Alfa 1-antitripsin

Inhibitor serpinske peptidaze, grupa A (alfa-1 antiproteinaza, antitripsin), član 1
Inhibitor serpinske peptidaze, grupa A (alfa-1 antiproteinaza, antitripsin), član 1
	Kristalna struktura serpina A1 (red) u inhibitornom kompleksu sa pankreatičkom elastazom (plavo). Prikaz je baziran na 2D26.
Dostupne strukture
	1ATU, 1D5S, 1EZX, 1HP7, 1IZ2, 1KCT, 1OO8, 1OPH, 1PSI, 1QLP, 1QMB, 2D26, 2QUG, 3CWL, 3CWM, 3DRM, 3DRU, 3NDD, 3NDF, 3NE4, 3T1P, 7API, 8API, 9API
Identifikatori
Simboli	SERPINA1; A1A; A1AT; AAT; PI; PI1; PRO2275; alpha1AT
Vanjski ID	OMIM: 107400 MGI: 891971 HomoloGene: 20103 GeneCards: SERPINA1 Gene
Ontologija gena
Molekularna funkcija	• vezivanje proteaze; • aktivnost inhibitora serinskog tipa endopeptidaze; • proteinsko vezivanje;
Celularna komponenta	• ekstracelularni region; • proteinski ekstracelularni matriks; • ekstracelularni prostor;
Biološki proces	• respons na hipoksiju; • degranulacija trombocita; • respons akutne faze;
Pregled RNK izražavanja
	podaci
Ortolozi
Vrsta	Čovek
Entrez	5265
Ensembl	ENSG00000197249
UniProt	P01009
RefSeq (mRNA)	NM_000295
RefSeq (protein)	NP_000286
Lokacija (UCSC)	Chr 14:; 94.84 - 94.86 Mb
PubMed pretraga	[1]

Alfa 1-antitripsin ili α₁-antitripsin (A1AT) je proteazni inhibitor iz serpinske superfamilije. On je generalno poznat kao serumski tripsinski inhibitor. Alfa 1-antitripsin se takođe naziva alfa-1 proteinazni inhibitor (A1PI), jer inhibira širok opseg proteaza.^[1] On štiti tkiva od enzima inflamatornih ćelija, posebno neutrofilne elastaze, i ima referentni opseg u krvi od 1,5 - 3,5 gram/litre, mada koncentracija može da bude znatno viša nakon akutne inflamacije.^[2] U njegovom odsustvu, neutrofilna elastaza nesmetano razlaže elastin, koji doprinosi elastičnosti pluća, što stvara respiratorne probleme, kao što je emfisema.

Reference уреди

^ Gettins PG (2002). „Serpin structure, mechanism, and function”. Chem Rev. 102 (12): 4751—804. PMID 12475206. doi:10.1021/cr010170.
^ Kushner, Mackiewicz A. (1993). The acute phase response: an overview. Acute-phase glycoproteins: molecular biology, biochemistry and clinical applications. CRC Press. стр. 3—19.

Literatura уреди

Wu Y, Foreman RC (1991). „The molecular genetics of alpha 1 antitrypsin deficiency”. Bioessays. 13 (4): 163—9. PMID 1859394. doi:10.1002/bies.950130404.
Kalsheker N (1989). „Alpha 1-antitrypsin: structure, function and molecular biology of the gene”. Biosci. Rep. 9 (2): 129—38. PMID 2669992. doi:10.1007/BF01115992.
Crystal RG (1990). „The alpha 1-antitrypsin gene and its deficiency states”. Trends Genet. 5 (12): 411—7. PMID 2696185. doi:10.1016/0168-9525(89)90200-X.
Carrell RW; Jeppsson JO; Laurell CB; et al. (1982). „Structure and variation of human alpha 1-antitrypsin”. Nature. 298 (5872): 329—34. PMID 7045697. doi:10.1038/298329a0.
Elliott PR, Abrahams JP, Lomas DA (1998). „Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation”. J. Mol. Biol. 275 (3): 419—25. PMID 9466920. doi:10.1006/jmbi.1997.1458.
Miyamoto Y, Akaike T, Maeda H (2000). „S-nitrosylated human alpha(1)-protease inhibitor”. Biochim. Biophys. Acta. 1477 (1–2): 90—7. PMID 10708851. doi:10.1016/S0167-4838(99)00264-2.
Coakley RJ, Taggart C, O'Neill S, McElvaney NG (2001). „Alpha1-antitrypsin deficiency: biological answers to clinical questions”. Am. J. Med. Sci. 321 (1): 33—41. PMID 11202478. doi:10.1097/00000441-200101000-00006.
Lomas DA, Lourbakos A, Cumming SA, Belorgey D (2002). „Hypersensitive mousetraps, alpha1-antitrypsin deficiency and dementia”. Biochem. Soc. Trans. 30 (2): 89—92. PMID 12023831. doi:10.1042/BST0300089.
Kalsheker N, Morley S, Morgan K (2002). „Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin”. Biochem. Soc. Trans. 30 (2): 93—8. PMID 12023832. doi:10.1042/BST0300093.
Perlmutter DH (2003). „Liver injury in α1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury”. J. Clin. Invest. 110 (11): 1579—83. PMC 151639  . PMID 12464659. doi:10.1172/JCI16787.
Lomas DA, Mahadeva R (2003). „α1-Antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy”. J. Clin. Invest. 110 (11): 1585—90. PMC 151637  . PMID 12464660. doi:10.1172/JCI16782.
Lisowska-Myjak B (2005). „AAT as a diagnostic tool”. Clin. Chim. Acta. 352 (1–2): 1—13. PMID 15653097. doi:10.1016/j.cccn.2004.03.012.
Lomas DA (2005). „Molecular mousetraps, alpha1-antitrypsin deficiency and the serpinopathies”. Clinical medicine (London, England). 5 (3): 249—57. PMID 16011217.
Rudnick DA, Perlmutter DH (2005). „Alpha-1-antitrypsin deficiency: a new paradigm for hepatocellular carcinoma in genetic liver disease”. Hepatology. 42 (3): 514—21. PMID 16044402. doi:10.1002/hep.20815.
Mahr AD, Neogi T, Merkel PA (2006). „Epidemiology of Wegener's granulomatosis: Lessons from descriptive studies and analyses of genetic and environmental risk determinants”. Clin. Exp. Rheumatol. 24 (2 Suppl 41): S82—91. PMID 16859601.
González-Sagrado M, López-Hernández S, Martín-Gil FJ, et al. (2000). "Alpha1-antitrypsin deficiencies masked by a clinical capillary electrophoresis system (CZE 2000)". Clinical Biochemistry, 33(1):79–80

Spoljašnje veze уреди

Alpha 1-antitrypsin
The MEROPS online database for peptidases and their inhibitors: I04.001 Архивирано на сајту Wayback Machine (1. април 2008)
Proteopedia: Alpha-1-antitrypsin

[Gettins_2002-1] Gettins PG (2002). „Serpin structure, mechanism, and function”. Chem Rev. 102 (12): 4751—804. PMID 12475206. doi:10.1021/cr010170.

[Kushner_1993-2] Kushner, Mackiewicz A. (1993). The acute phase response: an overview. Acute-phase glycoproteins: molecular biology, biochemistry and clinical applications. CRC Press. стр. 3—19.

[1]

[2]