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Alpha 1-antichymotrypsin

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Title: Alpha 1-antichymotrypsin  
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Alpha 1-antichymotrypsin

Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3
PDB rendering based on 1as4.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; AACT; ACT; GIG24; GIG25
External IDs ChEMBL: GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Alpha 1-antichymotrypsin (α1AC)[1] is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene.

Contents

  • Function 1
  • Clinical significance 2
  • Interactions 3
  • References 4
  • Further reading 5
  • External links 6

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]

References

  1. ^ Logan, Carolynn M.; Rice, M. Katherine (1987). Logan's Medical and Scientific Abbreviations. Philadelphia:  
  2. ^ a b Kalsheker N (1996). "Alpha 1-antichymotrypsin". Int. J. Biochem. Cell Biol. 28 (9): 961–4.  
  3. ^ "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3". 
  4. ^ 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.  

Further reading

  • Janciauskiene S, Wright HT (1999). "Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of Alzheimer's disease.". Bioessays 20 (12): 1039–46.  
  • 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.  

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)


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