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词条 Alpha 1-antichymotrypsin
释义

  1. Function

  2. Clinical significance

  3. Interactions

  4. See also

  5. References

  6. Further reading

  7. External links

{{Infobox_gene}}

Alpha 1-antichymotrypsin (symbol α1AC, 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.[1]

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.[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]

Interactions

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

See also

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

References

1. ^{{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}}
2. ^{{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 = }}
3. ^{{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 }}

}}

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

  • The MEROPS online database for peptidases and their inhibitors: I04.002
  • {{MeshName|Alpha+1-antichymotrypsin}}
  • {{UCSC gene info|SERPINA3}}
{{PDB Gallery|geneid=12}}{{Serpins}}{{Alpha globulins}}{{Glycoproteins}}{{Acute phase proteins}}{{gene-14-stub}}

1 : Acute phase proteins

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