Alpha 2-antiplasmin
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Alpha 2-antiplasmin
Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin, an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.[1]
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Contents
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Role in disease
Very few cases (<20) of A2AP deficiency have been described. As plasmin degrades blood clots, impaired inhibition of plasmin leads to a bleeding tendency, which was severe in the cases reported.
In liver cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of plasmin and a decrease in normal fibrinolysis. [2]
Interactions
Alpha 2-antiplasmin has been shown to interact with Plasmin[3][4] and Neutrophil elastase.[4][5]
See also
References
- ^ "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5345.
- ^ Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.
- ^ Wiman, B; Collen D (September 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. Chem. (UNITED STATES) 254 (18): 9291–7. ISSN 0021-9258. PMID 158022.
- ^ a b Shieh, B H; Travis J (May. 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. (UNITED STATES) 262 (13): 6055–9. ISSN 0021-9258. PMID 2437112.
- ^ Brower, M S; Harpel P C (August 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase". J. Biol. Chem. (UNITED STATES) 257 (16): 9849–54. ISSN 0021-9258. PMID 6980881.
Further reading
- Martí-Fàbregas J, Borrell M, Cocho D et al. (2008). "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization". Stroke 39 (1): 234–6. DOI:10.1161/STROKEAHA.107.493767. PMID 18048863.
- Nielsen VG (2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagul. Fibrinolysis 18 (7): 647–56. DOI:10.1097/MBC.0b013e3282a167dc. PMID 17890952.
- Sazonova IY, Thomas BM, Gladysheva IP et al. (2007). "Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate". J. Thromb. Haemost. 5 (10): 2087–94. DOI:10.1111/j.1538-7836.2007.02652.x. PMID 17883703.
- Mutch NJ, Thomas L, Moore NR et al. (2007). "TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots". J. Thromb. Haemost. 5 (4): 812–7. DOI:10.1111/j.1538-7836.2007.02430.x. PMID 17388801.
- Christiansen VJ, Jackson KW, Lee KN, McKee PA (2007). "The effect of a single nucleotide polymorphism on human α2-antiplasmin activity". Blood 109 (12): 5286–92. DOI:10.1182/blood-2007-01-065185. PMC 1890835. PMID 17317851. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1890835.
- Hayashido Y, Hamana T, Ishida Y et al. (2007). "Induction of alpha2-antiplasmin inhibits E-cadherin processing mediated by the plasminogen activator/plasmin system, leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell-cell adhesion". Oncol. Rep. 17 (2): 417–23. PMID 17203182.
- Shibata N, Kawarai T, Meng Y et al. (2007). "Association studies between the plasmin genes and late-onset Alzhemier's disease". Neurobiol. Aging 28 (7): 1041–3. DOI:10.1016/j.neurobiolaging.2006.05.028. PMC 2647723. PMID 16828203. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2647723.
- Liu T, Qian WJ, Gritsenko MA et al. (2006). "Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry". J. Proteome Res. 4 (6): 2070–80. DOI:10.1021/pr0502065. PMC 1850943. PMID 16335952. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850943.
- Lee KN, Jackson KW, Christiansen VJ et al. (2004). "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion". Blood 103 (10): 3783–8. DOI:10.1182/blood-2003-12-4240. PMID 14751930.
- Anderson NL, Polanski M, Pieper R et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Mol. Cell Proteomics 3 (4): 311–26. DOI:10.1074/mcp.M300127-MCP200. PMID 14718574.
- Kapadia C, Yousef GM, Mellati AA et al. (2004). "Complex formation between human kallikrein 13 and serum protease inhibitors". Clin. Chim. Acta 339 (1–2): 157–67. DOI:10.1016/j.cccn.2003.10.009. PMID 14687906.
- Matsuno H, Okada K, Ueshima S et al. (2004). "Alpha2-antiplasmin plays a significant role in acute pulmonary embolism". J. Thromb. Haemost. 1 (8): 1734–9. DOI:10.1046/j.1538-7836.2003.00252.x. PMID 12911586.
- Magklara A, Mellati AA, Wasney GA et al. (2003). "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors". Biochem. Biophys. Res. Commun. 307 (4): 948–55. DOI:10.1016/S0006-291X(03)01271-3. PMID 12878203.
- Cardoso C, Leventer RJ, Ward HL et al. (2003). "Refinement of a 400-kb Critical Region Allows Genotypic Differentiation between Isolated Lissencephaly, Miller-Dieker Syndrome, and Other Phenotypes Secondary to Deletions of 17p13.3". Am. J. Hum. Genet. 72 (4): 918–30. DOI:10.1086/374320. PMC 1180354. PMID 12621583. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1180354.
- Frank PS, Douglas JT, Locher M et al. (2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry 42 (4): 1078–85. DOI:10.1021/bi026917n. PMID 12549929.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Turner RB, Liu L, Sazonova IY, Reed GL (2002). "Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin". J. Biol. Chem. 277 (36): 33068–74. DOI:10.1074/jbc.M203782200. PMID 12080056.
- Askew YS, Pak SC, Luke CJ et al. (2002). "SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases". J. Biol. Chem. 276 (52): 49320–30. DOI:10.1074/jbc.M108879200. PMID 11604408.
- Uszynski M, Klyszejko A, Zekanowska E (2001). "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women". Eur. J. Obstet. Gynecol. Reprod. Biol. 93 (2): 167–71. DOI:10.1016/S0301-2115(00)00283-9. PMID 11074138.
- Hevessy Z, Patthy A, Kárpáti L, Muszbek L (2000). "alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study". Thromb. Res. 99 (4): 399–406. DOI:10.1016/S0049-3848(00)00261-9. PMID 10963790.
External links
- The MEROPS online database for peptidases and their inhibitors: I04.023
- alpha-2+Antiplasmin at the US National Library of Medicine Medical Subject Headings (MeSH)
- SERPINF2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
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