Alpha 1-antichymotrypsin
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SERPINA3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | SERPINA3, AACT, ACT, GIG24, GIG25, serpin family A member 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 107280 MGI: 98377 HomoloGene: 111129 GeneCards: SERPINA3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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[edit]
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[edit]
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[edit]
Alpha 1-antichymotrypsin has been shown to interact with DNAJC1.[8]
See also[edit]
- Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory proteases
References[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000196136 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058207 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ 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.
- ^ "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3".
- ^ 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[edit]
- Janciauskiene S, Wright HT (1999). "Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of Alzheimer's disease". BioEssays. 20 (12): 1039–46. doi:10.1002/(SICI)1521-1878(199812)20:12<1039::AID-BIES10>3.0.CO;2-Z. PMID 10048303.
- Kalsheker N, Morley S, Morgan K (2002). "Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin". Biochem. Soc. Trans. 30 (2): 93–8. doi:10.1042/BST0300093. PMID 12023832.
External links[edit]
- The MEROPS online database for peptidases and their inhibitors: I04.002
- Alpha+1-antichymotrypsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Human SERPINA3 genome location and SERPINA3 gene details page in the UCSC Genome Browser.
- Overview of all the structural information available in the PDB for UniProt: P01011 (Human Alpha-1-antichymotrypsin) at the PDBe-KB.