Alpha 1-antichymotrypsin

Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3
	; PDB rendering based on 1as4.
Available structures
PDB	1AS4, 1QMN, 2ACH, 3CAA, 3DLW, 4CAA
Identifiers
Symbols	SERPINA3; AACT; ACT; GIG25; MGC88254
External IDs	OMIM: 107280 MGI: 105045 HomoloGene: 111129 GeneCards: SERPINA3 Gene
Gene Ontology
Molecular function	• DNA binding; • serine-type endopeptidase inhibitor activity; • serine-type endopeptidase inhibitor activity; • protein binding; • peptidase inhibitor activity;
Cellular component	• extracellular region; • extracellular region; • intracellular; • nucleus;
Biological process	• acute-phase response; • inflammatory response; • negative regulation of endopeptidase activity; • regulation of lipid metabolic process; • regulation of proteolysis; • maintenance of gastrointestinal epithelium;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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Alpha 1-antichymotrypsin is an alpha globulin glycoprotein that is a member of the serpin superfamily.

It 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.^[1]

This protein is produced in the liver, and is an acute phase protein that is induced during inflammation. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease.^[2]

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

[edit] Interactions

Alpha 1-antichymotrypsin has been shown to interact with DNAJC1.^[3]

[edit] References

^ ^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.
^ "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=12.
^ Kroczynska, Barbara; Evangelista Christina M, Samant Shalaka S, Elguindi Ebrahim C, Blond Sylvie Y (Mar. 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. (United States) 279 (12): 11432–43. doi:10.1074/jbc.M310903200. ISSN 0021-9258. PMC 1553221. PMID 14668352. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1553221.

[edit] Further reading

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.

[edit] External links

The MEROPS online database for peptidases and their inhibitors: I04.002
MeSH Alpha+1-antichymotrypsin

This article on a gene on chromosome 14 is a stub. You can help Wikipedia by expanding it.

[kalsheker-0] 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.

[1] "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=12.

[pmid14668352-2] Kroczynska, Barbara; Evangelista Christina M, Samant Shalaka S, Elguindi Ebrahim C, Blond Sylvie Y (Mar. 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. (United States) 279 (12): 11432–43. doi:10.1074/jbc.M310903200. ISSN 0021-9258. PMC 1553221. PMID 14668352. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1553221.

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Alpha 1-antichymotrypsin

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