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Alpha 1-antichymotrypsin

alpha 1 antichymotrypsin, elevated fecal alpha 1 antichymotrypsin
1AS4, 1QMN, 2ACH, 3CAA, 3DLW, 4CAA

IdentifiersAliasesSERPINA3, AACT, ACT, GIG24, GIG25, serpin family A member 3External IDsMGI: 98377 HomoloGene: 111129 GeneCards: SERPINA3
Gene location Human
ChrChromosome 14 human[1]
Band14q3213Start94,612,377 bp[1]
End94,624,055 bp[1]
RNA expression pattern
More reference expression data
RefSeq mRNA



RefSeq protein



Location UCSCChr 14: 9461 – 9462 MbChr 12: 10434 – 10435 MbPubMed search[3][4]Wikidata
1 Function
  • 2 Clinical significance
  • 3 Interactions
  • 4 See also
  • 5 References
  • 6 Further reading
  • 7 External links
  • 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[6]

    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[7]

    Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimer's disease as it enhances the formation of amyloid-fibrils in this disease[6]


    Alpha 1-antichymotrypsin has been shown to interact with DNAJC1[8]

    See also

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


    1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196136 - Ensembl, May 2017
    2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058207 - Ensembl, May 2017
    3. ^ "Human PubMed Reference:" 
    4. ^ "Mouse PubMed Reference:" 
    5. ^ 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 
    6. ^ a b Kalsheker N 1996 "Alpha 1-antichymotrypsin" Int J Biochem Cell Biol 28 9: 961–4 doi:101016/1357-27259600032-5 PMID 8930118 
    7. ^ "Entrez Gene: SERPINA3 serpin peptidase inhibitor, clade A alpha-1 antiproteinase, antitrypsin, member 3" 
    8. ^ 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:101074/jbcM310903200 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:101002/SICI1521-187819981220:12<1039::AID-BIES10>30CO;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:101042/BST0300093 PMID 12023832 

    External links

    • The MEROPS online database for peptidases and their inhibitors: I04002
    • 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

    alpha 1 antichymotrypsin, alpha 1 antichymotrypsin elevated, alpha 1 antichymotrypsin stool, elevated fecal alpha 1 antichymotrypsin

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