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{{protein
{{Infobox_gene}}
| Name =  
'''Alpha 2-antiplasmin''' (or '''α<sub>2</sub>-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.<ref name="entrez">{{cite web | title = Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5345| accessdate = }}</ref>
| caption =  
| image =
| width =
| HGNCid = 9075
| Symbol = SERPINF2
| AltSymbols = PLI
| EntrezGene = 5345
| OMIM = 262850
| RefSeq = NM_000934
| UniProt = P08697
| PDB =
| ECnumber =
| Chromosome = 17
| Arm = p
| Band =
| LocusSupplementaryData = ter-p12
}}
{{SI}}
{{CMG}}


[[Image:Fibrinolysis.png|thumb|Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.]]


== Role in disease ==


'''Alpha 2-antiplasmin''' (or '''α<sub>2</sub>-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.
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.<ref>Sattar, Husain. ''Fundamentals of Pathology''. Pathoma LLC, 2011, p. 36.</ref>
 
== Interactions ==


[[Image:Fibrinolysis.png|center|frame|Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.]]
Alpha 2-antiplasmin has been shown to [[Protein-protein interaction|interact]] with:
* [[Neutrophil elastase]]<ref name = pmid2437112/><ref name = pmid6980881>{{cite journal | vauthors = Brower MS, Harpel PC | title = Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase | journal = The Journal of Biological Chemistry | volume = 257 | issue = 16 | pages = 9849–54 | date = Aug 1982 | pmid = 6980881 | doi =  }}</ref> and
* [[Plasmin]].<ref name = pmid2437112>{{cite journal | vauthors = Shieh BH, Travis J | title = The reactive site of human alpha 2-antiplasmin | journal = The Journal of Biological Chemistry | volume = 262 | issue = 13 | pages = 6055–9 | date = May 1987 | pmid = 2437112 | doi =  }}</ref><ref name = pmid158022>{{cite journal | vauthors = Wiman B, Collen D | title = On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin | journal = The Journal of Biological Chemistry | volume = 254 | issue = 18 | pages = 9291–7 | date = Sep 1979 | pmid = 158022 | doi =  }}</ref>


==Role in disease==
== See also ==
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.
* [[Serpin]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Martí-Fàbregas J, Borrell M, Cocho D, Martínez-Ramírez S, Martínez-Corral M, Fontcuberta J, Martí-Vilalta JL | title = Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization | journal = Stroke: A Journal of Cerebral Circulation | volume = 39 | issue = 1 | pages = 234–6  | date = Jan 2008 | pmid = 18048863 | doi = 10.1161/STROKEAHA.107.493767 | name-list-format = vanc }}
* {{cite journal | vauthors = Nielsen VG | title = Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions | journal = Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis | volume = 18 | issue = 7 | pages = 647–56  | date = Oct 2007 | pmid = 17890952 | doi = 10.1097/MBC.0b013e3282a167dc }}
* {{cite journal | vauthors = Sazonova IY, Thomas BM, Gladysheva IP, Houng AK, Reed GL | title = Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate | journal = Journal of Thrombosis and Haemostasis : JTH | volume = 5 | issue = 10 | pages = 2087–94  | date = Oct 2007 | pmid = 17883703 | doi = 10.1111/j.1538-7836.2007.02652.x | name-list-format = vanc }}
* {{cite journal | vauthors = Mutch NJ, Thomas L, Moore NR, Lisiak KM, Booth NA | title = TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots | journal = Journal of Thrombosis and Haemostasis : JTH | volume = 5 | issue = 4 | pages = 812–7  | date = Apr 2007 | pmid = 17388801 | doi = 10.1111/j.1538-7836.2007.02430.x | name-list-format = vanc }}
* {{cite journal | vauthors = Christiansen VJ, Jackson KW, Lee KN, McKee PA | title = The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity | journal = Blood | volume = 109 | issue = 12 | pages = 5286–92  | date = Jun 2007 | pmid = 17317851 | pmc = 1890835 | doi = 10.1182/blood-2007-01-065185 }}
* {{cite journal | vauthors = Hayashido Y, Hamana T, Ishida Y, Shintani T, Koizumi K, Okamoto T | title = 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 | journal = Oncology Reports | volume = 17 | issue = 2 | pages = 417–23  | date = Feb 2007 | pmid = 17203182 | doi = 10.3892/or.17.2.417 | name-list-format = vanc }}
* {{cite journal | vauthors = Shibata N, Kawarai T, Meng Y, Lee JH, Lee HS, Wakutani Y, Shibata E, Pathan N, Bi A, Sato C, Sorbi S, Bruni AC, Duara R, Mayeux R, Farrer LA, George-Hyslop PS, Rogaeva E | title = Association studies between the plasmin genes and late-onset Alzheimer's disease | journal = Neurobiology of Aging | volume = 28 | issue = 7 | pages = 1041–3  | date = Jul 2007 | pmid = 16828203 | pmc = 2647723 | doi = 10.1016/j.neurobiolaging.2006.05.028 | name-list-format = vanc }}
* {{cite journal | vauthors = Liu T, Qian WJ, Gritsenko MA, Camp DG, Monroe ME, Moore RJ, Smith RD | title = Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry | journal = Journal of Proteome Research | volume = 4 | issue = 6 | pages = 2070–80 | year = 2006 | pmid = 16335952 | pmc = 1850943 | doi = 10.1021/pr0502065 | name-list-format = vanc }}
* {{cite journal | vauthors = Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA | title = A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion | journal = Blood | volume = 103 | issue = 10 | pages = 3783–8  | date = May 2004 | pmid = 14751930 | doi = 10.1182/blood-2003-12-4240 | name-list-format = vanc }}
* {{cite journal | vauthors = Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, Veenstra TD, Adkins JN, Pounds JG, Fagan R, Lobley A | title = The human plasma proteome: a nonredundant list developed by combination of four separate sources | journal = Molecular & Cellular Proteomics | volume = 3 | issue = 4 | pages = 311–26  | date = Apr 2004 | pmid = 14718574 | doi = 10.1074/mcp.M300127-MCP200 | name-list-format = vanc }}
* {{cite journal | vauthors = Kapadia C, Yousef GM, Mellati AA, Magklara A, Wasney GA, Diamandis EP | title = Complex formation between human kallikrein 13 and serum protease inhibitors | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 339 | issue = 1-2 | pages = 157–67  | date = Jan 2004 | pmid = 14687906 | doi = 10.1016/j.cccn.2003.10.009 | name-list-format = vanc }}
* {{cite journal | vauthors = Matsuno H, Okada K, Ueshima S, Matsuo O, Kozawa O | title = Alpha2-antiplasmin plays a significant role in acute pulmonary embolism | journal = Journal of Thrombosis and Haemostasis : JTH | volume = 1 | issue = 8 | pages = 1734–9 | year = 2004 | date = Aug 2003 | pmid = 12911586 | doi = 10.1046/j.1538-7836.2003.00252.x | name-list-format = vanc }}
* {{cite journal | vauthors = Magklara A, Mellati AA, Wasney GA, Little SP, Sotiropoulou G, Becker GW, Diamandis EP | title = Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors | journal = Biochemical and Biophysical Research Communications | volume = 307 | issue = 4 | pages = 948–55  | date = Aug 2003 | pmid = 12878203 | doi = 10.1016/S0006-291X(03)01271-3 | name-list-format = vanc }}
* {{cite journal | vauthors = Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH | title = 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 | journal = American Journal of Human Genetics | volume = 72 | issue = 4 | pages = 918–30  | date = Apr 2003 | pmid = 12621583 | pmc = 1180354 | doi = 10.1086/374320 | name-list-format = vanc }}
* {{cite journal | vauthors = Frank PS, Douglas JT, Locher M, Llinás M, Schaller J | title = Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide | journal = Biochemistry | volume = 42 | issue = 4 | pages = 1078–85  | date = Feb 2003 | pmid = 12549929 | doi = 10.1021/bi026917n | name-list-format = vanc }}
* {{cite journal | vauthors = Turner RB, Liu L, Sazonova IY, Reed GL | title = Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin | journal = The Journal of Biological Chemistry | volume = 277 | issue = 36 | pages = 33068–74  | date = Sep 2002 | pmid = 12080056 | doi = 10.1074/jbc.M203782200 }}
* {{cite journal | vauthors = Askew YS, Pak SC, Luke CJ, Askew DJ, Cataltepe S, Mills DR, Kato H, Lehoczky J, Dewar K, Birren B, Silverman GA | title = SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases | journal = The Journal of Biological Chemistry | volume = 276 | issue = 52 | pages = 49320–30 | year = 2002 | date = Dec 2001 | pmid = 11604408 | doi = 10.1074/jbc.M108879200 | name-list-format = vanc }}
* {{cite journal | vauthors = Uszynski M, Klyszejko A, Zekanowska E | title = Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women | journal = European Journal of Obstetrics, Gynecology, and Reproductive Biology | volume = 93 | issue = 2 | pages = 167–71 | year = 2001 | date = Dec 2000 | pmid = 11074138 | doi = 10.1016/S0301-2115(00)00283-9 }}
* {{cite journal | vauthors = Hevessy Z, Patthy A, Kárpáti L, Muszbek L | title = alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study | journal = [[Thrombosis Research]] | volume = 99 | issue = 4 | pages = 399–406  | date = Aug 2000 | pmid = 10963790 | doi = 10.1016/S0049-3848(00)00261-9 }}
{{refend}}


==External links==
== External links ==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=I04.023 I04.023]
* {{MeshName|alpha-2+Antiplasmin}}
* {{MeshName|alpha-2+Antiplasmin}}
* {{MeshName|SERPINF2+protein,+human}}
* {{UCSC gene info|SERPINF2}}


{{Coagulation}}
{{Coagulation}}
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[[Category:Serine protease inhibitors]]
[[Category:Serine protease inhibitors]]
[[Category:Fibrinolytic system]]
[[Category:Fibrinolytic system]]
[[Category:Hematology]]
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{{WikiDoc Sources}}

Revision as of 01:14, 16 November 2017

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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.[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

External links

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