Alpha 2-antiplasmin

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SERPINF2
2R9Y.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSERPINF2, A2AP, AAP, ALPHA-2-PI, API, PLI, serpin family F member 2
External IDsOMIM: 613168 MGI: 107173 HomoloGene: 719 GeneCards: SERPINF2
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for SERPINF2
Genomic location for SERPINF2
Band17p13.3Start1,742,836 bp[1]
End1,755,268 bp[1]
RNA expression pattern
PBB GE SERPINF2 205075 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000934
NM_001165920
NM_001165921

NM_008878

RefSeq (protein)

NP_000925
NP_001159392
NP_001159393

NP_032904

Location (UCSC)Chr 17: 1.74 – 1.76 MbChr 11: 75.43 – 75.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin.[5] Plasmin is an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.[6]

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

Role in disease[edit]

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.[7]

Interactions[edit]

Alpha 2-antiplasmin has been shown to interact with:

See also[edit]

References[edit]

  1. ^ a b c ENSG00000276838 GRCh38: Ensembl release 89: ENSG00000167711, ENSG00000276838 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038224 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wu, Guojie; Quek, Adam J.; Caradoc-Davies, Tom T.; Ekkel, Sue M.; Mazzitelli, Blake; Whisstock, James C.; Law, Ruby H.P. (2019-03-05). "Structural studies of plasmin inhibition". Biochemical Society Transactions. 47 (2): 541–557. doi:10.1042/bst20180211. ISSN 0300-5127.
  6. ^ "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2".
  7. ^ Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.
  8. ^ a b 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.
  9. ^ 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.
  10. ^ 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[edit]

External links[edit]