Caspase 3

Caspase 3, apoptosis-related cysteine peptidase
	Renderização PDB baseado em 1rhk.
Estruturas disponíveis
PDB	Busca de ortólogos: PDBe, RCSB
Lista de códigos PDB
	1CP3, 1GFW, 1I3O, 1NME, 1NMQ, 1NMS, 1PAU, 1QX3, 1RE1, 1RHJ, 1RHK, 1RHM, 1RHQ, 1RHR, 1RHU, 2C1E, 2C2K, 2C2M, 2C2O, 2CDR, 2CJX, 2CJY, 2CNK, 2CNL, 2CNN, 2CNO, 2DKO, 2H5I, 2H5J, 2H65, 2J30, 2J31, 2J32, 2J33, 2XYG, 2XYH, 2XYP, 2XZD, 2XZT, 2Y0B, 3DEH, 3DEI, 3DEJ, 3DEK, 3EDQ, 3GJQ, 3GJR, 3GJS, 3GJT, 3H0E, 3ITN, 3KJF, 3PCX, 3PD0, 3PD1, 4DCJ, 4DCO, 4DCP, 4EHA, 4EHD, 4EHF, 4EHH, 4EHK, 4EHL, 4EHN, 4JJE, 4JQY, 4JQZ, 4JR0
Identificadores
Símbolos	CASP3; CPP32; CPP32B; SCA-1
IDs externos	OMIM: 600636 MGI: 107739 HomoloGene: 37912 ChEMBL: 2334 GeneCards: CASP3 Gene
Número EC	3.4.22.56
Ontologia do gene
Função molecular	•aspartic-type endopeptidase activity; •cysteine-type endopeptidase activity; •cyclin-dependent protein serine/threonine kinase inhibitor activity; •protein binding; •peptidase activity; •cysteine-type endopeptidase activity involved in apoptotic process; •cysteine-type endopeptidase activity involved in execution phase of apoptosis;
Componente celular	•nucleus; •nucleoplasm; •cytosol; •plasma membrane;
Processo biológico	•B cell homeostasis; •release of cytochrome c from mitochondria; •apoptotic DNA fragmentation; •proteolysis; •apoptotic process; •cellular component disassembly involved in execution phase of apoptosis; •cellular response to DNA damage stimulus; •heart development; •sensory perception of sound; •extrinsic apoptotic signaling pathway via death domain receptors; •intrinsic apoptotic signaling pathway in response to oxidative stress; •activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; •response to UV; •response to wounding; •extracellular matrix disassembly; •neuron differentiation; •extracellular matrix organization; •keratinocyte differentiation; •erythrocyte differentiation; •platelet formation; •negative regulation of B cell proliferation; •glial cell apoptotic process; •response to tumor necrosis factor; •hippo signaling; •regulation of apoptotic process; •T cell homeostasis; •positive regulation of apoptotic process; •negative regulation of apoptotic process; •regulation of cysteine-type endopeptidase activity involved in apoptotic process; •positive regulation of neuron apoptotic process; •cell fate commitment; •negative regulation of cyclin-dependent protein serine/threonine kinase activity; •negative regulation of activated T cell proliferation; •neurotrophin TRK receptor signaling pathway; •neuron apoptotic process; •apoptotic signaling pathway; •extrinsic apoptotic signaling pathway in absence of ligand; •intrinsic apoptotic signaling pathway; •execution phase of apoptosis;
	Sources: Amigo / QuickGO
Padrões de expressão do ARN
	Mais dados de expressão
Ortólogos
	v; d; e;

A caspase 3 é um das caspases existentes. Interage com a caspase 8.

O gene correspondente codifica uma proteína que é membro da família das proteases de cisteína-aspartato. A activação sequêncial das caspases desempenha um papel central na fase de execução da apoptose celular. As caspases existem como pró-enzimas inactivas que depois sofrem um processamento proteolítico em resíduos de aspartato, para produzirem duas subunidades, uma pequena e outra grande, que dimerizam para formar a enzima activa. Esta enzima faz a clivagem e a activação da caspase 6, caspase 7 e caspase 9. A própria proteína é processada pela caspase 8, caspase 9 e caspase 10. É a caspase predominante envolvida na clivagem da proteína percursora amilóide-beta 4A, que está associada à morte neuronal na doença de Alzheimer. O splicing alternativo deste gene resulta em dois transcritos que codificam a mesma proteína.^[1]

A Caspase 3 mostrou interação com:

CASP8,^[2]^[3]
CFLAR,^[4]^[5]
DCC,^[6]
GroEL,^[7]^[8]
HCLS1,^[9]^[10]
Survivin,^[11]^[12]
TRAF3,^[13]^[14] and
XIAP.^[15]^[16]^[17]^[18]^[19]^[20]

Referências

↑ «Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase»
↑ Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (2002). «Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria». United States. J. Biol. Chem. 277 (16): 13430–7. ISSN 0021-9258. PMID 11832478. doi:10.1074/jbc.M108029200
↑ Srinivasula, S M; Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri E S (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». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. ISSN 0027-8424. PMC 26159 . PMID 8962078. doi:10.1073/pnas.93.25.14486
↑ Shu, H B; Halpin D R, Goeddel D V (1997). «Casper is a FADD- and caspase-related inducer of apoptosis». UNITED STATES. Immunity. 6 (6): 751–63. ISSN 1074-7613. PMID 9208847. doi:10.1016/S1074-7613(00)80450-1
↑ 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 (1997). «MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11333–8. ISSN 0027-8424. PMC 23459 . PMID 9326610. doi:10.1073/pnas.94.21.11333
↑ Forcet, C; Ye X, Granger L, Corset V, Shin H, Bredesen D E, Mehlen P (2001). «The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3416–21. ISSN 0027-8424. PMC 30668 . PMID 11248093. doi:10.1073/pnas.051378298
↑ Samali, A; Cai J, Zhivotovsky B, Jones D P, Orrenius S (1999). «Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells». ENGLAND. EMBO J. 18 (8): 2040–8. ISSN 0261-4189. PMC 1171288 . PMID 10205158. doi:10.1093/emboj/18.8.2040
↑ Xanthoudakis, S; Roy S, Rasper D, Hennessey T, Aubin Y, Cassady R, Tawa P, Ruel R, Rosen A, Nicholson D W (1999). «Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis». ENGLAND. EMBO J. 18 (8): 2049–56. ISSN 0261-4189. PMC 1171289 . PMID 10205159. doi:10.1093/emboj/18.8.2049
↑ Ruzzene, Maria; Penzo Daniele, Pinna Lorenzo A (2002). «Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells». England. Biochem. J. 364 (Pt 1): 41–7. ISSN 0264-6021. PMC 1222543 . PMID 11988074
↑ Chen, Y R; Kori R, John B, Tan T H (2001). «Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis». United States. Biochem. Biophys. Res. Commun. 288 (4): 981–9. ISSN 0006-291X. PMID 11689006. doi:10.1006/bbrc.2001.5862
↑ Tamm, I; Wang Y, Sausville E, Scudiero D A, Vigna N, Oltersdorf T, Reed J C (1998). «IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs». UNITED STATES. Cancer Res. 58 (23): 5315–20. ISSN 0008-5472. PMID 9850056
↑ Shin, S; Sung B J, Cho Y S, Kim H J, Ha N C, Hwang J I, Chung C W, Jung Y K, Oh B H (2001). «An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7». United States. Biochemistry. 40 (4): 1117–23. ISSN 0006-2960. PMID 11170436. doi:10.1021/bi001603q
↑ Lee, Z H; Lee S E, Kwack K, Yeo W, Lee T H, Bae S S, Suh P G, Kim H H (2001). «Caspase-mediated cleavage of TRAF3 in FasL-stimulated Jurkat-T cells». United States. J. Leukoc. Biol. 69 (3): 490–6. ISSN 0741-5400. PMID 11261798
↑ Leo, E; Deveraux Q L, Buchholtz C, Welsh K, Matsuzawa S, Stennicke H R, Salvesen G S, Reed J C (2001). «TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis». United States. J. Biol. Chem. 276 (11): 8087–93. ISSN 0021-9258. PMID 11098060. doi:10.1074/jbc.M009450200
↑ Suzuki, Y; Nakabayashi Y, Takahashi R (2001). «Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (15): 8662–7. ISSN 0027-8424. PMC 37492 . PMID 11447297. doi:10.1073/pnas.161506698
↑ Silke, John; Hawkins Christine J, Ekert Paul G, Chew Joanne, Day Catherine L, Pakusch Miha, Verhagen Anne M, Vaux David L (2002). «The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites». United States. J. Cell Biol. 157 (1): 115–24. ISSN 0021-9525. PMC 2173256 . PMID 11927604. doi:10.1083/jcb.200108085
↑ Riedl, S J; Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik S W, Liddington R C, Salvesen G S (2001). «Structural basis for the inhibition of caspase-3 by XIAP». United States. Cell. 104 (5): 791–800. ISSN 0092-8674. PMID 11257232. doi:10.1016/S0092-8674(01)00274-4
↑ Roy, N; Deveraux Q L, Takahashi R, Salvesen G S, Reed J C (1997). «The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases». ENGLAND. EMBO J. 16 (23): 6914–25. ISSN 0261-4189. PMC 1170295 . PMID 9384571. doi:10.1093/emboj/16.23.6914
↑ Deveraux, Q L; Takahashi R, Salvesen G S, Reed J C (1997). «X-linked IAP is a direct inhibitor of cell-death proteases». ENGLAND. Nature. 388 (6639): 300–4. ISSN 0028-0836. PMID 9230442. doi:10.1038/40901
↑ Suzuki, Y; Nakabayashi Y, Nakata K, Reed J C, Takahashi R (2001). «X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes». United States. J. Biol. Chem. 276 (29): 27058–63. ISSN 0021-9258. PMID 11359776. doi:10.1074/jbc.M102415200

Leitura de apoio

Cohen GM (1997). «Caspases: the executioners of apoptosis.». Biochem. J. 326 (Pt 1): 1–16. PMC 1218630 . PMID 9337844
Roig J, Traugh JA (2001). «Cytostatic p21 G protein-activated protein kinase gamma-PAK.». Vitam. Horm. 62: 167–98. PMID 11345898. doi:10.1016/S0083-6729(01)62004-1
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. PMID 15578977. doi:10.2174/1568008043339668
Le Rouzic E, Benichou S (2006). «The Vpr protein from HIV-1: distinct roles along the viral life cycle.». Retrovirology. 2. 11 páginas. PMC 554975 . PMID 15725353. doi:10.1186/1742-4690-2-11
Sykes MC, Mowbray AL, Jo H (2007). «Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death.». Circ. Res. 100 (2): 152–4. PMID 17272816. doi:10.1161/01.RES.0000258171.08020.72

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[1] «Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase»

[pmid11832478-2] Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (2002). «Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria». United States. J. Biol. Chem. 277 (16): 13430–7. ISSN 0021-9258. PMID 11832478. doi:10.1074/jbc.M108029200

[pmid8962078-3] Srinivasula, S M; Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri E S (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». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. ISSN 0027-8424. PMC 26159 . PMID 8962078. doi:10.1073/pnas.93.25.14486

[pmid9208847-4] Shu, H B; Halpin D R, Goeddel D V (1997). «Casper is a FADD- and caspase-related inducer of apoptosis». UNITED STATES. Immunity. 6 (6): 751–63. ISSN 1074-7613. PMID 9208847. doi:10.1016/S1074-7613(00)80450-1

[pmid9326610-5] 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 (1997). «MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11333–8. ISSN 0027-8424. PMC 23459 . PMID 9326610. doi:10.1073/pnas.94.21.11333

[pmid11248093-6] Forcet, C; Ye X, Granger L, Corset V, Shin H, Bredesen D E, Mehlen P (2001). «The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3416–21. ISSN 0027-8424. PMC 30668 . PMID 11248093. doi:10.1073/pnas.051378298

[pmid10205158-7] Samali, A; Cai J, Zhivotovsky B, Jones D P, Orrenius S (1999). «Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells». ENGLAND. EMBO J. 18 (8): 2040–8. ISSN 0261-4189. PMC 1171288 . PMID 10205158. doi:10.1093/emboj/18.8.2040

[pmid10205159-8] Xanthoudakis, S; Roy S, Rasper D, Hennessey T, Aubin Y, Cassady R, Tawa P, Ruel R, Rosen A, Nicholson D W (1999). «Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis». ENGLAND. EMBO J. 18 (8): 2049–56. ISSN 0261-4189. PMC 1171289 . PMID 10205159. doi:10.1093/emboj/18.8.2049

[pmid11988074-9] Ruzzene, Maria; Penzo Daniele, Pinna Lorenzo A (2002). «Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells». England. Biochem. J. 364 (Pt 1): 41–7. ISSN 0264-6021. PMC 1222543 . PMID 11988074

[pmid11689006-10] Chen, Y R; Kori R, John B, Tan T H (2001). «Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis». United States. Biochem. Biophys. Res. Commun. 288 (4): 981–9. ISSN 0006-291X. PMID 11689006. doi:10.1006/bbrc.2001.5862

[pmid9850056-11] Tamm, I; Wang Y, Sausville E, Scudiero D A, Vigna N, Oltersdorf T, Reed J C (1998). «IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs». UNITED STATES. Cancer Res. 58 (23): 5315–20. ISSN 0008-5472. PMID 9850056

[pmid11170436-12] Shin, S; Sung B J, Cho Y S, Kim H J, Ha N C, Hwang J I, Chung C W, Jung Y K, Oh B H (2001). «An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7». United States. Biochemistry. 40 (4): 1117–23. ISSN 0006-2960. PMID 11170436. doi:10.1021/bi001603q

[pmid11261798-13] Lee, Z H; Lee S E, Kwack K, Yeo W, Lee T H, Bae S S, Suh P G, Kim H H (2001). «Caspase-mediated cleavage of TRAF3 in FasL-stimulated Jurkat-T cells». United States. J. Leukoc. Biol. 69 (3): 490–6. ISSN 0741-5400. PMID 11261798

[pmid11098060-14] Leo, E; Deveraux Q L, Buchholtz C, Welsh K, Matsuzawa S, Stennicke H R, Salvesen G S, Reed J C (2001). «TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis». United States. J. Biol. Chem. 276 (11): 8087–93. ISSN 0021-9258. PMID 11098060. doi:10.1074/jbc.M009450200

[pmid11447297-15] Suzuki, Y; Nakabayashi Y, Takahashi R (2001). «Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (15): 8662–7. ISSN 0027-8424. PMC 37492 . PMID 11447297. doi:10.1073/pnas.161506698

[pmid11927604-16] Silke, John; Hawkins Christine J, Ekert Paul G, Chew Joanne, Day Catherine L, Pakusch Miha, Verhagen Anne M, Vaux David L (2002). «The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites». United States. J. Cell Biol. 157 (1): 115–24. ISSN 0021-9525. PMC 2173256 . PMID 11927604. doi:10.1083/jcb.200108085

[pmid11257232-17] Riedl, S J; Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik S W, Liddington R C, Salvesen G S (2001). «Structural basis for the inhibition of caspase-3 by XIAP». United States. Cell. 104 (5): 791–800. ISSN 0092-8674. PMID 11257232. doi:10.1016/S0092-8674(01)00274-4

[pmid9384571-18] Roy, N; Deveraux Q L, Takahashi R, Salvesen G S, Reed J C (1997). «The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases». ENGLAND. EMBO J. 16 (23): 6914–25. ISSN 0261-4189. PMC 1170295 . PMID 9384571. doi:10.1093/emboj/16.23.6914

[pmid9230442-19] Deveraux, Q L; Takahashi R, Salvesen G S, Reed J C (1997). «X-linked IAP is a direct inhibitor of cell-death proteases». ENGLAND. Nature. 388 (6639): 300–4. ISSN 0028-0836. PMID 9230442. doi:10.1038/40901

[pmid11359776-20] Suzuki, Y; Nakabayashi Y, Nakata K, Reed J C, Takahashi R (2001). «X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes». United States. J. Biol. Chem. 276 (29): 27058–63. ISSN 0021-9258. PMID 11359776. doi:10.1074/jbc.M102415200

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