Alpha-1-Antichymotrypsin (a1ACT)

A1-ACT; SERPINA3; AACT; ACT; GIG24; GIG25; Serpin Peptidase Inhibitor Clade A Member 3(Alpha-1 Antiproteinase; Antitrypsin); Cell growth-inhibiting gene 24/25 protein

SPN	V797
HGNC	16
MGI	105045
PubMed	9822922
RGD	3747
UniProt	P01011
Wiki	A1ACT

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.

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.

Reference

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Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

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"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease."
Cell 52:487-501(1988) [PubMed] [Europe PMC] [Abstract]

"Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver."
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"The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide."
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"Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose."
Biol. Chem. Hoppe-Seyler 375:335-341(1994) [PubMed] [Europe PMC] [Abstract]

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"Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins."
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Nature 311:175-177(1984) [PubMed] [Europe PMC] [Abstract]

"Amino acid sequence at the reactive site of human alpha 1-antichymotrypsin."
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"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
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"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
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"Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A resolution and its comparison with other serpins."
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"Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement."
Nat. Struct. Biol. 3:888-893(1996) [PubMed] [Europe PMC] [Abstract]

"Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction."
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"Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease."
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"Detection of a new mutant alpha-1-antichymotrypsin in patients with occlusive-cerebrovascular disease."
FEBS Lett. 304:66-68(1992) [PubMed] [Europe PMC] [Abstract]

"Mis-sense mutation of alpha 1-antichymotrypsin gene associated with chronic lung disease."
Lancet 339:1538-1538(1992) [PubMed] [Europe PMC] [Abstract]

"Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is associated with a lacunar type of ischemic cerebrovascular disease."
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