Biology:Alpha 2-antiplasmin

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Alpha 2-antiplasmin (or α₂-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin. Plasmin is 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.

In liver cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of plasmin and an increase in fibrinolysis. This is associated with an increase risk of bleeding in liver disease.

Interactions

Alpha 2-antiplasmin has been shown to interact with:

• Neutrophil elastase and
• Plasmin.

See also

• Serpin

Further reading

• "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization". Stroke: A Journal of Cerebral Circulation 39 (1): 234–6. Jan 2008. doi:10.1161/STROKEAHA.107.493767. PMID 18048863. 
• "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagulation & Fibrinolysis 18 (7): 647–56. Oct 2007. doi:10.1097/MBC.0b013e3282a167dc. PMID 17890952. 
• "Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate". Journal of Thrombosis and Haemostasis 5 (10): 2087–94. Oct 2007. doi:10.1111/j.1538-7836.2007.02652.x. PMID 17883703. 
• "TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots". Journal of Thrombosis and Haemostasis 5 (4): 812–7. Apr 2007. doi:10.1111/j.1538-7836.2007.02430.x. PMID 17388801. 
• "The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity". Blood 109 (12): 5286–92. Jun 2007. doi:10.1182/blood-2007-01-065185. PMID 17317851. 
• "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". Oncology Reports 17 (2): 417–23. Feb 2007. doi:10.3892/or.17.2.417. PMID 17203182. 
• "Association studies between the plasmin genes and late-onset Alzheimer's disease". Neurobiology of Aging 28 (7): 1041–3. Jul 2007. doi:10.1016/j.neurobiolaging.2006.05.028. PMID 16828203. 
• "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research 4 (6): 2070–80. December 2005. doi:10.1021/pr0502065. PMID 16335952. 
• "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion". Blood 103 (10): 3783–8. May 2004. doi:10.1182/blood-2003-12-4240. PMID 14751930. 
• "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Molecular & Cellular Proteomics 3 (4): 311–26. Apr 2004. doi:10.1074/mcp.M300127-MCP200. PMID 14718574. 
• "Complex formation between human kallikrein 13 and serum protease inhibitors". Clinica Chimica Acta; International Journal of Clinical Chemistry 339 (1–2): 157–67. Jan 2004. doi:10.1016/j.cccn.2003.10.009. PMID 14687906. 
• "Alpha2-antiplasmin plays a significant role in acute pulmonary embolism". Journal of Thrombosis and Haemostasis 1 (8): 1734–9. Aug 2003. doi:10.1046/j.1538-7836.2003.00252.x. PMID 12911586. 
• "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors". Biochemical and Biophysical Research Communications 307 (4): 948–55. Aug 2003. doi:10.1016/S0006-291X(03)01271-3. PMID 12878203. 
• "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". American Journal of Human Genetics 72 (4): 918–30. Apr 2003. doi:10.1086/374320. PMID 12621583. 
• "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry 42 (4): 1078–85. Feb 2003. doi:10.1021/bi026917n. PMID 12549929. 
• "Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin". The Journal of Biological Chemistry 277 (36): 33068–74. Sep 2002. doi:10.1074/jbc.M203782200. PMID 12080056. 
• "SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases". The Journal of Biological Chemistry 276 (52): 49320–30. Dec 2001. doi:10.1074/jbc.M108879200. PMID 11604408. 
• "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women". European Journal of Obstetrics, Gynecology, and Reproductive Biology 93 (2): 167–71. Dec 2000. doi:10.1016/S0301-2115(00)00283-9. PMID 11074138. 
• "alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study". Thrombosis Research 99 (4): 399–406. Aug 2000. 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)
• Human SERPINF2 genome location and SERPINF2 gene details page in the UCSC Genome Browser.