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Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3
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| PDB rendering based on 1as4. | ||||||||||||||
| Available structures: 1as4, 1qmn, 2ach, 3caa, 4caa | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbols | SERPINA3; AACT; ACT; GIG24; GIG25; MGC88254 | |||||||||||||
| External IDs | OMIM: 107280 MGI: 105045 HomoloGene: 40658 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 12 | 20716 | ||||||||||||
| Ensembl | ENSG00000196136 | ENSMUSG00000021091 | ||||||||||||
| Uniprot | P01011 | Q91WP6 | ||||||||||||
| Refseq | NM_001085 (mRNA) NP_001076 (protein) |
NM_009252 (mRNA) NP_033278 (protein) |
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| Location | Chr 14: 94.15 - 94.16 Mb | Chr 12: 104.81 - 104.82 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Alpha 1-antichymotrypsin is an alpha globulin glycoprotein that is a member of the serine proteinase inhibitor (serpin) family.
It inhibits the activity of certain enzymes called proteinases, 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 enzyme 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]
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Interactions
Alpha 1-antichymotrypsin has been shown to interact with DNAJC1.[3]
References
- ^ a b Kalsheker N (1996). "Alpha 1-antichymotrypsin". Int. J. Biochem. Cell Biol. 28 (9): 961–4. doi:. 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:. ISSN 0021-9258. PMID 14668352.
Further reading
- Janciauskiene S, Wright HT (1999). "Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of Alzheimer's disease.". Bioessays 20 (12): 1039–46. doi:. 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:. PMID 12023832.
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External links
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