Alpha 2-antiplasmin: Wikis


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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 OMIM262850 MGI107173 HomoloGene719 GeneCards: SERPINF2 Gene
RNA expression pattern
PBB GE SERPINF2 205075 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5345 18816
Ensembl ENSG00000167711 ENSMUSG00000038224
UniProt P08697 Q5ND35
RefSeq (mRNA) NM_000934 NM_008878
RefSeq (protein) NP_000925 NP_032904
Location (UCSC) Chr 17:
1.59 - 1.61 Mb
Chr 11:
75.25 - 75.26 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.[1]

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


Contents

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[2][3] and Neutrophil elastase.[4][3]

See also

References

  1. ^ "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.  
  2. ^ Wiman, B; Collen D (Sep. 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.  
  3. ^ 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.  
  4. ^ Brower, M S; Harpel P C (Aug. 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 alpha 2-antiplasmin activity". Blood 109 (12): 5286–92. doi:10.1182/blood-2007-01-065185. PMID 17317851.  
  • 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 Alzheimer's disease". Neurobiol. Aging 28 (7): 1041–3. doi:10.1016/j.neurobiolaging.2006.05.028. PMID 16828203.  
  • 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. PMID 16335952.  
  • 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. PMID 12621583.  
  • 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. PMID 12477932.  
  • 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.  

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