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Kaspaza-3

S Wikipedije, slobodne enciklopedije
Kaspaza-3
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

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, 4PRY, 4PS0, 4QTX, 4QTY, 4QU0, 4QU5, 4QU8, 4QU9, 4QUA, 4QUB, 4QUD, 4QUE, 4QUG, 4QUH, 4QUI, 4QUJ, 4QUL, 5IC4

Identifikatori
AliasiCASP3
Vanjski ID-jeviOMIM: 600636 MGI: 107739 HomoloGene: 37912 GeneCards: CASP3
Lokacija gena (miš)
Hromosom 8 (miš)
Hrom.Hromosom 8 (miš)[1]
Hromosom 8 (miš)
Genomska lokacija za Kaspaza-3
Genomska lokacija za Kaspaza-3
Bend8 B1.1|8 26.39 cMPočetak47,070,326 bp[1]
Kraj47,092,724 bp[1]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija cysteine-type peptidase activity
GO:0070122 peptidase activity
GO:0001948, GO:0016582 vezivanje za proteine
phospholipase A2 activator activity
cyclin-dependent protein serine/threonine kinase inhibitor activity
cysteine-type endopeptidase activity involved in apoptotic process
cysteine-type endopeptidase activity involved in execution phase of apoptosis
cysteine-type endopeptidase activity
hydrolase activity
cysteine-type endopeptidase activator activity involved in apoptotic process
aspartic-type endopeptidase activity
protease binding
death receptor binding
GO:0032403 protein-containing complex binding
cysteine-type endopeptidase activity involved in apoptotic signaling pathway
Ćelijska komponenta citoplazma
citosol
nukleoplazma
death-inducing signaling complex
Lipidni splav
jedro
soma
Biološki proces cellular response to organic substance
neuron apoptotic process
cell fate commitment
response to estradiol
GO:0007243 intracellular signal transduction
response to hypoxia
response to amino acid
apoptotic DNA fragmentation
GO:1904578 response to organic cyclic compound
negative regulation of cyclin-dependent protein serine/threonine kinase activity
GO:1904576 response to antibiotic
platelet formation
protein processing
response to nicotine
response to metal ion
negative regulation of cell cycle
Zarastanje rana
response to glucocorticoid
GO:1904579 cellular response to organic cyclic compound
B cell homeostasis
negative regulation of apoptotic process
sluh
response to glucose
response to organic substance
hippo signaling
glial cell apoptotic process
keratinocyte differentiation
Proteoliza
cellular response to DNA damage stimulus
T cell homeostasis
response to tumor necrosis factor
negative regulation of activated T cell proliferation
heart development
response to lipopolysaccharide
positive regulation of neuron apoptotic process
response to wounding
neuron differentiation
extrinsic apoptotic signaling pathway in absence of ligand
learning or memory
positive regulation of apoptotic process
erythrocyte differentiation
apoptotic signaling pathway
negative regulation of B cell proliferation
response to cobalt ion
hippocampus development
response to UV
response to X-ray
response to hydrogen peroxide
regulation of macroautophagy
neurotrophin TRK receptor signaling pathway
execution phase of apoptosis
intrinsic apoptotic signaling pathway in response to osmotic stress
cellular response to staurosporine
GO:0097285 apoptoza
cytokine-mediated signaling pathway
activation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0048554 positive regulation of catalytic activity
luteolysis
axonal fasciculation
striated muscle cell differentiation
leukocyte apoptotic process
regulation of protein stability
positive regulation of amyloid-beta formation
anterior neural tube closure
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)

NM_004346
NM_032991

NM_009810
NM_001284409

RefSeq (bjelančevina)
NP_004337
NP_116786
NP_001341706
NP_001341708
NP_001341709

NP_001341710
NP_001341711
NP_001341712
NP_001341713

NP_001271338
NP_033940

Lokacija (UCSC)n/aChr 8: 47.07 – 47.09 Mb
PubMed pretraga[2][3]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Kaspaza-3 je kaspazni protein koji je u interakciji sa kaspazom-8 i kaspazom-9. Kodira ga gen "'CASP3"' koji se kod ljudi nalazi na hromosoma 4, sekvenca q35.1. CASP3 ortolozi[4] identificirani su kod brojnih sisara za koje su dostupni potpuni podaci o genomu. Jedinstveni ortolozi su također prisutni u ptica, guštera, Lissamphibia, i teleostea.

CASP3 protein je član porodice cistein-aspartata (kaspaza).[5] Sekvencna aktivacija kaspaza ima centralnu ulogu u fazi izvršenja ćelijske apoptoze. Kaspaze postoje kao neaktivni proenzimi koji se podvrgavaju proteolitskoj obradi na konzerviranim asparaginskim ostacima kako bi se proizvele dvije podjedinice, velika i mala, koje se dimeriziraju i formiraju aktivni enzim. Ovaj protein cijepa i aktivira kaspazu-6 i 7; a sam protein se obrađuje i aktivira kaspazama 8, 9 i 10. To je dominantna kaspaza uključena u cijepanje amiloid-beta 4A prekursorskog proteina, koja je povezana sa neuronskom smrću u Alzheimeromoj bolesti .[6] Alternativna prerada ovog gena rezultira u dvije varijante transkripta koje kodiraju isti protein.[7]

Signalni put TNF-R1: Isprekidane sive linije predstavljaju više koraka
Putevi koji vode do aktivacije kaspaze 3.[8]

Kaspaza-3 dijeli mnoge tipske karakteristike zajedničke svim sada poznatim kaspazama. Naprimjer, njegovo aktivno mjesto sadrži cisteinski ostatak (Cys-163) i histidinski ostatak (His-121) koji stabiliziraju peptidnu vezu cijepanjem proteinske sekvence na karboksi-terminalnoj strani asparaginske kiseline kada je dio određene sekvence 4-amino kiseline.[9][10] Ova specifičnost omogućava kaspazama da budu nevjerovatno selektivne, sa 20.000 puta prednosti asparaginske kiseline u odnosu na glutaminsku.[11] Ključna karakteristika kaspaza u ćeliji je da su prisutne kao zimogeni, zvani prokaspaze, koje su neaktivne sve dok biohemijska promjena ne izazove njihovu aktivaciju. Svaka prokaspaza ima veliku N-terminalnu podjedinicu od oko 20 kDa, a zatim manju podjedinicu od oko 10 kDa, zvanu+e p20 i p10.[12]

Specifičnost supstrata

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U normalnim okolnostima, kaspaze prepoznaju tetrapeptidne sekvence na svojim supstratima i hidroliziraju peptidne veze nakon ostataka asparaginske kiseline. Kaspaza 3 i kaspaza-7 dijele sličnu specifičnost supstrata, prepoznavanjem tetrapeptidnog motiva Asp-x-x-Asp.[13] C-terminal Asp je apsolutno neophodan dok se varijacije na ostala tri položaja mogu tolerisati.[14] Specifičnost supstrata kaspaze se široko koristi u kaspazi zasnovanoj na inhibitorima i dizajnu lijekova.[15]

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 277 aminokiselina, a molekulska težina 31.608 Da.[15]

1020304050
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIII
NNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELM
RDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRS
LTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTA
PGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESF
SFDATFHAKKQIPCIVSMLTKELYFYH

Struktura

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Kaspaza-3, posebno, (također poznata kao CPP32/Yama/apopain)[16][17][18] formira se od zimogena od 32 kDa koji se cijepa na podjedinice od 17 kDa i 12 kDa. Kada se prokapaza cijepa na određenom ostatku, aktivni heterotetramer se tada može formirati hidrofobnim interakcijama, uzrokujući da se četiri antiparalelna beta-lista od p17 i dva od p12 spoje kako bi napravili heterodimer, koji zauzvrat stupa u interakciju s drugim heterodimerom da formira punu 12-lančanu beta-listnu strukturu okruženu alfa-heliksima koja je jedinstvena za kaspaze.[12][19] Kada se heterodimeri poravnaju jedan s drugim, aktivno mjesto je pozicionirano na svakom kraju molekule formirane od ostataka iz obje sudioničke podjedinice, iako se neophodni ostaci Cys-163 i His-121 nalaze na p17 (većoj) podjedinici.[19]

Podjedinice p12 (ružičasta) i p17 (svijetloplava) kaspaze-3 sa strukturama beta-listova svake crvene i plave boje; slika generirana u Pymolu iz 1rhm.pdb

Mehanizam

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Katalitsko mjesto kaspaze-3 uključuje tiolnu grupu Cys-163 i imidazolski prsten His-121. His-121 stabilizira karbonil grupu ključnog aspartatnog ostatka, dok Cys-163 napada kako bi konačno cijepao peptidnu vezu. Cys-163 i Gly-238 takođe funkcionišu da stabilizuju tetraedarsko prijelazno stanje kompleksa supstrat-enzim putem vodikove veze.[19] In vitro, utvrđeno je da kaspaza -3 preferira peptidnu sekvencu DEVDG (Asp-Glu-Val-Asp-Gly) sa cijepanjem koje se događa na karboksi strani drugog ostatka asparaginske kiseline (između D i G).[20]

Posdjedinice Cys-285 (žuta) i His-237 (zelena i tamnoplava) u aktivnom mjestu kaspaze-3, p12 u ružičastoj i p17 podjedinica u sviietloplavoj; slika generirana u Pymolu iz 1rhr.pdb

Aktivacija

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Kaspaza-3 se aktivira u apoptotskoj ćeliji i vanjskimim (ligand smrti) i unutrašnjim (mitohondrijskim) putevima.[12][21] The zymogen feature of caspase-3 is necessary because if unregulated, caspase activity would kill cells indiscriminately.[22] Kao egzekutorska kaspaza, zimogen kaspaze-3 nema praktično nikakvu aktivnost sve dok ga kaspaza inicijatora ne rascijepi nakon što su se dogodili događaji apoptotske signalizacije.[23] Jedan takav signalni događaj je uvođenje granzima B, koji može aktivirati inicijatorske kaspaze, u ćelije ciljane na apoptozu putem T-ćelija.[24][25] Ova vanjska aktivacija zatim pokreće osobenu kaspaznu kaskadu karakterističnu za apoptotski put, u kojoj kaspaza-3 ima dominantnu ulogu. U unutrašnjoj aktivaciji, citohrom c iz mitohondrija djeluje u kombinaciji sa kaspazom-9, faktorom 1 koji aktivira apoptozu (Apaf-1) i ATP za obradu prokapaze-3.[26] Ove molekule su dovoljne da aktiviraju kaspazu-3 in vitro, ali su neophodni i drugi regulatorni proteini in vivo.[26]

Pokazalo se da ekstrakt mangostina (Garcinia mangostana) inhibira aktivaciju kaspaze-3 u ljudskim neuronskim ćelijama tretiranim B-amiloidom.[27]

Inhibicija

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Jedan od načina inhibicije kaspaze je preko porodice proteina IAP (inhibitor apoptoze), koja uključuje c-IAP1, c-IAP2, XIAP i ML-IAP.[19] XIAP binds and inhibits initiator caspase-9, which is directly involved in the activation of executioner caspase-3.[26] Međutim, tokom kaskade kaspaze, kaspaza-3 funkcioniše tako da inhibira aktivnost XIAP, cijepajući kaspazu-9 na određenom mjestu, sprječavajući XIAP da se veže i inhibira aktivnost kaspaze-9.[28]

Interakcije

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Pokazalo se da je kaspaza-3 u interakciji sa:

Klinički značaj

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Utvrđeno je da je kaspaza-3 neophodna za normalan razvoj mozga, kao i njenu tipsku ulogu u apoptozi, gdje je odgovorna za kondenzaciju hromatina i fragmentaciju DNK. Povišeni nivoi fragmenta kaspaze-3, p17, u krvotoku je znak nedavnog infarkta miokarda.[50] Sada je pokazano da kaspaza-3 može imati ulogu u embrionskoj i hematopoetskoj diferencijaciji matičnih ćelija.[51]

Također pogledajte

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Reference

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