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Alpha 1-antichymotrypsin

From Wikipedia, the free encyclopedia
SERPINA3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSERPINA3, AACT, ACT, GIG24, GIG25, serpin family A member 3
External IDsOMIM: 107280; MGI: 98377; HomoloGene: 111129; GeneCards: SERPINA3; OMA:SERPINA3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001085

NM_011458

RefSeq (protein)

NP_001076

NP_035588

Location (UCSC)Chr 14: 94.61 – 94.62 MbChr 12: 104.3 – 104.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha 1-antichymotrypsin (symbol α1AC,[5] A1AC, or a1ACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene.

Function

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Alpha 1-antichymotrypsin inhibits the activity of certain enzymes called proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes.[6]

This protein is produced in the liver, and is an acute phase protein that is induced during inflammation.

Clinical significance

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Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease.[7]

Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimer's disease as it enhances the formation of amyloid-fibrils in this disease.[6]

Interactions

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Alpha 1-antichymotrypsin has been shown to interact with DNAJC1.[8]

See also

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  • Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory proteases

References

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  1. ^ Jump up to: a b c GRCh38: Ensembl release 89: ENSG00000196136Ensembl, May 2017
  2. ^ Jump up to: a b c GRCm38: Ensembl release 89: ENSMUSG00000058207Ensembl, 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. ^ Logan, Carolynn M.; Rice, M. Katherine (1987). Logan's Medical and Scientific Abbreviations. Philadelphia: J. B. Lippincott Company. p. 3. ISBN 0-397-54589-4.
  6. ^ Jump up to: a b Kalsheker N (1996). "Alpha 1-antichymotrypsin". Int. J. Biochem. Cell Biol. 28 (9): 961–4. doi:10.1016/1357-2725(96)00032-5. PMID 8930118. S2CID 11230631.
  7. ^ "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3".
  8. ^ Kroczynska B, Evangelista CM, Samant SS, Elguindi EC, Blond SY (March 2004). "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity". J. Biol. Chem. 279 (12): 11432–43. doi:10.1074/jbc.M310903200. PMC 1553221. PMID 14668352.

Further reading

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