Movatterモバイル変換


[0]ホーム

URL:


Jump to content
WikipediaThe Free Encyclopedia
Search

Alpha 2-antiplasmin

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens
SERPINF2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2R9Y

Identifiers
AliasesSERPINF2, A2AP, AAP, ALPHA-2-PI, API, PLI, serpin family F member 2, alpha2AP
External IDsOMIM:613168;MGI:107173;HomoloGene:719;GeneCards:SERPINF2;OMA:SERPINF2 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for SERPINF2
Genomic location for SERPINF2
Band17p13.3Start1,742,836bp[1]
End1,755,265bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for SERPINF2
Genomic location for SERPINF2
Band11|11 B5Start75,322,558bp[2]
End75,330,417bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • left uterine tube

  • prostate

  • upper lobe of left lung

  • human kidney

  • right ovary

  • lactiferous gland

  • right testis

  • right lobe of thyroid gland

  • myometrium
Top expressed in
  • yolk sac

  • liver

  • right kidney

  • proximal tubule

  • left lobe of liver

  • human kidney

  • gallbladder

  • fetal liver hematopoietic progenitor cell

  • abdominal wall

  • human fetus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5345

18816

Ensembl

ENSG00000167711
ENSG00000276838

ENSMUSG00000038224

UniProt

P08697

Q61247

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: 75.32 – 75.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha 2-antiplasmin (orα2-antiplasmin orplasmin inhibitor) is aserine protease inhibitor (serpin) responsible for inactivatingplasmin.[5] Plasmin is an importantenzyme that participates infibrinolysis and degradation of various other proteins. This protein is encoded by theSERPINF2 gene.[6]

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

Role in disease

[edit]

Very few cases (<20) ofalpha-2-antiplasmin 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 livercirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation ofplasmin and an increase infibrinolysis. This is associated with an increased risk of bleeding in liver disease.[7] It has been suggested, however, that the observed decreases in alpha 2-antiplasmin levels are due to a chronic state ofdisseminated intravascular coagulation in cirrhosis rather than defective protein synthesis.[8]

Interactions

[edit]

Alpha 2-antiplasmin has been shown tointeract with:

See also

[edit]

References

[edit]
  1. ^abcENSG00000276838 GRCh38: Ensembl release 89: ENSG00000167711, ENSG00000276838Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000038224Ensembl, 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 G, Quek AJ, Caradoc-Davies TT, Ekkel SM, Mazzitelli B, Whisstock JC, Law RH (2019-03-05). "Structural studies of plasmin inhibition".Biochemical Society Transactions.47 (2):541–557.doi:10.1042/bst20180211.ISSN 0300-5127.PMID 30837322.S2CID 73463150.
  6. ^"Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2".
  7. ^Sattar H (2011).Fundamentals of Pathology. Pathoma LLC. p. 36.ISBN 978-0983224600.
  8. ^Marongiu F, Mamusa AM, Mameli G, Mulas G, Solinas A, Demelia L, Contu L (1985). "α2Antiplasmin and Disseminated Intravascular Coagulation in Liver Cirrhosis".Thrombosis Research.37 (2):287–294.doi:10.1016/0049-3848(85)90017-9.PMID 3975873.
  9. ^abShieh BH, Travis J (May 1987)."The reactive site of human alpha 2-antiplasmin".The Journal of Biological Chemistry.262 (13):6055–9.doi:10.1016/S0021-9258(18)45536-6.PMID 2437112.
  10. ^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.doi:10.1016/S0021-9258(18)34149-8.PMID 6980881.
  11. ^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.doi:10.1016/S0021-9258(19)86843-6.PMID 158022.

Further reading

[edit]

External links

[edit]
Coagulation factors
Primary hemostasis
(platelet activation)
Intrinsic pathway
(contact activation)
Extrinsic pathway
(tissue factor)
Common pathway
Anticoagulant factors
Fibrinolytic factors
Coagulation markers
Platelet activation
Thrombin generation
Fibrin generation
Fibrinolysis
inhibitory
Cross class inhibitory
noninhibitory
Serumglobulins
Alpha globulins
serpins:
carrier proteins:
other:
Beta globulins
carrier proteins:
other:
Gamma globulin
Other
Other globulins
Albumins
Egg white
Serum albumin
Other
Retrieved from "https://en.wikipedia.org/w/index.php?title=Alpha_2-antiplasmin&oldid=1282762725"
Categories:
Hidden categories:

[8]ページ先頭

©2009-2025 Movatter.jp