Alpha 2-antiplasmin

Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
Identifiers
SymbolsSERPINF2 ; A2AP; AAP; ALPHA-2-PI; API; PLI
External IDsOMIM: 613168 MGI: 107173 HomoloGene: 719 GeneCards: SERPINF2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez534518816
EnsemblENSG00000167711ENSMUSG00000038224
UniProtP08697Q61247
RefSeq (mRNA)NM_000934NM_008878
RefSeq (protein)NP_000925NP_032904
Location (UCSC)Chr 17:
1.65 – 1.66 Mb		Chr 11:
75.43 – 75.44 Mb
PubMed search

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.

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. [2]

Interactions

Alpha 2-antiplasmin has been shown to interact with:

See also

References

  1. ↑ "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2".
  2. ↑ Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.
  3. ↑ 3.0 3.1 Shieh BH, Travis J (May 1987). "The reactive site of human alpha 2-antiplasmin". The Journal of Biological Chemistry 262 (13): 6055–9. PMID 2437112.
  4. ↑ Brower MS, Harpel PC (Aug 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase". The Journal of Biological Chemistry 257 (16): 9849–54. PMID 6980881.
  5. ↑ Wiman B, Collen D (Sep 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". The Journal of Biological Chemistry 254 (18): 9291–7. PMID 158022.

Further reading

  • Martí-Fàbregas J, Borrell M, Cocho D, Martínez-Ramírez S, Martínez-Corral M, Fontcuberta J et al. (Jan 2008). "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. doi:10.1161/STROKEAHA.107.493767. PMID 18048863.
  • Nielsen VG (Oct 2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis 18 (7): 647–56. doi:10.1097/MBC.0b013e3282a167dc. PMID 17890952.
  • Sazonova IY, Thomas BM, Gladysheva IP, Houng AK, Reed GL (Oct 2007). "Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate". Journal of Thrombosis and Haemostasis : JTH 5 (10): 2087–94. doi:10.1111/j.1538-7836.2007.02652.x. PMID 17883703.
  • Mutch NJ, Thomas L, Moore NR, Lisiak KM, Booth NA (Apr 2007). "TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots". Journal of Thrombosis and Haemostasis : JTH 5 (4): 812–7. doi:10.1111/j.1538-7836.2007.02430.x. PMID 17388801.
  • Christiansen VJ, Jackson KW, Lee KN, McKee PA (Jun 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. PMC 1890835. PMID 17317851.
  • Hayashido Y, Hamana T, Ishida Y, Shintani T, Koizumi K, Okamoto T (Feb 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". Oncology Reports 17 (2): 417–23. doi:10.3892/or.17.2.417. PMID 17203182.
  • Shibata N, Kawarai T, Meng Y, Lee JH, Lee HS, Wakutani Y et al. (Jul 2007). "Association studies between the plasmin genes and late-onset Alzheimer's disease". Neurobiology of Aging 28 (7): 1041–3. doi:10.1016/j.neurobiolaging.2006.05.028. PMC 2647723. PMID 16828203.
  • Liu T, Qian WJ, Gritsenko MA, Camp DG, Monroe ME, Moore RJ et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
  • Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA (May 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, Gatlin T, Tirumalai RS, Conrads TP et al. (Apr 2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Molecular & Cellular Proteomics : MCP 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
  • Kapadia C, Yousef GM, Mellati AA, Magklara A, Wasney GA, Diamandis EP (Jan 2004). "Complex formation between human kallikrein 13 and serum protease inhibitors". Clinica Chimica Acta; International Journal of Clinical Chemistry 339 (1-2): 157–67. doi:10.1016/j.cccn.2003.10.009. PMID 14687906.
  • Matsuno H, Okada K, Ueshima S, Matsuo O, Kozawa O (Aug 2003). "Alpha2-antiplasmin plays a significant role in acute pulmonary embolism". Journal of Thrombosis and Haemostasis : JTH 1 (8): 1734–9. doi:10.1046/j.1538-7836.2003.00252.x. PMID 12911586. Check date values in: |year= / |date= mismatch (help)
  • Magklara A, Mellati AA, Wasney GA, Little SP, Sotiropoulou G, Becker GW et al. (Aug 2003). "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. doi:10.1016/S0006-291X(03)01271-3. PMID 12878203.
  • Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A et al. (Apr 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". American Journal of Human Genetics 72 (4): 918–30. doi:10.1086/374320. PMC 1180354. PMID 12621583.
  • Frank PS, Douglas JT, Locher M, Llinás M, Schaller J (Feb 2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry 42 (4): 1078–85. doi:10.1021/bi026917n. PMID 12549929.
  • Turner RB, Liu L, Sazonova IY, Reed GL (Sep 2002). "Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin". The Journal of Biological Chemistry 277 (36): 33068–74. doi:10.1074/jbc.M203782200. PMID 12080056.
  • Askew YS, Pak SC, Luke CJ, Askew DJ, Cataltepe S, Mills DR et al. (Dec 2001). "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. doi:10.1074/jbc.M108879200. PMID 11604408. Check date values in: |year= / |date= mismatch (help)
  • Uszynski M, Klyszejko A, Zekanowska E (Dec 2000). "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. doi:10.1016/S0301-2115(00)00283-9. PMID 11074138. Check date values in: |year= / |date= mismatch (help)
  • Hevessy Z, Patthy A, Kárpáti L, Muszbek L (Aug 2000). "alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study". Thrombosis Research 99 (4): 399–406. doi:10.1016/S0049-3848(00)00261-9. PMID 10963790.

External links