- 同
- FLICE
- 同
- FLICE
WordNet
- any of a group of proteases that mediate apoptosis
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/02/13 11:29:12」(JST)
[Wiki en表示]
| Caspase 8, apoptosis-related cysteine peptidase |
PDB rendering based on 1f9e. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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1F9E, 1I4E, 1QDU, 1QTN, 2C2Z, 2FUN, 2K7Z, 2Y1L, 3H11, 3KJN, 3KJQ, 4JJ7
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| Identifiers |
| Symbols |
CASP8; ALPS2B; CAP4; Casp-8; FLICE; MACH; MCH5 |
| External IDs |
OMIM: 601763 MGI: 1261423 HomoloGene: 7657 ChEMBL: 3776 GeneCards: CASP8 Gene |
| EC number |
3.4.22.61 |
| Gene Ontology |
| Molecular function |
• protease binding
• cysteine-type endopeptidase activity
• tumor necrosis factor receptor binding
• protein binding
• cysteine-type peptidase activity
• identical protein binding
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| Cellular component |
• nucleus
• nucleolus
• cytoplasm
• mitochondrion
• mitochondrial outer membrane
• centrosome
• cytosol
• cytoskeleton
• Noc1p-Noc2p complex
• death-inducing signaling complex
• CD95 death-inducing signaling complex
• neuron projection
• cell body
• membrane raft
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| Biological process |
• angiogenesis
• neural tube formation
• toll-like receptor signaling pathway
• MyD88-independent toll-like receptor signaling pathway
• proteolysis
• apoptotic process
• activation of cysteine-type endopeptidase activity involved in apoptotic process
• cellular component disassembly involved in execution phase of apoptosis
• heart development
• response to cold
• virus-host interaction
• macrophage differentiation
• response to cobalt ion
• response to estradiol stimulus
• response to lipopolysaccharide
• toll-like receptor 3 signaling pathway
• toll-like receptor 4 signaling pathway
• response to tumor necrosis factor
• TRIF-dependent toll-like receptor signaling pathway
• nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway
• positive regulation of I-kappaB kinase/NF-kappaB cascade
• negative regulation of I-kappaB kinase/NF-kappaB cascade
• innate immune response
• response to ethanol
• positive regulation of macrophage differentiation
• positive regulation of proteolysis
• response to antibiotic
• protein heterooligomerization
• proteolysis involved in cellular protein catabolic process
• nucleotide-binding oligomerization domain containing signaling pathway
• cellular response to mechanical stimulus
• apoptotic signaling pathway
• extrinsic apoptotic signaling pathway
• intrinsic apoptotic signaling pathway
• activation of cysteine-type endopeptidase activity
• positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
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| Sources: Amigo / QuickGO |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
841 |
12370 |
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| Ensembl |
ENSG00000064012 |
ENSMUSG00000026029 |
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| UniProt |
Q14790 |
O89110 |
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| RefSeq (mRNA) |
NM_001080124 |
NM_001080126 |
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| RefSeq (protein) |
NP_001073593 |
NP_001073595 |
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| Location (UCSC) |
Chr 2:
202.1 – 202.15 Mb |
Chr 1:
58.8 – 58.85 Mb |
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| PubMed search |
[1] |
[2] |
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Caspase 8 is a caspase protein, encoded by the CASP8 gene. It most likely acts upon caspase 3. CASP8 orthologs [1] have been identified in numerous mammals for which complete genome data are available. These unique orthologs are also present in birds.
Contents
- 1 Description
- 2 Interactions
- 3 Additional Photos
- 4 See also
- 5 References
- 6 Further reading
- 7 External links
Description[edit]
The CASP8 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.[2]
Interactions[edit]
Caspase 8 has been shown to interact with CFLAR,[3][4][5][6][7][8][9] PEA15,[10][11] Caspase 10,[3][12][13][14] Caspase-9,[13][14] Fas receptor,[4][12][15] Fas ligand,[3][12] Caspase 7,[13][14] NOL3,[16] BH3 interacting domain death agonist,[12][13] DEDD,[17][18][19] TRAF1,[3][20] Bcl-2,[13][21] RIPK1,[22][23][24] TNFRSF10B,[12][15] FADD,[3][6][12][23][25][26][27] BCAP31,[28] IFT57,[29] Caspase 3,[13][14] Caspase 2[13][14] and Caspase 6.[13][14][30]
Additional Photos[edit]
Signaling pathway of TNF-R1. Dashed grey lines represent multiple steps
Overview of signal transduction pathways involved in apoptosis.
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See also[edit]
- The Proteolysis Map
- FADD
- Caspase
References[edit]
- ^ "OrthoMaM phylogenetic marker: CASP8 coding sequence".
- ^ "Entrez Gene: CASP8 caspase 8, apoptosis-related cysteine peptidase".
- ^ a b c d e Micheau, Olivier; Tschopp Jürg (July 2003). "Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes". Cell (United States) 114 (2): 181–90. doi:10.1016/S0092-8674(03)00521-X. ISSN 0092-8674. PMID 12887920.
- ^ a b Shu, H B; Halpin D R, Goeddel D V (June 1997). "Casper is a FADD- and caspase-related inducer of apoptosis". Immunity (UNITED STATES) 6 (6): 751–63. doi:10.1016/S1074-7613(00)80450-1. ISSN 1074-7613. PMID 9208847.
- ^ Goltsev, Y V; Kovalenko A V, Arnold E, Varfolomeev E E, Brodianskii V M, Wallach D (August 1997). "CASH, a novel caspase homologue with death effector domains". J. Biol. Chem. (UNITED STATES) 272 (32): 19641–4. doi:10.1074/jbc.272.32.19641. ISSN 0021-9258. PMID 9289491.
- ^ a b Srinivasula, S M; Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce C M, Litwack G, Tomaselli K J, Armstrong R C, Alnemri E S (July 1997). "FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis". J. Biol. Chem. (UNITED STATES) 272 (30): 18542–5. doi:10.1074/jbc.272.30.18542. ISSN 0021-9258. PMID 9228018.
- ^ Micheau, Olivier; Thome Margot, Schneider Pascal, Holler Nils, Tschopp Jürg, Nicholson Donald W, Briand Christophe, Grütter Markus G (November 2002). "The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex". J. Biol. Chem. (United States) 277 (47): 45162–71. doi:10.1074/jbc.M206882200. ISSN 0021-9258. PMID 12215447.
- ^ Han, D K; Chaudhary P M, Wright M E, Friedman C, Trask B J, Riedel R T, Baskin D G, Schwartz S M, Hood L (October 1997). "MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (21): 11333–8. doi:10.1073/pnas.94.21.11333. ISSN 0027-8424. PMC 23459. PMID 9326610.
- ^ Roth, Wilfried; Stenner-Liewen Frank, Pawlowski Krzysztof, Godzik Adam, Reed John C (March 2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. (United States) 277 (9): 7501–8. doi:10.1074/jbc.M110749200. ISSN 0021-9258. PMID 11741985.
- ^ Kitsberg, D; Formstecher E, Fauquet M, Kubes M, Cordier J, Canton B, Pan G, Rolli M, Glowinski J, Chneiweiss H (October 1999). "Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis". J. Neurosci. (UNITED STATES) 19 (19): 8244–51. PMID 10493725.
- ^ Condorelli, G; Vigliotta G, Cafieri A, Trencia A, Andalò P, Oriente F, Miele C, Caruso M, Formisano P, Beguinot F (August 1999). "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis". Oncogene (ENGLAND) 18 (31): 4409–15. doi:10.1038/sj.onc.1202831. ISSN 0950-9232. PMID 10442631.
- ^ a b c d e f Gajate, Consuelo; Mollinedo Faustino (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. (United States) 280 (12): 11641–7. doi:10.1074/jbc.M411781200. ISSN 0021-9258. PMID 15659383.
- ^ a b c d e f g h Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (April 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. (United States) 277 (16): 13430–7. doi:10.1074/jbc.M108029200. ISSN 0021-9258. PMID 11832478.
- ^ a b c d e f Srinivasula, S M; Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri E S (December 1996). "Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 93 (25): 14486–91. doi:10.1073/pnas.93.25.14486. ISSN 0027-8424. PMC 26159. PMID 8962078.
- ^ a b MacFarlane, M; Ahmad M, Srinivasula S M, Fernandes-Alnemri T, Cohen G M, Alnemri E S (October 1997). "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL". J. Biol. Chem. (UNITED STATES) 272 (41): 25417–20. doi:10.1074/jbc.272.41.25417. ISSN 0021-9258. PMID 9325248.
- ^ Koseki, T; Inohara N, Chen S, Núñez G (April 1998). "ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (9): 5156–60. doi:10.1073/pnas.95.9.5156. ISSN 0027-8424. PMC 20230. PMID 9560245.
- ^ Zhan, Y; Hegde R, Srinivasula S M, Fernandes-Alnemri T, Alnemri E S (April 2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. (England) 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. ISSN 1350-9047. PMID 11965497.
- ^ Alcivar, Allison; Hu Shimin, Tang Jun, Yang Xiaolu (January 2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene (England) 22 (2): 291–7. doi:10.1038/sj.onc.1206099. ISSN 0950-9232. PMID 12527898.
- ^ Stegh, A H; Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann T G, Grummt I, Krammer P H, Peter M E (October 1998). "DEDD, a novel death effector domain-containing protein, targeted to the nucleolus". EMBO J. (ENGLAND) 17 (20): 5974–86. doi:10.1093/emboj/17.20.5974. ISSN 0261-4189. PMC 1170924. PMID 9774341.
- ^ Leo, E; Deveraux Q L, Buchholtz C, Welsh K, Matsuzawa S, Stennicke H R, Salvesen G S, Reed J C (March 2001). "TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis". J. Biol. Chem. (United States) 276 (11): 8087–93. doi:10.1074/jbc.M009450200. ISSN 0021-9258. PMID 11098060.
- ^ Poulaki, V; Mitsiades N, Romero M E, Tsokos M (June 2001). "Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2". Cancer Res. (United States) 61 (12): 4864–72. ISSN 0008-5472. PMID 11406564.
- ^ Chaudhary, P M; Eby M T, Jasmin A, Kumar A, Liu L, Hood L (September 2000). "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene (ENGLAND) 19 (39): 4451–60. doi:10.1038/sj.onc.1203812. ISSN 0950-9232. PMID 11002417.
- ^ a b Oshima, Shigeru; Turer Emre E, Callahan Joseph A, Chai Sophia, Advincula Rommel, Barrera Julio, Shifrin Nataliya, Lee Bettina, Benedict Yen T S, Yen Benjamin, Woo Tammy, Malynn Barbara A, Ma Averil (February 2009). "ABIN-1 is a Ubiquitin Sensor that Restricts Cell Death and Sustains Embryonic Development". Nature (England) 457 (7231): 906–9. doi:10.1038/nature07575. PMC 2642523. PMID 19060883.
- ^ Bertrand, Mathieu J M; Milutinovic Snezana, Dickson Kathleen M, Ho Wai Chi, Boudreault Alain, Durkin Jon, Gillard John W, Jaquith James B, Morris Stephen J, Barker Philip A (June 2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell (United States) 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID 18570872.
- ^ Henshall, David C; Araki Tomohiro, Schindler Clara K, Shinoda Sachiko, Lan Jing-Quan, Simon Roger P (September 2003). "Expression of death-associated protein kinase and recruitment to the tumor necrosis factor signaling pathway following brief seizures". J. Neurochem. (England) 86 (5): 1260–70. doi:10.1046/j.1471-4159.2003.01934.x. ISSN 0022-3042. PMID 12911633.
- ^ Boldin, M P; Goncharov T M, Goltsev Y V, Wallach D (June 1996). "Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death". Cell (UNITED STATES) 85 (6): 803–15. doi:10.1016/S0092-8674(00)81265-9. ISSN 0092-8674. PMID 8681376.
- ^ Thomas, Lance R; Stillman David J, Thorburn Andrew (September 2002). "Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen". J. Biol. Chem. (United States) 277 (37): 34343–8. doi:10.1074/jbc.M204169200. ISSN 0021-9258. PMID 12107169.
- ^ Ng, F W; Nguyen M, Kwan T, Branton P E, Nicholson D W, Cromlish J A, Shore G C (October 1997). "p28 Bap31, a Bcl-2/Bcl-XL- and Procaspase-8–associated Protein in the Endoplasmic Reticulum". J. Cell Biol. (UNITED STATES) 139 (2): 327–38. doi:10.1083/jcb.139.2.327. ISSN 0021-9525. PMC 2139787. PMID 9334338.
- ^ Gervais, François G; Singaraja Roshni, Xanthoudakis Steven, Gutekunst Claire-Anne, Leavitt Blair R, Metzler Martina, Hackam Abigail S, Tam John, Vaillancourt John P, Houtzager Vicky, Rasper Dita M, Roy Sophie, Hayden Michael R, Nicholson Donald W (February 2002). "Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi". Nat. Cell Biol. (England) 4 (2): 95–105. doi:10.1038/ncb735. ISSN 1465-7392. PMID 11788820.
- ^ Cowling, V; Downward J (October 2002). "Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain". Cell Death Differ. (England) 9 (10): 1046–56. doi:10.1038/sj.cdd.4401065. ISSN 1350-9047. PMID 12232792.
Further reading[edit]
- Song, HJ, Parodo, J, Kapus, A, Rotstein, OD, and Marshall, JC (2008). "Dynamic Regulation of Neutrophil Survival through Tyrosine Phosphorylation or Dephosphorylation of Caspase-8". Journal of Biological Chemistry 283 (9): 5402–5413. doi:10.1074/jbc.M706462200. PMID 18086677.
- Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 ( Pt 1) (Pt 1): 1–16. PMC 1218630. PMID 9337844.
- Siegel RM, Chan FK, Chun HJ, Lenardo MJ (2001). "The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity". Nat. Immunol. 1 (6): 469–74. doi:10.1038/82712. PMID 11101867.
- Ye S, Goldsmith EJ (2002). "Serpins and other covalent protease inhibitors". Curr. Opin. Struct. Biol. 11 (6): 740–5. doi:10.1016/S0959-440X(01)00275-5. PMID 11751056.
- Gupta S (2002). "Tumor necrosis factor-alpha-induced apoptosis in T cells from aged humans: a role of TNFR-I and downstream signaling molecules". Exp. Gerontol. 37 (2–3): 293–9. doi:10.1016/S0531-5565(01)00195-4. PMID 11772515.
- Pomerantz RJ (2004). "Effects of HIV-1 Vpr on neuroinvasion and neuropathogenesis". DNA Cell Biol. 23 (4): 227–38. doi:10.1089/104454904773819815. PMID 15142380.
- Zhao LJ, Zhu H (2005). "Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design". Curr. Drug Targets Immune Endocr. Metabol. Disord. 4 (4): 265–75. doi:10.2174/1568008043339668. PMID 15578977.
External links[edit]
- The MEROPS online database for peptidases and their inhibitors: C14.009
- Apoptosis & Caspase 8 - The Proteolysis Map-animation
- Caspase 8 at the US National Library of Medicine Medical Subject Headings (MeSH)
- caspase-8
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PDB gallery
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1f9e: CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO
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1i4e: CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX
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1qdu: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK
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1qtn: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE
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2c2z: CRYSTAL STRUCTURE OF CASPASE-8 IN COMPLEX WITH AZA-PEPTIDE MICHAEL ACCEPTOR INHIBITOR
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2fun: alternative p35-caspase-8 complex
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Proteases: cysteine proteases (EC 3.4.22)
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| Caspase |
- Caspase 1
- Caspase 2
- Caspase 3
- Caspase 4
- Caspase 5
- Caspase 6
- Caspase 7
- Caspase 8
- Caspase 9
- Caspase 10
- Caspase 12
- Caspase 13
- Caspase 14
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| Fruit-derived |
- Papain
- Ficain
- Bromelain
- Actinidain
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| Calpain |
- CAPN1
- CAPN2
- CAPN3
- CAPN5
- CAPN6
- CAPN7
- CAPN8
- CAPN9
- CAPN10
- CAPN11
- CAPN12
- CAPN13
- CAPN14
- CAPNS1
- CAPNS2
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| Cathepsin |
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| Other |
- Clostripain
- Cancer procoagulant
- Separase
- Autophagin
- Cruzipain
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Apoptosis signaling pathway
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| Fas path |
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Ligand
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Receptor
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Intracellular
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- Death-inducing signaling complex
- Cytochrome c
- Caspase 9
- Caspase 3
- Pro-apoptotic:
- BAX
- BAK1/Bcl-2 homologous antagonist killer
- Bcl-2-associated death promoter
- Anti-apoptotic:
- Bcl-2
- Bcl-xL
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| TNF path |
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Ligand
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Receptor
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- Tumor necrosis factor receptor
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Intracellular
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- FADD
- Caspase 8
- Caspase 3
- BID
- TRAF2
- ASK-1
- MEKK1
- IKK
- IκBα
- MKK7
- JNK
- NF-κB
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| Other |
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Intracellular
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- IAPs
- XIAP
- NAIP
- Survivin
- c-IAP-1
- c-IAP-2
- Apoptosis-inducing factor
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B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- IFN-γ combined with targeting of XIAP leads to increased apoptosis-sensitisation of TRAIL resistant pancreatic carcinoma cells.
- Büneker CK, Yu R, Deedigan L, Mohr A, Zwacka RM.SourceNational University of Ireland, Galway, National Centre for Biomedical Engineering Science (NCBES), Galway, Ireland, Molecular Therapeutics Group, University Road, Galway, Ireland.
- Cancer letters.Cancer Lett.2012 Mar 28;316(2):168-77. Epub 2011 Nov 2.
- The tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) is a specific and potent inducer of apoptosis in cancer cells, but the resistance of many tumour cells to TRAIL still represents a major hurdle for the clinical treatment of tumours with TRAIL. As apoptosis is regulated by the bala
- PMID 22104728
- Differential effects of PXD101 (belinostat) on androgen-dependent and androgen-independent prostate cancer models.
- Gravina GL, Marampon F, Giusti I, Carosa E, Di Sante S, Ricevuto E, Dolo V, Tombolini V, Jannini EA, Festuccia C.SourceDepartment of Experimental Medicine, Division of Radiotherapy, University of L'Aquila, I-67100 L'Aquila, Italy.
- International journal of oncology.Int J Oncol.2012 Mar;40(3):711-20. doi: 10.3892/ijo.2011.1270. Epub 2011 Nov 23.
- Histone deacetylase inhibitors (HDACi) are promising epigenetic cancer chemotherapeutics rapidly approaching clinical use. In this study, we tested using in vitro and in vivo models the differential biological effects of a novel HDAC inhibitor [belinostat (PXD101)
- PMID 22134754
Japanese Journal
- Ochratoxin A mediates MAPK activation, modulates IL-2 and TNF-α mRNA expression and induces apoptosis by mitochondria-dependent and mitochondria-independent pathways in human H9 T cells
- Conservation of structure and function in vertebrate c-FLIP proteins despite rapid evolutionary change
- プロテアソーム阻害剤およびIMiDsの作用機序研究の進展 (特集 多発性骨髄腫をめぐる最近の進歩と話題)
Related Links
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】Caspase-8 (1C12) Mouse mAbページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
- caspaseのcascadeはなかなか複雑で、関連する蛋白質がたくさん登場します。適宜解説を加えてくれているのでたすかりますが、理解を深めるために、重要なタンパク質 （たとえば、 BclやIAPファミリーなど）について、リンクを入れて ...
Related Pictures
★リンクテーブル★
[★]
- 英
- caspase
- 同
- ICEファミリープロテアーゼ ICE family protease
ヒトICEプロテアーゼスーパーファミリー
| Family
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Caspase
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Other Name
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Recognition
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Target (Truncation site)
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| caspase-1
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caspase-1
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ICE
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WEHD
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pro IL-1β (FEAD/G, YVHD/A), procaspase-3, procaspase-4
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| caspase-4
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ICErel-II, TX, ICH-2
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| caspase-5
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ICErel-III, TY
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| caspase-2
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caspase-2
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ICH-1
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DEHD
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PARP (DEVD/G)
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| caspase-9
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ICE-LAP6, Mch6
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LEHD
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PARP, procaspase-3
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| caspase-3
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caspase-3
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CPP32, Yama
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DEVD
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PARP, SREBP (DEPD/S), U1snRNP (DGPD/G), lamin B, D4-GDI (DELD/S), DNA-PK (DEVD/N), DFF (DETD/S, DAVD/T), actin (ELPD/G) ?, PKCδ (DMQD/N) ?]]
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| caspase-7
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Mch3, ICE-LAP3, CMH-1
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DEVD
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PARP, procaspase-6
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| caspase-6
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Mch2
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VEHD
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lamin A (VEID/N)]]
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| caspase-8
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FLICE, MACH, Mch5
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LETD
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procaspase-3, Bid
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| caspase-10
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Mch4
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LEXD
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| caspase-11
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Ich3
|
|
|
[★]
- 同
- caspase-8
- 同
- caspase-8