Alpha 2-antiplasmin

Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
Identifiers
Symbols	SERPINF2; A2AP; AAP; ALPHA-2-PI; API; PLI
External IDs	OMIM: 613168 MGI: 107173 HomoloGene: 719 GeneCards: SERPINF2 Gene
Gene Ontology Molecular function • protease binding • endopeptidase inhibitor activity • serine-type endopeptidase inhibitor activity • serine-type endopeptidase inhibitor activity • serine-type endopeptidase inhibitor activity • protein binding Cellular component • extracellular region • extracellular region • extracellular space • platelet alpha granule lumen Biological process • platelet degranulation • acute-phase response • blood coagulation • response to organic substance • negative regulation of endopeptidase activity • negative regulation of endopeptidase activity • regulation of proteolysis • platelet activation • fibrinolysis • negative regulation of fibrinolysis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5345	18816
Ensembl	ENSG00000167711	ENSMUSG00000038224
UniProt	P08697	Q5ND35
RefSeq (mRNA)	NM_000934.3	NM_008878.2
RefSeq (protein)	NP_000925.2	NP_032904.1
Location (UCSC)	Chr 17: 1.65 – 1.66 Mb	Chr 11: 75.25 – 75.25 Mb
PubMed search	[1]	[2]

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.

Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.

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.

Interactions

Alpha 2-antiplasmin has been shown to interact with Plasmin and Neutrophil elastase.

See also

• Serpin

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. http://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. http://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. http://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. http://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. http://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
• MeSH alpha-2+Antiplasmin
• MeSH SERPINF2+protein,+human