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
• neuronal cell body
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
• sensory perception of sound
• 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

836

12367

Ensembl

ENSG00000164305

ENSMUSG00000031628

UniProt

P42574

P70677

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[uredi | uredi izvor]

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[uredi | uredi izvor]

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

1020304050
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIII
NNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELM
RDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRS
LTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTA
PGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESF
SFDATFHAKKQIPCIVSMLTKELYFYH

Struktura[uredi | uredi izvor]

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[uredi | uredi izvor]

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[uredi | uredi izvor]

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[uredi | uredi izvor]

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[uredi | uredi izvor]

Pokazalo se da je kaspaza-3 u interakciji sa:

Klinički značaj[uredi | uredi izvor]

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[uredi | uredi izvor]

Reference[uredi | uredi izvor]

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