Wikipedia

S100A1

S100A1, znan i kao S100 kalcij-vezujući protein A1 jest protein koji je kod ljudi kodiran genom S100A1 sa hromosoma 1.[5][6] S100A1 je visoko eksprimiran u srčanom i skeletnim mišićima, a nalazi sena Z-diskovima i sarkoplazmatskom retikulumu. S100A1 je obećavajući kao efikasan kandidat za gensku terapiju za liječenje srčanog tkiva nakon infarkta miokarda.

S100A1
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

2L0P, 2LHL, 2LLS, 2LLT, 2LLU, 2LP2, 2LP3, 2LUX, 2M3W

Identifikatori
AliasiS100A1
Vanjski ID-jeviOMIM: 176940 MGI: 1338917 HomoloGene: 4566 GeneCards: S100A1
Lokacija gena (čovjek)
Hromosom 1 (čovjek)
Hrom.Hromosom 1 (čovjek)[1]
Hromosom 1 (čovjek)
Genomska lokacija za S100A1
Genomska lokacija za S100A1
Bend1q21.3Početak153,627,926 bp[1]
Kraj153,632,039 bp[1]
Lokacija gena (miš)
Hromosom 3 (miš)
Hrom.Hromosom 3 (miš)[2]
Hromosom 3 (miš)
Genomska lokacija za S100A1
Genomska lokacija za S100A1
Bend3 F1|3 39.24 cMPočetak90,418,341 bp[2]
Kraj90,421,699 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• calcium ion binding
• S100 protein binding
• protein homodimerization activity
• ATPase binding
• calcium-dependent protein binding
• vezivanje iona metala
• GO:0001948, GO:0016582 vezivanje za proteine
• vezivanje identičnih proteina
Ćelijska komponenta• citoplazma
• M band
• I band
• Sarkoplazmatski retikulum
• Z discdkac
• neuron projection
• A band
• jedro
• extracellular region
• GO:0009327 makromolekulani kompleks
Biološki proces• GO:0007243 intracellular signal transduction
• regulation of heart contraction
• substantia nigra development
• positive regulation of voltage-gated calcium channel activity
• GO:1901227 negative regulation of transcription by RNA polymerase II
• toll-like receptor signaling pathway
• positive regulation of nitric-oxide synthase activity
• positive regulation of sprouting angiogenesis
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

6271

20193

Ensembl

ENSG00000160678

ENSMUSG00000044080

UniProt

P23297

P56565

RefSeq (mRNK)

NM_006271

NM_011309

RefSeq (bjelančevina)

NP_006262

NP_035439

Lokacija (UCSC)Chr 1: 153.63 – 153.63 MbChr 3: 90.42 – 90.42 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 94 aminokiseline, a molekulska težina 10.546 Da.[7]

1020304050
MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQK
DVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS

Struktura

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S100A1 je član porodice S100 proteina, eksprimiranih u srčanom mi i skeletnim mišićima i mozgu,[8] sa najvećom gustoćom na Z-linijama i sarkoplazmatskom retikulumu.[9] S100A1 sadrži 4 F-šakin kalcij-vezujući motiv u svom dimeriziranom obliku,[10] a može postojati ili kao hetero- ili kao homodimer. Homodimer S100A1 je visokog afiniteta (nanomolarni raspon ili manji), a formira se kroz hidrofobno pakovanje snopa X-tipa od četiri spirale, stvorenog između heliksa 1, 1', 4 i 4'. Proteinska nuklearna magnetna rezonantna spektroskopija pokazuje strukturne informacije o homodimernom obliku ovog proteina, gdje je svaki monomer spiralan i da sadrži dvije EF-šakine petlje za vezanje kalcija; jedan na N-terminalu i kanonska EF-šaka u C-terminalu, koji ima veći afinitet za kalcij (konstanta disocijacije od otprilike 20 mikromolara). Dva domena EF-šaka sususjedna su u trodimenzijskom prostoru i međusobno povezana kratkom regijom beta-listova(ostaci 27–29 i 68–70).

Nakon vezivanja kalcija, heliks 3 S100A1 se preorijentiše od relativno antiparalelnog prema heliksu 4 da bude otprilike okomit. Ova konformaciona promena razlikuje se od većine EF- šaka, po tome što se kreće spirala koja ulazi, a ne izlazi. Ova konformaciona promena otkriva veliki hidrofobni džep između heliksa 3, 4 i zglobnog regiona S100A1, koji je uključen u gotovo sve kalcij-ovisne interakcije ciljnog proteina. Čini se da su ova biofizička svojstva dobro konzervirana u porodici proteina S100. Heliksi 3, 4 i zglobni region su područja sa najdivergentnijima između pojedinačnih S100 proteina, pa je vjerovatno da je sekvenca ovih regiona ključna u finom podešavanju vezivanja ovisnog od kalcija, putem S100 proteina.[11] S-Nitrozilacija S100A1 na Cys85 reorganizira konformaciju S100A1 na C-terminalnom heliksu i linker koji povezuje dva domena EF-šaka.[12]

Najpreciznija struktura rastvora visoke rezolucije ljudskog apo-S100A1 proteina (PDB pristupni kod: 2L0P) određena je pomoću NMR spektroskopije u 2011.[13]

Geni S100 uključuju najmanje 19 članova koji su locirani kao klaster na hromosomskoj regiji 1q21.[14][15]

Funkcija

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S100 proteini su lokalizovani u citoplazmi i/ili jedru širokog spektra ćelija i uključeni su u regulaciju brojnih ćelijskih procesa kao što su progresija ćelijskog ciklusa i diferencijacija. Ovaj protein može funkcionirati u stimulaciji Ca2+-indukovanog oslobađanja Ca2+, inhibiciji sklapanja mikrotubula i inhibiciji protein-kinaza C-posredovanih fosforilacija.

S100A1 se eksprimira tokom razvoja u primitivnom srcu 8. embrionskog dana, na nivoima koji su slični između pretkomore i komora. Kako razvoj napreduje do embrionskog dana 17.5, ekspresija S100A1 se pomjera na niže nivoe u predkomorama i više u komorama miokarda.[16]

S100A1 pokazao se kao regulator kontraktilnosti miokarda. Prekomjerna ekspresija S100A1 preko adenovirusnog prijenosa gena kod kardiomiocita odraslih kunića ili kod mišjeg transgenog S100A1 ograničenog na rad srca, poboljšava srčanu kontraktilnost, povećanjem prolaznih procesa i unosa kalcija u sarkoplazmatski retikulum, menjajući osjetljivost na kalcij i kooperativnost miofibrila, pojačavajući aktivnost SERCA2A i pojačavajući kalcij-inducirano oslobađanje kalcija.[17][18][19] Konkretno, S100A1 povećava pojačanje sprege nadražaj-kontrakcija[20] i smanjuje frekvenciju kalcijevih podražaja[21] u kardiomiocitima. Pokazalo se da povećanje priliva L-tipa kalcijskog kanala transsarkolemnog kalcija putem S100A ovisi od protein-kinaza A.[22] Efekti S100A1 na proteine miofilamenta mogu biti preko titina; pokazalo se da S100A1 stupa u interakciju s PEVK regijom titina na kalcij- ovisan način, a njegovo vezivanje smanjuje silu u in vitro testu pokretljivosti, sugerirajući da S100A može modulirati titin-pasivnu tenziju prije sistola.[23][24] Kod miševa sa ablacijom gena S100A1 (S100A1 –/–), srčana rezerva nakon beta adrenalinske stimulacije bila je poremećena, pokazujući smanjenu brzinu kontrakcije i brzinu opuštanja, kao i smanjenu osjetljivostna kalcij. Međutim, S100A1–/– nije pokazao eventualnu srčanu hipertrofiju ili proširenje komore kod starijih miševa.[25]

U životinjskim modelima bolesti, pokazalo se da su nivoi proteina S100A1 promijenjeni u desnoj komori, hipertrofirano u tkivu u modelu plućne hipertenzije;[26] nekoliko tipova tkiva (mozak, skeletni mišić i srčani mišić) u modelu tip I dijabetes melitus;[27] S100A1 je demonstriran kao regulator genetičkog programa koji leži u osnovi hipertrofije srca, jer S100A1 inhibira alfa1 adrenalinsku stimulaciju hipertrofijskih gena, uključujući MYH7 , ACTA1 i S100B.[28] U pacovskom modelu infarkta miokarda, intrakoronski prijenos gena S100A1 adenovirusom obnovio je kalcijske prolazne procese i opterećenja sarkoplazmatskog retikuluma, normalizirjuču unutarćelijske koncentracije natrija, a poništio je patološku ekspresiju fetusog genskog programa, obnovio opskrbu energijom, normalizirao kontraktilnu funkciju, sačuvao inotropnu rezervu i smanjio hipertrofiju srca sedmicu nakon infarkta miokarda.[29][30] U prilog eksperimentima adenovirusne, transgeneze kod miševa s prekomjernom ekspresijom S100A1 podvrgnutih infarktu miokarda pokazali su očuvanu kontraktilnu funkciju, poništenu apoptozu, očuvan kalcijski ciklus u sarkoplazmatskom retikulumu i beta adrennalinsku signalizaciju, prevenciju hipertrofije srca i srčane insuficijencije, kao i produženo preživljavanje u odnosu na netransgene kontrole.[31][32]

S100A1 je također identificiran kao novi regulator endotelnih ćelija postishemijske angiogeneze, jer su pacijenti sa ishemijom ekstremiteta pokazali smanjenje ekspresije S100A1 u hipoksijskom tkivu.[33][34]

U melanocitnim ćelijama, ekspresija gena S100A1 može biti regulirana transkripcijskim faktorom povezanim sa mikroftalmijom (MITF).[35]

Klinički značaj

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S100A1 je pokazao djelotvornost u izvodljivosti u liječenju simptoma srčane insuficijencije na velikim, pretkliničkim modelima i ljudskim kardiomiocitima,[36][37] and thus shows great promise for clinical trials.[38][39][40][41][42][43][44]

Smanjena ekspresija ovog proteina je uključena u kardiomiopatije,[45] i terapiju zasnovanu na uređaju za pomoć lijevoj komori, ne vraćajući nivoe S100A1 kod pacijenata.[46] S100A1 se pokazao obećavajućim kao rani dijagnostički biomarker za akutnu ishemiju miokarda, koji se predstavlja s različitim vremenskim tokom u ljudskoj plazmi nakon ishemijskog događaja u odnosu na tradicionalne markere kreatin-kinaza, CKMB i troponin I.[47][48] Ovaj vanćelijski skup S100A1 koji se oslobađa od povreda, eksprimiran je kod neonatusnih mišjih kardiomiocita i pokazalo se da sprječava apoptoze putem ERK1/2-zavisnog puta, što sugerira da je oslobađanje S100A1 iz ozlijeđenih ćelija unutrašnji mehanizam preživljavanja za održivi miokard.[49] S100 se također pokazao obećavajućim kao biomarker za nekontroliranu hiperoksičnu reoksigenaciju tokom kardiopulmonalne premosnice kod novorođenčadi sa cijanoznom srčanom bolešću[50] i kod odraslih.[51] Pokazalo se da transfer gena S100A1 u projektovano srčano tkivo povećava kontraktilne performanse tkivnih implantata, sugerirajući da S100A1 može biti efikasan u olakšavanju terapije zamjene srčanog tkiva kod pacijenata sa srčanom insuficijencijom.[52] Međutim, ostaje da se utvrdi klinička efikasnost ove strategije.

Osim toga, više lijekova, uključujući Pentamidin,[11] Amlexanox, Olopatadin, Cromolyn, i Propanolol,[11] Poznato je da sevezuju za S100A1, iako su njihovi afiniteti često u srednjem mikromolarnom rasponu.

Interakcije

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S100 ima interakcije sa:

Reference

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  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000044080 - Ensembl, maj 2017
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  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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