路图(2004-7-9)•·心律失常的分子机制图(2004-7-9)•·hSWI/SNF ATP依赖的染色体重塑(2004-7-9)•·碳水化合物和cAMP调节ChREBP图(2004-7-9)•·分子伴侣调节干扰素信号图(2004-7-9)•·Ceramide信号图(2004-7-9)•·局部急性感染的细胞与分子信号(2004-7-9)•·细胞与细胞粘附信号(2004-7-9)•·细胞周期G2/M调控点信号调节(2004-7-9)•·细胞周期 G1/S调控点信号图(2004-7-9)•·CDK调节DNA复制(2004-7-9)•·cdc25和chk1在DNA破坏中的作用图(2004-7-9)•·CD40L信号通路图(2004-7-9)•·CCR3信号图(2004-7-9)•·CBL下调EGF受体的信号转导图(2004-7-9)•·一些氨基酸的代谢通路图 3 (2004-7-9)•·一些氨基酸的代谢通路图 2 (2004-7-9)•·一些氨基酸的代谢通路图(2004-7-9)•·Catabolic pathway for asparagine and asp (2004-7-9)•·Caspase 信号级联通路在细胞凋亡中的作用(2004-7-9)•·CARM1和雌激素的信号转导调控(2004-7-9)•·抗氧自由基的心脏保护作用信号转导图(2004-7-9)•·乙肝病毒中的钙信号调控(2004-7-9)•·镉诱导巨噬细胞的DNA合成和增殖(2004-7-9)•·Ca2+/CaM依赖的激活(2004-7-9)•·B细胞活化机理图(2004-6-9)•·BTG家族蛋白和细胞周期的调节(2004-6-9)•·BRCA1作用机理(2004-6-9)•·骨重塑示意图(2004-6-9)•·Botulinum Toxin阻断神经递质释放示意图(2004-6-9)•·缬氨酸的生物合成图(2004-6-9)•·Tryptophan在植物和细菌内的生物合成(2004-6-9)•·苏氨酸和蛋氨酸的体内合成示意图(2004-6-9)•·sphingolipids生物合成(2004-6-9)•·spermidine和spermine生物合成(2004-6-9)•·细菌体内合成脯氨酸的示意图(2004-6-9)•·苯丙氨酸和酪氨酸的生物合成(2004-6-9)•·神经递质的合成示意图(2004-6-9)•·赖氨酸生物合成图(2004-6-9)•·亮氨酸的体内生物合成图(2004-6-9)•·异亮氨酸的生物合成图(2004-6-9)•·甘氨酸和色氨酸的生物合成(2004-6-9)•·Cysteine在哺乳动物中的合成图(2004-6-9)•·Cysteine在细菌和植物内生物合成图(2004-6-9)•·Chorismate在细菌和植物内的生物合成(2004-6-9)•·Arginine在细菌内的生物合成(2004-6-9)•·生物活性肽诱导的通路(2004-6-9)•·脂肪酸的β氧化通路(2004-6-9)•·BCR信号通路示意图(2004-6-9)•·SUMOylation基本机理(2004-6-9)•·PPAR影响基因表达的基本信号机制图(2004-6-9)•·B淋巴细胞表面分子示意图(2004-6-9)•·B细胞生存信号通路(2004-6-5)•·B细胞信号通路的复杂性(2004-6-5)•·GPCR信号的衰减的机理(2004-6-4)•·ATM信号通路(2004-6-4)•·阿斯匹林的抗凝机理(2004-6-4)•·细胞凋亡信号调节DNA片段化(2004-6-4)•·细胞凋亡DNA片段化与组织稳态的机理(2004-6-4)•·反义核酸的作用机理---RNA polymerase III (2004-6-4)•·抗原递呈与处理信号图(2004-6-4)•·Antigen依赖的B细胞激活(2004-6-4)•·Anthrax Toxin Mechanism of Action (2004-6-4)•·血管紧张素转换酶2调节心脏功能(2004-6-4)•·Angiotensin II 介导JNK信号通路的激活(2004-6-4)•·Alternative Complement Pathway (2004-6-4)•·Alpha-synuclein和Parkin在怕金森病中的作用(2004-6-4)•·ALK在心肌细胞中的功能图(2004-6-4)•·AKT信号通路(2004-6-4)•·AKAP95在有丝分裂中的作用图(2004-6-4)•·Ahr信号转导图(2004-6-4)•·Agrin突触后的功能图(2004-6-4)•·ADP-Ribosylation 因子(2004-6-4)•·淋巴细胞粘附分子信号图(2004-6-4)•·Adhesion and Diapedesis of Lymphocytes (2004-6-4)•·Adhesion and Diapedesis of Granulocytes (2004-6-4)•·急性心肌梗死信号转导图(2004-6-4)•·src蛋白质激活图(2004-6-4)•·PKC与G蛋白耦联受体的关系(2004-6-4)•·cAMP依赖的CSK抑制T细胞功能示意图(2004-6-4)•·PKA功能示意图(2004-6-4)•·一氧化氮（NO）在心脏中的功能示意图(2004-6-4)•·RelA 在细胞核内乙酰化和去乙酰化(2004-6-4)actin肌丝Mammalian cell motility requires actin polymerization in the direction of movement to change membrane shape and extend cytoplasm into lamellipodia. The polymerization of actin to drive cell movement also involves branching of actin filaments into a network oriented with the growing ends of the fibers near the cell membrane. Manipulation of this process helps bacteria like Salmonella gain entry into cells they infect. Two of the proteins involved in the formation of Y branches and in cell motility are Arp2 and Arp3, both members of a large multiprotein complex containing several other polypeptides as well. The Arp2/3 complex is localized at the Y branch junction and induces actin polymerization. Activity of this complex is regulated by multiple different cell surface receptor signaling systems, activating WASP, and Arp2/3 in turn to cause changes in cell shape and cell motility. Wasp and its cousin Wave-1 interact with the Arp2/3 complex through the p21 component of the complex. The crystal structure of the Arp2/3 complex has revealed further insights into the nature of how the complex works.Activation by Wave-1, another member of the WASP family, also induces actin alterations in response to Rac1 signals upstream. Wave-1 is held in an inactive complex in the cytosol that is activated to allow Wave-1 to associate with Arp2/3. While WASP is activated by interaction with Cdc42, Wave-1, is activated by interaction with Rac1 and Nck. Wave-1 activation by Rac1 and Nck releases Wave-1 with Hspc300 to activate actin Y branching and polymerization by Arp2/3. Different members of this gene family may produce different actin cytoskeletal architectures. The immunological defects associated with mutation of the WASP gene, theWiskott-Aldrich syndrome for which WASP was named, indicates the importance of this system for normal cellular function.Cory GO, Ridley AJ. Cell motility: braking WAVEs. Nature. 2002 Aug 15;418(6899):732-3. No abstract available.Eden, S., et al. (2002) Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418(6899), 790-3Falet H, Hoffmeister KM, Neujahr R, Hartwig JH. Normal Arp2/3 complex activation in platelets lacking WASp. Blood. 2002 Sep 15;100(6):2113-22.Kreishman-Deitrick M, Rosen MK, Kreishman-Deltrick M. Ignition of a cellular machine. Nat Cell Biol. 2002 Feb;4(2):E31-3. No abstract available.Machesky, L.M., Insall, R.H. (1998) Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr Biol 8(25), 1347-56Robinson, R.C. et al. (2001) Crystal structure of Arp2/3 complex. Science 294(5547), 1679-84Weeds A, Yeoh S. Structure. Action at the Y-branch. Science. 2001 Nov 23;294(5547):1660-1. No abstract available.Wnt/LRP6 信号Wnt glycoproteins play a role in diverse processes during embryonic patterning in metazoa through interaction with frizzled-type seven-transmembrane-domain receptors (Frz) to stabilize b-catenin. LDL-receptor-related protein 6 (LRP6), a Wnt co-receptor, is required for this interaction. Dikkopf (dkk) proteins are both positive and negative modulators of this signalingWNT信号转导West Nile 西尼罗河病毒West Nile virus (WNV) is a member of the Flaviviridae, a plus-stranded virus family that includes St. Louis encephalitis virus, Kunjin virus, yellow fever virus, Dengue virus, and Japanese encephalitis virus. WNV was initially isolated in 1937 in the West Nile region of Uganda and has become prevalent in Africa, Asia, and Europe. WNV has rapidly spread across the United States through its insect host and causes neurological symptoms and encephalitis, which can result in paralysis or death. Since 1999 about 3700 cases of West Nile virus (WNV) infection and 200 deaths have been recorded in United States. The viral capsid protein likely contributes to the WNV-associated deadly inflammation via apoptosis induced through the mitochondrial pathway.WNV particles (50 nm in diameter) consist of a dense core (viral protein C encapsidated virus RNA genome)surrounded by a membrane envelope (viral E and M proteins embedded in a lipid bilayer). The virus binds to a specific cell surface protein (not yet identified), an interaction thought to involve E protein with highly sulfated neperan sulfate (HSHS) residues that are present on the surfaces of many cells and enters the cell by a process similar to that of endocytosis. Once inside the cell, the genome RNA is released into the cytoplasm via endosomal release, a fusion process involving acidic pH induced conformation change in the E protein. The RNA genome serves as mRNA and is translated by ribosomes into ten mature viral proteins are produced via proteolytic cleavage, which include three structural components and seven different nonstructural components of the virus. These proteins assemble and transcribe complimentary minus strand RNAs from the genomic RNA. The complimentary minus strand RNA in turns serves as template for the synthesis of positive-stranded genomic RNAs. Once viral E, preM and C proteins have accumulated to sufficient level, they assemble with the genomic RNA to form progeny virions, which migrate to the cell surface where they are surrounded with lipid envelop and released.Vitamin C 维生素C在大脑中的作用Vitamin C (ascorbic acid) was first identified by virtue of the essential role it plays in collagen modification, preventing the nutritional deficiency scurvy. Vitamin C acts as a cofactor for hydroxylase enzymes thatpost-translationally modify collagen to increase the strength and elasticity of tissues. Vitamin C reduces the metal ion prosthetic groups of many enzymes, maintaining activity of enzymes, also acts as an anti-oxidant. Although the prevention of scurvy through modification of collagen may be the most obvious role for vitamin C, it is not necessarily the only role of vitamin C. Svct1 and Svct2 are ascorbate transporters for vitamin C import into tissues and into cells. Both of these transporters specifically transport reduced L-ascorbic acid against a concentration gradient using the intracellular sodium gradient to drive ascorbate transport. Svct1 is expressed in epithelial cells in the intestine, upregulated in cellular models for intestinal epithelium and appears to be responsible for the import of dietary vitamin C from the intestinal lumen. The vitamin C imported from the intestine is present in plasma at approximately 50 uM, almost exclusively in the reduced form, and is transported to tissues to play a variety of roles. Svct2 imports reduced ascorbate from the plasma into veryactive tissues like the brain. Deletion in mice of the gene for Svct2 revealed that ascorbate is required for normal development of the lungs and brain during pregnancy. A high concentration of vitamin C in neurons of the developing brain may help protect the developing brain from free radical damage. The oxidized form of ascorbate, dehydroascorbic acid, is transported into a variety of cells by the glucose transporter Glut-1. Glut-1, Glut-3 and Glut-4 can transport dehydroascorbate, but may not transport significant quantities of ascorbic acid in vivo.视觉信号转导信息来源：本站原创生物谷网站The signal transduction cascade responsible for sensing light in vertebrates is one of the best studied signal transduction processes, and is initiated by rhodopsin in rod cells, a member of the G-protein coupled receptor gene family. Rhodopsin remains the only GPCR whose structure has been resolved at high resolution. Rhodopsinin the discs of rod cells contains a bound 11-cis retinal chromophore, a small molecule derived from Vitamin A that acts as the light sensitive portion of the receptor molecule, absorbing light to initiate the signal transduction cascade. When light strikes 11-cis retinal and is absorbed, it isomerizes to all-trans retinal, changing the shape of the molecule and the receptor it is bound to. This change in rhodopsin抯shape alters its interaction with transducin, the member of the G-protein gene family that is specific in its role in visual signal transduction. Activation of transducin causes its alpha subunit to dissociate from the trimer and exchange bound GDP for GTP, activating in turn a membrane-bound cyclic-GMP specific phosphodiesterase that hydrolyzes cGMP. In the resting rod cell, high levels of cGMP associate with a cyclic-GMP gated sodium channel in the plasma membrane, keeping the channels open and the membrane of the resting rod cells depolarized. This is distinct from synaptic generation of action potentials, in which stimulation induces opening of sodium channels and depolarization. When cGMP gated channels in rod cells open, both sodium and calcium ions enter the cell, hyperpolarizing the membrane and initiating the electrochemical impulse responsible for conveying the signal from the sensory neuron to the CNS. The rod cell in the resting state releases high levels of the inhibitory neurotransmitter glutamate, while the release of glutamate is repressed by the hyperpolarization in the presence of light to trigger a downstream action potential by ganglion cells that convey signals to the brain. The calcium which enters the cell also activates GCAP, which activates guanylate cyclase (GC-1 and GC-2) to rapidly produce more cGMP, ending the hyperpolarization and returning the cell to its resting depolarized state. A protein called recoverin helps mediate the inactivation of the signal transduction cascade, returning rhodopsin to its preactivated state, along with the rhodopsin kinase Grk1. Phosphorylation of rhodopsin by Grkl causes arrestin to bind, helping to terminate the receptor activation signal. Dissociation and reassociation of retinal, dephosphorylation of rhodopsin and release of arrestin all return rhodopsin to its ready state, prepared once again to respond to light.VEGF，低氧信息来源：本站原创生物谷网站Vascular endothelial growth factor (VEGF) plays a key role in physiological blood vessel formation and pathological angiogenesis such as tumor growth and ischemic diseases. Hypoxia is a potent inducer of VEGF in vitro. The increase in secreted biologically active VEGF protein from cells exposed to hypoxia is partly because of an increased transcription rate, mediated by binding of hypoxia-inducible factor-1 (HIF1) to a hypoxia responsive element in the 5'-flanking region of the VEGF gene. bHLH-PAS transcription factor that interacts with the Ah receptor nuclear translocator (Arnt), and its predicted amino acid sequence exhibits significant similarity to the hypoxia-inducible factor 1alpha (HIF1a) product. HLF mRNA expression is closely correlated with that of VEGF mRNA.. The high expression level of HLF mRNA in the O2 delivery system of developing embryos and adult organs suggests that in a normoxic state, HLF regulates gene expression of VEGF, various glycolytic enzymes, and others driven by the HRE sequence, and may be involved in development of blood vessels and the tubularsystem of lung. VEGF expression is dramatically induced by hypoxia due in large part to an increase in the stability of its mRNA. HuR binds with high affinity and specificity to the VRS element that regulates VEGF mRNA stability by hypoxia. In addition, an internal ribosome entry site (IRES) ensures efficient translation of VEGF mRNA even under hypoxia. The VHL tumor suppressor (von Hippel-Lindau) regulates also VEGF expression at a post-transcriptional level. The secreted VEGF is a major angiogenic factor that regulates multiple endothelial cell functions, including mitogenesis. Cellular and circulating levels of VEGF are elevated in hematologic malignancies and are adversely associated with prognosis. Angiogenesis is a very complex, tightly regulated, multistep process, the targeting of which may well prove useful in the creation of novel therapeutic agents. Current approaches being investigated include the inhibition of angiogenesis stimulants (e.g., VEGF), or their receptors, blockade of endothelial cell activation, inhibition of matrix metalloproteinases, and inhibition of tumor vasculature. Preclinical, phase I, and phase II studies of both monoclonal antibodies to VEGF and blockers of the VEGF receptor tyrosine kinase pathway indicate that these agents are safe and offer potential clinical utility in patients with hematologic malignancies.TSP-1诱导细胞凋亡信息来源：本站原创生物谷网站As tissues grow they require angiogenesis to occur if they are to be supplied with blood vessels and survive. Factors that inhibit angiogenesis might act as cancer therapeutics by blocking vessel formation in tumors and starving cancer cells. Thrombospondin-1 (TSP-1) is a protein that inhibits angiogenesis and slows tumor growth, apparently by inducing apoptosis of microvascular endothelial cells that line blood vessels. TSP-1 appears to produce this response by activating a signaling pathway that begins with its receptor CD36 at the cell surface of the microvascular endothelial cell. The non-receptor tyrosine kinase fyn is activated by TSP-1 through CD36, activating the apoptosis inducing proteases like caspase-3 and p38 protein kinases. p38 is a mitogen-activated kinase that also induces apoptosis in some conditions, perhaps through AP-1 activation and the activation of genes that lead to apoptosis.Trka信号转导信息来源：本站原创生物谷网站Nerve growth factor (NGF) is a neurotrophic factor that stimulates neuronal survival and growth through TrkA, a member of the trk family of tyrosine kinase receptors that also includes TrkB and TrkC. Some NGF responses are also mediated or modified by p75LNTR, a low affinity neurotrophin receptor. Binding of NGF to TrkA stimulates neuronal survival, and also proliferation. Pathways coupled to these responses are linked to TrkAthrough association of signaling factors with specific amino acids in the TrkA cytoplasmic domain. Cell survival through inhibition of apoptosis is signaled through activation of PI3-kinase and AKT. Ras-mediated signaling and phospholipase C both activate the MAP kinase pathway to stimulate proliferation.dbpb调节mRNA信息来源：本站原创生物谷网站Endothelial cells respond to treatment with the protease thrombin with increased secretion of the PDGF B-chain. This activation occurs at the transcriptional level and a thrombin response element was identified in the promoter of the PDGF B-chain gene. A transcription factor called the DNA-binding protein B (dbpB) mediates the activation of PDGF B-chain transcription in response to thrombin treatment. DbpB is a member of the Y box family of transcription factors and binds to both RNA and DNA. In the absence of thrombin, endothelial cells contain a 50 kD form of dbpB that binds RNA in the cytoplasm and may play a role as a chaperone for mRNA. The 50 kD version of dbpB also binds DNA to regulate genes containing Y box elements in their promoters. Thrombin activation results in the cleavage of dbpB to a 30 kD form. The proteolytic cleavage releases dbpB from RNA in the nucleus, allowing it to enter the nucleus and binds to a regulatory element distinct from the site recognized by the full length 50 kD dbpB. The genes activated by cleaved dbpB include the PDGF B chain. Dephosphorylation of dbpB also regulates nuclear entry and transcriptional activation.RNA digestion in vitro can release dbpB in its active form, suggesting that the protease responsible for dbpB may be closely associated in a complex. Identification of the protease that cleaves dbpB, the mechanisms of phosphorylation and dephosphorylation, and elucidation of the signaling path by which thrombin induces dbpB will provide greater understanding of this novel signaling pathway.CARM1甲基化信息来源：本站原创生物谷网站Several forms of post-translational modification regulate protein activities. Recently, protein methylation by CARM1 (coactivator-associated arginine methyltransferase 1) has been observed to play a key role in transcriptional regulation. CARM1 associates with the p160 class of transcriptional coactivators involved in gene activation by steroid hormone family receptors. CARM1 also interacts with CBP/p300 transcriptional coactivators involved in gene activation by a large variety of transcription factors, including steroid hormone receptors and CEBP. One target of CARM1 is the core histones H3 and H4, which are also targets of the histone acetylase activity of CBP/p300 coactivators. Recruitment of CARM1 to the promoter region by binding to coactivators increases histone methylation and makes promoter regions more accessible for transcription. Another target of CARM1 methylation is a coactivator it interacts with, CBP. Methylation of CBP by CARM1 blocks。

细胞通讯系统：五大分子信号通路

Wnt受体，其胞外N端具有富含半胱氨酸的结构域，Frz作用于胞质内的蓬乱蛋白（Dsh），Dsh 能切断β-catenin的降解途径，从而使β-catenin在细胞
质中积累，并进入细胞核，与T细胞因子（TCF/LEF）相互作用，调节靶基因的表达。 Hedgehog信号通路 Hedgehog是一种共价结合胆固醇的分泌性蛋
u通过自我磷酸化激活并进而磷酸化其底物Cos2 与Sufu而将Hh信号传递至下游。这一过程将促使全长的转录因子Ci155由Cos2及Sufu动态解离出来并进入细胞
核内启动目的基因的表达。这项研究表明，细胞能够通过动态调节Fu二聚化及其激酶活性而感应不同水平的Hh信号。另外也提示了Hh信号通路成员如何通过磷酸化影响他们的活
的Bouras等科学家发表文章称，他们发现了 Notch信号途径在调控乳房干细胞功能和乳房上皮层级当中所发挥的作用。 Notch是一种跨膜的受体，它们广泛存在于
各种动物细胞中。Notch信号途径对于多种组织和细胞命运非常重要，包括表皮、神经、血液和肌肉等。在本期的封面文章中，研究人员发现，敲除MaSC富集细胞群当中的规
癌细胞中保持高活性的通路。他们还指出，Wnt 信号转导通路与恶性癌症的发生有密切关系 “基因突变激活Wnt信号通路一般会导致结肠癌的发生，肺癌通常是由其他基因变
异引起，所以我们对于Wnt细胞信号转导通路与肺癌有莫大关系也非常惊讶。”论文通讯作者琼马萨格博士表示。[详细] 我国科学家在Hedgehog信号通路传递研究方
向取得新进展 CellResearch在线发表了中科院上海生命科学研究院生化与细胞所赵允和张雷研究组在研究 Hedgehog信号通路传递方面的新进展。通过研究揭
示，Hh浓度梯度信号所引发的Smo磷酸化水平的升高，能够通过Smo与Cos2之间的动态相互作用将Cos2/Fu复合物招募到质膜上，从而诱导Fu 二聚化。二聚化的F

细胞信号通路的理论和应用

细胞信号通路的理论和应用细胞信号通路指的是细胞内外物质之间的信息传递机制。

这些信息可以通过化学物质或者物理信号的形式传递。

这种信号传递过程对于细胞的生理和病理过程起着至关重要的作用。

细胞信号通路的研究是现代生物学重要的研究方向之一。

本文将分别从理论和应用两个方面进行介绍。

一、细胞信号通路的理论1.信号传导的类型细胞信号可以通过细胞内和细胞外的化学物质进行传递。

细胞内信号通路包括直接的细胞膜通道，酶反应，离子通道等；而细胞外信号通路包括激素，神经递质以及生物活性物质等。

这些信号可以通过各种信号途径进行传递，最终作用于细胞内的信号传导途径，进而影响细胞的代谢和功能。

2.信号转导的机制信号转导是信息从细胞膜到细胞核的传递过程。

这个过程中，信号分子在物理上与受体分子进行绑定。

此后，分子会激活一个酶反应阶段，从而引导信号从受体到活化酶的传递。

当信号到达细胞核时，它将影响基因表达和细胞生理过程。

3.信号通路的分类细胞信号通路可以分为两大类：内源性通路和外源性通路。

内源性通路是指细胞内部因子对细胞的影响，包括细胞周期的调控，细胞凋亡和细胞形态的调节等。

而外源性通路则是指从周围环境中引入的化学因子和物理因子，如细胞因子，激素，氧气，光线等。

这些环境因素通过作用于细胞表面的受体激活信号通路，进而影响细胞内的生理过程。

二、细胞信号通路的应用1.肿瘤治疗中的应用细胞信号通路在肿瘤治疗过程中的应用已经得到了长期的研究。

白血病、卵巢癌和肺癌等疾病的治疗中，靶向信号通路的药物已经得到了广泛的应用。

靶向细胞信号通路可以通过抑制细胞生长和凋亡来帮助控制癌细胞的发展。

这种药物可以通过选择性作用于癌细胞的外在和内在的生长和发展因素，从而帮助通过靶向信号通路来攻击癌症细胞。

2.神经退行性疾病的治疗信号通路在神经退行性疾病治疗中也得到了广泛的应用。

在老年痴呆症等疾病的治疗中，对神经信号通路进行靶向治疗可以帮助改善病人的神经系统活动和参数。

细胞信号通路及靶向(一)

细胞信号通路及靶向(一)细胞信号通路及靶向细胞信号通路是指通过化学信号进行细胞内外信息传递的一系列分子机制。

它在生物体内起着重要的调节、控制生理功能的作用。

在疾病的发病机制以及治疗方法中，细胞信号通路的研究变得越来越重要。

一、细胞信号通路种类细胞信号通路可分为内源性通路和外源性通路。

内源性通路主要是由细胞内部的物质和分子机制来控制。

例如，环磷酰胺作为癌症治疗的药物，主要通过在细胞内引起DNA链断裂而阻止肿瘤细胞的增殖。

外源性通路主要是通过外界物质对细胞的影响来实现。

例如，神经递质可与神经元的膜上受体结合，从而引起神经元内的信号传递。

二、细胞信号通路的作用细胞信号通路可控制和调节多种细胞生理过程，包括细胞增殖、分化、凋亡、基因转录、代谢调节等等。

在疾病的发病机制中，细胞信号通路也扮演着重要的角色。

例如，癌症的发生通过细胞信号通路的错乱造成，治疗癌症的方法也多以干涉细胞信号通路为基础。

三、细胞信号通路的靶向细胞信号通路靶向治疗是一种新的癌症治疗方法。

该方法利用分子生物学和细胞信号通路的研究成果，把临床治疗方案调整到分子水平上。

它可靶向治疗癌症细胞的特定信号通路，避免对正常细胞的损害。

目前，靶向治疗还有许多挑战和限制，例如，很难确立各类癌症的分子标志物，故而无法准确把握靶向治疗的有效靶点；靶向治疗抗药性的产生等。

但是，随着科技的发展以及对细胞信号通路机制的深入了解，相信以靶向治疗为基础的细胞信号通路研究会为新一代白血病、乳腺癌、结直肠癌、肺癌治疗带来新的希望。

总之，细胞信号通路是生命体的基础，也是疾病发病机制和治疗方法的关键。

通过深入了解细胞信号通路的各种机制，并以此为基础进行针对性干预治疗，有望为人类的健康带来福音。

细胞信号传导通路

细胞信号传导通路细胞信号传导通路是一种复杂而精确的过程，通过这个过程，细胞能够感知和响应外界环境的变化。

细胞信号传导通路大致可以分为两个主要部分：细胞外信号的感知和细胞内信号的传导。

在细胞外信号感知的过程中，膜上受体将外界信号转化为细胞内信号，然后这些细胞内信号通过一系列的信号传导分子传递到靶分子，最终引发特定的细胞响应。

细胞外信号的感知：细胞外的信号通常是化学物质，例如激素、神经递质或细胞因子等。

当这些信号分子与膜上的受体结合时，激活这些受体，并使其发生构象变化。

这个构象变化将导致受体激活并激发下游的信号传导级联反应。

不同类型的受体有不同的激活机制，例如离子通道受体、酪氨酸激酶受体和G蛋白偶联受体等。

在这个阶段，细胞表面的膜受体起到了非常重要的作用，它们充当了信号分子的接受者，并将外界信号传递到细胞内。

细胞内信号的传导：在受体激活后，细胞内信号传导分子被激活，并通过一系列的反应形成信号传导通路。

这些信号传导分子主要包括蛋白激酶、蛋白磷酸酶和次级信号分子等。

蛋白激酶的活化可以引发一系列的磷酸化级联反应，从而将信号传递到下游的分子。

蛋白磷酸酶可以将磷酸基团从分子上去除，从而停止或逆转反应。

此外，次级信号分子如环磷酸腺苷、二酸磷酸腺苷等也起到了重要的调节作用，它们可以直接或间接地影响其他分子的活性。

信号传导路径的调控：细胞信号传导通路的调控对于维持细胞内稳态和功能正常发挥至关重要。

因此，细胞通过多种机制对信号传导通路进行调控，以确保信号的准确传递，并在必要时进行反馈调节。

这些调控机制包括负反馈回路、交叉激活和信号转导的时空调控等。

负反馈回路可以抑制信号传导级联反应，以维持信号的稳定和防止过度激活。

交叉激活是指不同的信号通路之间相互影响和调节的一种机制，通过这种方式，细胞可以实现复杂的信号调控网络。

信号转导的时空调控指的是细胞通过调节信号传导通路中组分的时空分布来达到合理调控信号传导的目的。

细胞信号传导通路的研究不仅有助于揭示细胞内信号传递的机制，还有助于理解疾病的发生和发展过程。

细胞内信号传导通路

细胞内信号传导通路细胞内信号传导通路是指细胞内外环境信息在细胞内通过一系列分子事件传递的途径。

它是细胞生物学领域的一个重要研究方向，对于理解细胞功能、生理过程以及疾病的发生发展具有重要意义。

本文将对细胞内信号传导通路的基本概念、分类以及在细胞生物学研究中的应用进行探讨。

一、基本概念细胞内信号传导通路是一种细胞内机制，能够将外界刺激转化为细胞内化学变化和生理响应。

细胞内通路的开启和关闭往往伴随着一系列酶的活化或抑制，从而导致蛋白质的磷酸化、变形或降解等。

这些信号被传递到细胞质内，进而影响到细胞的功能和行为。

二、分类根据信号传导的性质和途径，细胞内信号传导通路可分为五大类型：离子通道介导的信号传导、酶促反应、GPCR介导的信号传导、核受体介导的信号传导和细胞附着介导的信号传导。

1.离子通道介导的信号传导细胞膜上的离子通道，如钠离子通道、钾离子通道等，能够让离子迅速通过细胞膜从而改变细胞内电位，传递电化学信号。

2.酶促反应细胞内酶类参与的信号传导通路主要包括磷酸化酶、去磷酸化酶、激酶和磷酸酶等。

这些酶能够催化底物的转化，从而调控细胞内化学反应和代谢过程。

3.GPCR介导的信号传导G蛋白偶联受体（GPCR）是一类重要的细胞表面受体，它们能够与胞内G蛋白结合，调控细胞内二级信号产生，如腺苷酸环化酶、脂酶C、蛋白激酶A等。

4.核受体介导的信号传导核受体介导的信号传导主要指核受体家族，包括雌激素受体、雄激素受体和甲状腺激素受体等，它们能够结合到DNA上，并通过调控转录因子的活性来影响基因的表达，从而调控细胞的生物合成和代谢。

5.细胞附着介导的信号传导细胞附着介导的信号传导通路主要指细胞和细胞外基质之间的相互作用，它能够引发多个信号分子的级联反应，从而影响细胞形态、运动和增殖等。

三、应用细胞内信号传导通路的研究在许多领域都具有重要的应用价值。

在疾病治疗方面，针对信号通路中的关键分子设计和开发特异性抑制剂能够有效地治疗癌症、自身免疫性疾病等疾病。

细胞信号转导通路的不同类型

细胞信号转导通路的不同类型细胞信号转导通路是细胞内的一种复杂的动态过程，它通过传递化学信息，引导细胞作出生理反应。

在细胞内，各种各样的信号通路网络呈现出不同的形态和类型，这些通路的启动和终止都受到多种因素的影响。

下面我们将着重讨论细胞信号转导通路的不同类型。

简单的传递通路简单的传递通路是指信号通路中只有一个中间环节或目标信号分子，例如胰岛素信号。

当胰岛素结合到细胞膜上的胰岛素受体上时，受体活化，使得内部酶被活化，进而催化葡萄糖从血液中转运到细胞内进行利用。

这个通路的转导是相对较简单的，只涉及单个目标分子。

级联式通路级联式通路是最常见的信号转导通路。

它包含多个步骤，每个步骤都需要激活前一步骤的分子以及目标分子。

它的其中一个典型例子就是MAPK通路。

这个通路引导细胞响应各种刺激，如压力、炎症、缺氧等。

当外在信号被检测到时，受体会被激活，将信号传递到一系列下游蛋白中，最后激活细胞核中的转录因子，以产生相应的基因表达。

环形信号转导通路环形信号转导通路是指信号从蛋白质开始，沿着一系列的酶、途径、交换因子再到达相同的蛋白质。

这种环路通路的最公认例子就是G蛋白耦合受体通路。

当足够的荷尔蒙或药物结合到G蛋白偶联受体时，受体激活经过甲状腺素、钙、cAMP (环磷酸腺苷)、PKA等一系列交换因子转化，最终以相同的受体进行转导，反复产生本体差异效应。

核受体信号转导通路核受体信号转导通路是由细胞内的溶质或激素所引发的反应，在这种反应中，受体被激活，进入细胞内，与核受体结合。

这种反应可以引起目标基因的转录，例如睾酮的作用。

睾酮被检测到后，通过激活核受体引发的反应使得蛋白质复合物形成，总体上增加了基因表达水平。

总之，细胞信号传导通路总体上由多种因素的集合影响。

每个信号转导通路都是由一系列复杂的调节机制所组成的。

对不同类型信号转导通路的深入理解有助于设计更好的药物，并广泛应用于医学、农业等领域。

细胞常见信号通路图片合集

目录actin肌丝 (5)Wnt/LRP6 信号 (7)WNT信号转导 (7)West Nile 西尼罗河病毒 (8)Vitamin C 维生素C在大脑中的作用 (10)视觉信号转导 (11)VEGF，低氧 (13)TSP-1诱导细胞凋亡 (15)Trka信号转导 (16)dbpb调节mRNA (17)CARM1甲基化 (19)CREB转录因子 (20)TPO信号通路 (21)Toll-Like 受体 (22)TNFR2 信号通路 (24)TNFR1信号通路 (25)IGF-1受体 (26)TNF/Stress相关信号 (27)共刺激信号 (29)Th1/Th2 细胞分化 (30)TGF beta 信号转导 (32)端粒、端粒酶与衰老 (33)TACI和BCMA调节B细胞免疫 (35)T辅助细胞的表面受体 (36)T细胞受体信号通路 (37)T细胞受体和CD3复合物 (38)Cardiolipin的合成 (40)Synaptic突触连接中的蛋白 (42)HSP在应激中的调节的作用 (43)Stat3 信号通路 (45)SREBP控制脂质合成 (46)酪氨酸激酶的调节 (48)Sonic Hedgehog (SHH)受体ptc1调节细胞周期 (51)Sonic Hedgehog (Shh) 信号 (53)SODD/TNFR1信号 (56)AKT/mTOR在骨骼肌肥大中的作用 (58)G蛋白信号转导 (59)IL1受体信号转导 (60)acetyl从线粒体到胞浆过程 (62)趋化因子chemokine在T细胞极化中的选择性表达 (63)SARS冠状病毒蛋白酶 (65)SARS冠状病毒蛋白酶 (67)Parkin在泛素-蛋白酶体中的作用 (69)nicotinic acetylcholine受体在凋亡中的作用 (71)线粒体在细胞凋亡中的作用 (73)MEF2D在T细胞凋亡中的作用 (74)Erk5和神经元生存 (75)ERBB2信号转导 (77)GPCRs调节EGF受体 (78)BRCA1调节肿瘤敏感性 (79)Rho细胞运动的信号 (81)Leptin能逆转胰岛素抵抗 (82)转录因子DREAM调节疼敏感 (84)PML调节转录 (86)p27调节细胞周期 (88)MAPK信号调节 (89)细胞因子调节造血细胞分化 (91)eIF4e和p70 S6激酶调节 (92)eIF2调节 (93)谷氨酸受体调节ck1/cdk5 (94)BAD磷酸化调节 (95)plk3在细胞周期中的作用 (96)Reelin信号通路 (97)RB肿瘤抑制和DNA破坏 (98)NK细胞介导的细胞毒作用 (99)Ras信号通路 (100)Rac 1细胞运动信号 (101)PTEN依赖的细胞生长抑制和细胞凋亡 (103)蛋白激酶A（PKA）在中心粒中的作用 (104)notch信号通路 (106)蛋白酶体Proteasome复合物 (108)Prion朊病毒的信号通路 (109)早老素Presenilin在notch和wnt信号中的作用 (110)淀粉样蛋白前体信号 (112)mRNA的poly(A)形成 (113)PKC抑制myosin磷酸化 (114)磷脂酶C（PLC）信号 (115)巨噬细胞Pertussis toxin不敏感的CCR5信号通路 (116)Pelp1调节雌激素受体的活性 (117)PDGF信号通路 (118)p53信号通路 (120)p38MAPK信号通路 (121)Nrf2是氧化应激基本表达的关键基因 (122)OX40信号通路 (123)hTert转录因子的调节作用 (124)hTerc转录调节活性图 (125)AIF在细胞凋亡中的作用 (126)Omega氧化通路 (127)核受体在脂质代谢和毒性中的作用 (129)NK细胞中NO2依赖的IL-12信号通路 (131)TOR信号通路 (133)NO信号通路 (134)NF-kB信号转导通路 (135)NFAT与心肌肥厚的示意图 (137)神经营养素及其表面分子 (139)神经肽VIP和PACAP防止活化T细胞凋亡图 (141)神经生长因子信号图 (142)细胞凋亡信号通路 (144)MAPK级联通路 (144)MAPK信号通路图 (145)BCR信号通路 (146)蛋白质乙酰化示意图 (147)wnt信号通路 (148)胰岛素受体信号通路 (149)细胞周期在G2/M期的调控机理图 (151)细胞周期G1/S检查点调控机理图 (152)Jak-STAT关系总表 (153)Jak/STAT 信号 (155)TGFbeta信号 (156)NFkappaB信号 (157)p38 MAPK信号通路 (159)SAPK/JNK 信号级联通路 (160)从G蛋白偶联受体到MAPK (161)MAPK pathwayMAPK级联信号图 (162)eIF-4E和p70 S6激酶调控蛋白质翻译 (163)eif2蛋白质翻译 (164)蛋白质翻译示意图 (165)线粒体凋亡通路 (167)死亡受体信号通路 (168)凋亡抑制通路 (170)细胞凋亡综合示意图 (171)Akt/Pkb信号通路 (172)MAPK/ERK信号通路 (174)哺乳动物MAPK信号通路 (175)Pitx2多步调节基因转录 (176)IGF-1R导致BAD磷酸化的多个凋亡路径 (177)多重耐药因子 (179)mTOR信号通路 (180)Msp/Ron受体信号通路 (181)单核细胞和其表面分子 (182)线粒体的肉毒碱转移酶（CPT）系统 (183)METS影响巨噬细胞的分化 (184)Anandamide，内源性大麻醇的代谢 (186)黑色素细胞（Melanocyte）发育和信号 (187)DNA甲基化导致转录抑制的机理图 (188)蛋白质的核输入信号图 (190)PPARa调节过氧化物酶体的增殖 (192)对乙氨基酚（Acetaminophen）的活性和毒性机理 (194)mCalpain在细胞运动中的作用 (196)MAPK信号图 (198)MAPK抑制SMRT活化 (200)苹果酸和天门冬酸间的转化 (201)低密度脂蛋白（LDL）在动脉粥样硬化中的作用 (202)LIS1基因在神经细胞的发育和迁移中的作用图 (204)Pyk2与Mapk相连的信号通路 (205)galactose代谢通路 (206)Lectin诱导补体的通路 (207)Lck和Fyn在TCR活化中的作用 (208)乳酸合成图 (209)Keratinocyte分化图 (210)离子通道在心血管内皮细胞中的作用 (211)离子通道和佛波脂（Phorbal Esters）信号 (213)内源性Prothrombin激活通路 (214)Ribosome内化通路 (216)整合素（Integrin）信号通路 (217)胰岛素（Insulin）信号通路 (218)Matrix Metalloproteinases (219)组氨酸去乙酰化抑制剂抑制Huntington病 (220)Gleevec诱导细胞增殖 (222)Ras和Rho在细胞周期的G1/S转换中的作用 (224)DR3，4，5受体诱导细胞凋亡 (225)AKT调控Gsk3图 (226)IL-7信号转导 (227)IL22可溶性受体信号转导图 (229)IL-2活化T细胞图 (230)IL12和Stat4依赖的TH1细胞发育信号通路 (232)IL-10信号通路 (233)IL 6信号通路 (234)IL 5信号通路 (236)actin肌丝Mammalian cell motility requires actin polymerization in the direction of movement to change membrane shape and extend cytoplasm into lamellipodia. The polymerization of actin to drive cell movement also involves branching of actin filaments into a network oriented with the growing ends of the fibers near the cell membrane. Manipulation of this process helps bacteria like Salmonella gain entry into cells they infect. Two of the proteins involved in the formation of Y branches and in cell motility are Arp2 and Arp3, both members of a large multiprotein complex containing several other polypeptides as well. The Arp2/3 complex is localized at the Y branch junction and induces actin polymerization. Activity of this complex is regulated by multiple different cell surface receptor signaling systems, activating WASP, and Arp2/3 in turn to cause changes in cell shape and cell motility. Wasp and its cousin Wave-1 interact with the Arp2/3 complex through the p21 component of the complex. The crystal structure of the Arp2/3 complex has revealed further insights into the nature of how the complex works.Activation by Wave-1, another member of the WASP family, also induces actinalterations in response to Rac1 signals upstream. Wave-1 is held in an inactive complex in the cytosol that is activated to allow Wave-1 to associate with Arp2/3. While WASP is activated by interaction with Cdc42, Wave-1, is activated by interaction with Rac1 and Nck. Wave-1 activation by Rac1 and Nck releases Wave-1 with Hspc300 to activate actin Y branching and polymerization by Arp2/3. Different members of this gene family may produce different actin cytoskeletal architectures. The immunological defects associated with mutation of the WASP gene, the Wiskott-Aldrich syndrome for which WASP was named, indicates the importance of this system for normal cellular function.Cory GO, Ridley AJ. Cell motility: braking WAVEs. Nature. 2002 Aug15;418(6899):732-3. No abstract available.Eden, S., et al. (2002) Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418(6899), 790-3Falet H, Hoffmeister KM, Neujahr R, Hartwig JH. Normal Arp2/3 complex activation in platelets lacking WASp. Blood. 2002 Sep 15;100(6):2113-22.Kreishman-Deitrick M, Rosen MK, Kreishman-Deltrick M. Ignition of a cellular machine. Nat Cell Biol. 2002 Feb;4(2):E31-3. No abstract available.Machesky, L.M., Insall, R.H. (1998) Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr Biol 8(25), 1347-56Robinson, R.C. et al. (2001) Crystal structure of Arp2/3 complex. Science 294(5547), 1679-84Weeds A, Yeoh S. Structure. Action at the Y-branch. Science. 2001 Nov23;294(5547):1660-1. No abstract available.Wnt/LRP6 信号Wnt glycoproteins play a role in diverse processes during embryonic patterning in metazoa through interaction with frizzled-type seven-transmembrane-domain receptors (Frz) to stabilize b-catenin. LDL-receptor-related protein 6 (LRP6), a Wnt co-receptor, is required for this interaction. Dikkopf (dkk) proteins are both positive and negative modulators of this signalingWNT信号转导West Nile 西尼罗河病毒West Nile virus (WNV) is a member of the Flaviviridae, a plus-stranded virus family that includes St. Louis encephalitis virus, Kunjin virus, yellow fever virus, Dengue virus, and Japanese encephalitis virus. WNV was initially isolated in 1937 in the West Nile region of Uganda and has become prevalent in Africa, Asia, and Europe. WNV has rapidly spread across the United States through its insect host and causes neurological symptoms and encephalitis, which can result in paralysis or death. Since 1999 about 3700 cases of West Nile virus (WNV) infection and 200 deaths have been recorded in United States. The viral capsid protein likely contributes to theWNV-associated deadly inflammation via apoptosis induced through the mitochondrial pathway.WNV particles (50 nm in diameter) consist of a dense core (viral protein C encapsidated virus RNA genome) surrounded by a membrane envelope (viral E and M proteins embedded in a lipid bilayer). The virus binds to a specific cell surface protein (not yet identified), an interaction thought to involve E protein with highly sulfated neperan sulfate (HSHS) residues that are present on the surfaces of many cells and enters the cell by a process similar to that of endocytosis. Once inside the cell, the genome RNA is released into the cytoplasm via endosomal release, a fusion process involving acidic pH induced conformation change in the E protein. The RNA genome serves as mRNA and is translated by ribosomes into ten mature viral proteins are produced via proteolytic cleavage, which include three structural components and seven different nonstructural components of the virus. These proteins assemble and transcribe complimentary minus strand RNAs from the genomic RNA. The complimentary minus strand RNA in turns serves as template for the synthesis of positive-stranded genomic RNAs. Once viral E, preM and C proteins have accumulated to sufficient level, they assemble with the genomic RNA to form progeny virions, which migrate to the cell surface where they are surrounded with lipid envelop and released.Vitamin C 维生素C在大脑中的作用Vitamin C (ascorbic acid) was first identified by virtue of the essential role it plays in collagen modification, preventing the nutritional deficiency scurvy. Vitamin C acts as a cofactor for hydroxylase enzymes that post-translationally modify collagen to increase the strength and elasticity of tissues. Vitamin C reduces the metal ion prosthetic groups of many enzymes, maintaining activity of enzymes, also acts as an anti-oxidant. Although the prevention of scurvy through modification of collagen may be the most obvious role for vitamin C, it is not necessarily the only role of vitamin C. Svct1 and Svct2 are ascorbate transporters for vitamin C import into tissues and into cells. Both of these transporters specifically transport reduced L-ascorbic acid against a concentration gradient using the intracellular sodium gradient to drive ascorbate transport. Svct1 is expressed in epithelial cells in the intestine, upregulated in cellular models for intestinal epithelium and appears to be responsible for the import ofdietary vitamin C from the intestinal lumen. The vitamin C imported from the intestine is present in plasma at approximately 50 uM, almost exclusively in the reduced form, and is transported to tissues to play a variety of roles. Svct2 imports reduced ascorbate from the plasma into very active tissues like the brain. Deletion in mice of the gene for Svct2 revealed that ascorbate is required for normal development of the lungs and brain during pregnancy. A high concentration of vitamin C in neurons of the developing brain may help protect the developing brain from free radical damage. The oxidized form of ascorbate, dehydroascorbic acid, is transported into a variety of cells by the glucose transporter Glut-1. Glut-1, Glut-3 and Glut-4 can transport dehydroascorbate, but may not transport significant quantities of ascorbic acid in vivo.视觉信号转导The signal transduction cascade responsible for sensing light in vertebrates is one of the best studied signal transduction processes, and is initiated by rhodopsin in rodcells, a member of the G-protein coupled receptor gene family. Rhodopsin remains the only GPCR whose structure has been resolved at high resolution. Rhodopsin in the discs of rod cells contains a bound 11-cis retinal chromophore, a small molecule derived from Vitamin A that acts as the light sensitive portion of the receptor molecule, absorbing light to initiate the signal transduction cascade. When light strikes 11-cis retinal and is absorbed, it isomerizes to all-trans retinal, changing the shape of the molecule and the receptor it is bound to. This change in rhodopsin抯shape alters its interaction with transducin, the member of the G-protein gene family that is specific in its role in visual signal transduction. Activation of transducin causes its alpha subunit to dissociate from the trimer and exchange bound GDP for GTP, activating in turn a membrane-bound cyclic-GMP specific phosphodiesterase that hydrolyzes cGMP. In the resting rod cell, high levels of cGMP associate with a cyclic-GMP gated sodium channel in the plasma membrane, keeping the channels open and the membrane of the resting rod cells depolarized. This is distinct from synaptic generation of action potentials, in which stimulation induces opening of sodium channels and depolarization. When cGMP gated channels in rod cells open, both sodium and calcium ions enter the cell, hyperpolarizing the membrane and initiating the electrochemical impulse responsible for conveying the signal from the sensory neuron to the CNS. The rod cell in the resting state releases high levels of the inhibitory neurotransmitter glutamate, while the release of glutamate is repressed by the hyperpolarization in the presence of light to trigger a downstream action potential by ganglion cells that convey signals to the brain. The calcium which enters the cell also activates GCAP, which activates guanylate cyclase (GC-1 and GC-2) to rapidly produce more cGMP, ending the hyperpolarization and returning the cell to its resting depolarized state. A protein called recoverin helps mediate the inactivation of the signal transduction cascade, returning rhodopsin to its preactivated state, along with the rhodopsin kinase Grk1. Phosphorylation of rhodopsin by Grkl causes arrestin to bind, helping to terminate the receptor activation signal. Dissociation and reassociation of retinal, dephosphorylation of rhodopsin and release of arrestin all return rhodopsin to its ready state, prepared once again to respond to light.VEGF，低氧Vascular endothelial growth factor (VEGF) plays a key role in physiological blood vessel formation and pathological angiogenesis such as tumor growth and ischemic diseases. Hypoxia is a potent inducer of VEGF in vitro. The increase in secreted biologically active VEGF protein from cells exposed to hypoxia is partly because of an increased transcription rate, mediated by binding of hypoxia-inducible factor-1 (HIF1) to a hypoxia responsive element in the 5'-flanking region of the VEGF gene. bHLH-PAS transcription factor that interacts with the Ah receptor nuclear translocator (Arnt), and its predicted amino acid sequence exhibits significantsimilarity to the hypoxia-inducible factor 1alpha (HIF1a) product. HLF mRNA expression is closely correlated with that of VEGF mRNA.. The high expression level of HLF mRNA in the O2 delivery system of developing embryos and adult organs suggests that in a normoxic state, HLF regulates gene expression of VEGF, various glycolytic enzymes, and others driven by the HRE sequence, and may be involved in development of blood vessels and the tubular system of lung. VEGF expression is dramatically induced by hypoxia due in large part to an increase in the stability of its mRNA. HuR binds with high affinity and specificity to the VRS element that regulates VEGF mRNA stability by hypoxia. In addition, an internal ribosome entry site (IRES) ensures efficient translation of VEGF mRNA even under hypoxia. The VHL tumor suppressor (von Hippel-Lindau) regulates also VEGF expression at a post-transcriptional level. The secreted VEGF is a major angiogenic factor that regulates multiple endothelial cell functions, including mitogenesis. Cellular and circulating levels of VEGF are elevated in hematologic malignancies and are adversely associated with prognosis. Angiogenesis is a very complex, tightly regulated, multistep process, the targeting of which may well prove useful in the creation of novel therapeutic agents. Current approaches being investigated include the inhibition of angiogenesis stimulants (e.g., VEGF), or their receptors, blockade of endothelial cell activation, inhibition of matrix metalloproteinases, and inhibition of tumor vasculature. Preclinical, phase I, and phase II studies of both monoclonal antibodies to VEGF and blockers of the VEGF receptor tyrosine kinase pathway indicate that these agents are safe and offer potential clinical utility in patients with hematologic malignancies.TSP-1诱导细胞凋亡As tissues grow they require angiogenesis to occur if they are to be supplied with blood vessels and survive. Factors that inhibit angiogenesis might act as cancer therapeutics by blocking vessel formation in tumors and starving cancer cells. Thrombospondin-1 (TSP-1) is a protein that inhibits angiogenesis and slows tumor growth, apparently by inducing apoptosis of microvascular endothelial cells that line blood vessels. TSP-1 appears to produce this response by activating a signaling pathway that begins with its receptor CD36 at the cell surface of the microvascular endothelial cell. The non-receptor tyrosine kinase fyn is activated by TSP-1 through CD36, activating the apoptosis inducing proteases like caspase-3 and p38 protein kinases. p38 is a mitogen-activated kinase that also induces apoptosis in some conditions, perhaps through AP-1 activation and the activation of genes that lead to apoptosis.Trka信号转导Nerve growth factor (NGF) is a neurotrophic factor that stimulates neuronal survival and growth through TrkA, a member of the trk family of tyrosine kinase receptors that also includes TrkB and TrkC. Some NGF responses are also mediated or modified by p75LNTR, a low affinity neurotrophin receptor. Binding of NGF to TrkA stimulates neuronal survival, and also proliferation. Pathways coupled to these responses are linked to TrkA through association of signaling factors with specific amino acids in the TrkA cytoplasmic domain. Cell survival through inhibition of apoptosis is signaled through activation of PI3-kinase and AKT. Ras-mediated signaling and phospholipase C both activate the MAP kinase pathway to stimulate proliferation.dbpb调节mRNAEndothelial cells respond to treatment with the protease thrombin with increased secretion of the PDGF B-chain. This activation occurs at the transcriptional level and a thrombin response element was identified in the promoter of the PDGF B-chain gene. A transcription factor called the DNA-binding protein B (dbpB) mediates the activation of PDGF B-chain transcription in response to thrombin treatment. DbpB is a member of the Y box family of transcription factors and binds to both RNA and DNA. In the absence of thrombin, endothelial cells contain a 50 kD form of dbpB that binds RNA in the cytoplasm and may play a role as a chaperone for mRNA. The 50 kD version of dbpB also binds DNA to regulate genes containing Y box elements in their promoters. Thrombin activation results in the cleavage of dbpB to a 30 kD form. The proteolytic cleavage releases dbpB from RNA in the nucleus, allowing it to enter the nucleus and binds to a regulatory element distinct from the site recognized by the full length 50 kD dbpB. The genes activated by cleaved dbpB include the PDGF B chain. Dephosphorylation of dbpB also regulates nuclear entry and transcriptional activation.RNA digestion in vitro can release dbpB in its active form, suggesting that the protease responsible for dbpB may be closely associated in a complex. Identification of the protease that cleaves dbpB, the mechanisms of phosphorylation and dephosphorylation, and elucidation of the signaling path by which thrombin induces dbpB will provide greater understanding of this novel signaling pathway.CARM1甲基化Several forms of post-translational modification regulate protein activities. Recently, protein methylation by CARM1 (coactivator-associated arginine methyltransferase 1) has been observed to play a key role in transcriptional regulation. CARM1 associates with the p160 class of transcriptional coactivators involved in gene activation by steroid hormone family receptors. CARM1 also interacts with CBP/p300 transcriptional coactivators involved in gene activation by a large variety of transcription factors, including steroid hormone receptors and CEBP. One target of CARM1 is the core histones H3 and H4, which are also targets of the histone acetylase activity of CBP/p300 coactivators. Recruitment of CARM1 to the promoter region by binding to coactivators increases histone methylation and makes promoter regions more accessible for transcription. Another target of CARM1 methylation is a coactivator it interacts with, CBP. Methylation of CBP by CARM1 blocks CBP from acting as a coactivator for CREB and redirects the limited CBP pool in the cell to be available for steroid hormone receptors. Other forms of post-translational protein modification such as phosphorylation are reversible in nature, but as of yet a protein demethylase is not known.CREB转录因子The transcription factor CREB binds the cyclic AMP response element (CRE) and activates transcription in response to a variety of extracellular signals including neurotransmitters, hormones, membrane depolarization, and growth and neurotrophic factors. Protein kinase A and the calmodulin-dependent protein kinases CaMKII stimulate CREB phosphorylation at Ser133, a key regulatory site controlling transcriptional activity. Growth and neurotrophic factors also stimulate CREB phosphorylation at Ser133. Phosphorylation occurs at Ser133 via p44/42 MAP Kinase and p90RSK and also via p38 MAP Kinase and MSK1. CREB exhibit deficiencies in spatial learning tasks, while flies overexpressing or lacking CREB show enhanced or diminished learning, respectively.TPO信号通路Thrombopoietin (TPO) binds to its receptor inducing aggregation and activation. TPO signals its growth regulating effects to the cell through several major pathways including MAPK (ERK and JNK), Protein Kinase C, and JAK/Stat.Toll-Like 受体The innate immune response responds in a general manner to factors present in invading pathogens. Bacterial factors such as lipopolysaccharides (LPS, endotoxin), bacterial lipoproteins, peptidoglycans and also CpG nucleic acids activate innate immunity as well as stimulating the antigen-specific immune response and triggering the inflammatory response. Members of the toll-like receptor (TLR) gene family convey signals stimulated by these factors, activating signal transduction pathways that result in transcriptional regulation and stimulate immune function. TLR2 is activated by bacterial lipoproteins, TLR4 is activated by LPS, and TLR9 is activated by CpG DNA; peptidoglycan recognition protein (PGRP) is activated bypeptidoglycan (PGN). The downstream signaling pathways used by these receptors are similar to that used by the IL-1 receptor, activating the IL-1 receptor associated kinase (IRAK) through the MyD88 adaptor protein, and signaling through TRAF-6 and protein kinase cascades to activate NF-kB and Jun. NF-kB and c-Jun activate transcription of genes such as the proinflammatory cytokines IL-1 and IL-12. Several recent reports have suggested that the functional outcomes of signaling via TLR2, TLR4 and PGRP are not equivalent. For example, while the LPS-induced,p38-dependent response was dependent upon PU.1 binding, the PGN-induced, p38 response was not. The intracelular receptor for PGN, PGRP is conserved from insects to mammals. In insects, PGRP activates prophenoloxidase cascade, a part of the insect antimicrobial defense system. Because mammals do not have the prophenoloxidase cascade, its function in mammals is unknown. However, it was suggested that an identical protein Tag7 was a tumor necrosis factor-like (TNF-like) cytokine.PGRP/Tag7 possesses cytotoxicity and triggers intranucleosomal DNA fragmentation in target cells in the same way as many known members of the TNF family. Fragmentation of DNA is one of the characteristics of apoptosis. The possibility that in another system, PGRP/Tag7 would induce NF-kB activation, as observed for TRAIL (TNF-related apoptosis-inducing ligand) receptors canot be ruled out.TNFR2 is the receptor for the 171 amino acid 19 kD TNF(beta) (a.k.a. lymphotoxin). TNF(beta) is produced by activated lymphocytes and can be cytotoxic to many tumor and other cells. In neutrophils, endothelial cells and osteoclasts TNF(beta) can lead to activation while in many other cell types it can lead to increased expression of MHC and adhesion molecules.TNFR1 (a.k.a. p55, CD120a) is the receptor for TNF(alpha) and also will bind TNF(beta). Upon binding TNF(alpha) a TNFR1+ cell is triggered to undergo apoptosis. This critical regulatory process is accomplished by activating the proteolytic caspase cascade that results in the degradation of many critical cellular proteinsIGF-1受体TNF/Stress相关信号TNF acts on several different signaling pathways through two cell surface receptors, TNFR1 and TNFR2 (See TNFR1 and TNFR2 Signaling Pathways) to regulate apoptotic pathways, NF-kB activation of inflammation, and activate stress-activated protein kinases (SAPKs). Interaction of TNFR1 with TRADD leads to activation of NF-kB and apoptosis pathways, while interaction with TRAF2 has generally been thought to be involved in stress kinase and NF-kB activation but is not required for TNF to induce apoptosis. Activation of NF-kB is mediated by TRAF2 through the NIK kinase and also by RIP but the observation that TNF activates NF-kB in mice lacking TRAF2 indicates that TRAF-2 does not play an essential role in this process. Stress-activated protein kinases, also called JNKs, are a family of map kinases activated by cellular stress and inflammatory signals. Binding of TNF to the TNFR1 receptor activates the germinal center kinase (GCK) through the TNF adaptor Traf2, activating the map kinase MEKK1. Both GCK and MEKK1 interact with Traf2, andGCK is required for MEKK1 activation by TNF, but GCK kinase activity does not appear to be required for MEKK1 activation. Instead, GCK activates MEKK1 by causing MEKK1 oligomerization and autophosphorylation. Tank increases the affinity of Traf2 for GCK to increase Map kinase activation by TNF. Once activated, MEKK1 stands at the top of a map kinase pathways leading to transcriptional regulation, including JNK phosphorylation of c-Jun to stimulate transcriptional activation by AP-1, a heterodimer of c-jun and fos or ATF proteins. The activation of the p38 Map kinase also contributes to AP-1 activation leading to the transcriptional activation of many stress and growth related genes. RIP has been suggested as a component of the p38 pathway in addition to playing a role in NF-kB activation. MEKK1 knockout mice support the role of MEKK1 in JNK activation in some cells but did not support MEKK1 dependent activation of NF-kB. Alternative redundant mechanisms may obscure the role of MEKK1 in NF-kB mechanisms. TNF activation of stress kinase pathways and downstream transcription factors may help to modulate the apoptotic pathways also activated by TNF.共刺激信号For a T cell to be activated by a specific antigen, the T cell receptor must recognize complexes of MHCI with the antigen on the surface of an antigen-presenting cell. T cells and the T cell receptor complex do not respond to antigen in solution, but even for the specific antigen they only respond to antigen-MHC-1 complexes on the cell surface. This interaction is necessary for T cell activation, but it is not sufficient. T cell activation also requires a co-stimulatory signal involving interaction of CD28 on the T cell with CD80 or CD86 (B7 family genes) on the antigen-presenting cell.CD28 activates a signal transduction pathway acting through PI-3K, Lck andGrb-2/ITK to provide its co-stimulatory signal for T cell activation. Another means to control T cell activation is by expressing factors that down-regulate T cell activation. Signaling by activated T cell receptors induces expression of CTLA-4, a receptor that opposes T cell activation. CTLA-4 has a higher affinity than CD28 for B7 proteins, terminating T cell activation. ICOS is a protein related to CD28 that is only expressed on activated T cells, and that provides another important co-stimulatory signal. The requirement for co-stimulatory signals provides additional control mechanisms that prevent inappropriate and hazardous T cell activation.。

细胞信号通路

细胞信号通路细胞信号通路是指细胞内外环境改变时，细胞内部如何接收、转导和响应这些信号的一系列生化反应和调节机制。

细胞信号通路在维持细胞生命活动、发育和繁殖过程中起着至关重要的作用。

对于人类健康和疾病的研究，细胞信号通路也具有重要的理论和实践意义。

简介细胞信号通路是由一系列分子相互作用和信号传递构成的复杂网络。

这些分子包括受体、信号分子、信号转导蛋白和效应蛋白等。

细胞信号通路的重要组成部分为受体与配体相互作用，激活信号分子，最终调控细胞生物学效应。

信号通路类型细胞信号通路可以分为内源性和外源性信号通路。

内源性信号通路是指细胞通过与邻近细胞进行直接或间接的相互作用来传递信号。

而外源性信号通路是指细胞通过与外界分子或细胞进行相互作用来传递信号。

细胞信号通路的传递方式有多种，其中常见的包括激酶信号通路、G蛋白偶联受体信号通路和核内受体信号通路等。

这些信号通路可以独立工作，也可以相互配合，形成复杂的信号调控网络。

酶信号通路酶信号通路是细胞内最常见的信号传导机制之一。

主要通过激酶-底物反应来完成信号传递。

当外界信号分子与受体结合后，受体会激活下游酶，进而磷酸化下游底物分子。

磷酸化可以改变底物分子的结构和功能，从而调控细胞的生物学效应。

酶信号通路的代表性例子包括了丝裂原活化激酶（MAPK）信号通路。

这个信号通路在调控细胞的分裂、增殖和生长等生物学过程中起着重要作用。

MAPK信号通路可以通过多个中间分子的级联反应来传递信号，形成一个复杂的调控网络。

G蛋白偶联受体信号通路G蛋白偶联受体（GPCR）信号通路是另外一种常见的信号传导机制。

GPCR是一类在细胞膜上表达的受体，通过与G蛋白相互作用来传递信号。

当外界信号分子结合到GPCR上时，GPCR会与G蛋白结合，并激活G蛋白。

激活的G蛋白能够改变细胞内二信使的水平，如环磷酸腺苷（cAMP）和胞内钙离子等。

这些二信使能够进一步调控多种酶的活性和细胞内各种功能。

核内受体信号通路核内受体信号通路是一种与核内受体相互作用的信号传导机制。

细胞信号通路大全

细胞信号通路大全

细胞信号通路大全

细胞信号通路大全

细胞信号通路

细胞信号通路大全

专题二 常见的细胞信号转导通路

细胞信号通路大全

细胞信号通路大全.pdf

细胞常见信号通路图片合集

细胞通讯系统：五大分子信号通路

细胞信号通路的理论和应用

细胞信号通路及靶向(一)

细胞信号传导通路

细胞内信号传导通路

细胞信号转导通路的不同类型

细胞常见信号通路图片合集

细胞信号通路

专题二常见的细胞信号转导通路