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'''Alpha 1-antichymotrypsin''' (symbol '''α<sub>1</sub>AC''',<ref name=loganabbrev /> '''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 == | |||
Alpha 1-antichymotrypsin inhibits the activity of certain [[enzyme]]s called [[protease]]s, such as [[cathepsin G]] that is found in [[neutrophil]]s, and [[chymases]] found in [[mast cell]]s, by cleaving them into a different shape or [[Chemical structure|conformation]]. This activity protects some tissues, such as the [[lower respiratory tract]], from damage caused by [[proteolysis|proteolytic]] enzymes.<ref name=kalsheker>{{cite journal |author=Kalsheker N |title=Alpha 1-antichymotrypsin |journal=Int. J. Biochem. Cell Biol. |volume=28 |issue=9 |pages=961–4 |year=1996 |pmid=8930118 |doi=10.1016/1357-2725(96)00032-5}}</ref> | |||
This protein is produced in the [[liver]], and is an [[acute phase protein]] that is induced during [[inflammation]]. | |||
== Clinical significance == | |||
Deficiency of this protein has been associated with [[liver disease]]. Mutations have been identified in patients with [[Parkinson disease]] and [[chronic obstructive pulmonary disease]].<ref>{{cite web | title = Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=12| accessdate = }}</ref> | |||
Alpha 1-antichymotrypsin is also associated with the [[pathogenesis]] of [[Alzheimer's disease]] as it enhances the formation of amyloid-fibrils in this disease.<ref name=kalsheker/> | Alpha 1-antichymotrypsin is also associated with the [[pathogenesis]] of [[Alzheimer's disease]] as it enhances the formation of amyloid-fibrils in this disease.<ref name=kalsheker/> | ||
==Interactions== | |||
Alpha 1-antichymotrypsin has been shown to [[Protein-protein interaction|interact]] with [[DNAJC1]].<ref name="pmid14668352">{{cite journal |vauthors=Kroczynska B, Evangelista CM, Samant SS, Elguindi EC, Blond SY | title = 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 | journal = J. Biol. Chem. | volume = 279 | issue = 12 | pages = 11432–43 |date=March 2004 | pmid = 14668352 | pmc = 1553221 | doi = 10.1074/jbc.M310903200 }}</ref> | |||
==See also== | |||
* [[Alpha-1 antitrypsin]], another serpin that is analogous for protecting the body from excessive effects of its own inflammatory proteases | |||
==References== | ==References== | ||
< | {{reflist | refs= | ||
* <ref name=loganabbrev>{{cite book|author1=Logan, Carolynn M.|author2=Rice, M. Katherine|title=Logan's Medical and Scientific Abbreviations|date=1987|publisher=[[J. B. Lippincott Company]]|location=Philadelphia|isbn=0-397-54589-4|page=3|ref=logansaabrev}}</ref> | |||
}} | |||
==Further reading== | |||
{{refbegin | 2}} | |||
*{{cite journal |vauthors=Janciauskiene S, Wright HT |title=Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of Alzheimer's disease. |journal=BioEssays |volume=20 |issue= 12 |pages= 1039–46 |year= 1999 |pmid= 10048303 |doi= 10.1002/(SICI)1521-1878(199812)20:12<1039::AID-BIES10>3.0.CO;2-Z }} | |||
*{{cite journal |vauthors=Kalsheker N, Morley S, Morgan K |title=Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 93–8 |year= 2002 |pmid= 12023832 |doi= 10.1042/BST0300093 }} | |||
{{refend}} | |||
==External links== | ==External links== | ||
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=I04.002 I04.002] | |||
* {{MeshName|Alpha+1-antichymotrypsin}} | * {{MeshName|Alpha+1-antichymotrypsin}} | ||
* {{UCSC gene info|SERPINA3}} | |||
{{PDB Gallery|geneid=12}} | |||
{{Serpins}} | {{Serpins}} | ||
{{Alpha globulins}} | {{Alpha globulins}} | ||
{{Glycoproteins}} | {{Glycoproteins}} | ||
{{Acute phase proteins}} | {{Acute phase proteins}} | ||
[[ | [[Category:Acute phase proteins]] | ||
{{ | {{gene-14-stub}} | ||
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Alpha 1-antichymotrypsin (symbol α1AC,[1] 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
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.[2]
This protein is produced in the liver, and is an acute phase protein that is induced during inflammation.
Clinical significance
Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease.[3]
Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimer's disease as it enhances the formation of amyloid-fibrils in this disease.[2]
Interactions
Alpha 1-antichymotrypsin has been shown to interact with DNAJC1.[4]
See also
- Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory proteases
References
- ↑ 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.
- ↑ 2.0 2.1 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".
- ↑ 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
- 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
- The MEROPS online database for peptidases and their inhibitors: I04.002
- Alpha+1-antichymotrypsin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human SERPINA3 genome location and SERPINA3 gene details page in the UCSC Genome Browser.
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