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In vivo catabolism of alpha 1-antichymotrypsin is mediated by the Serpin receptor which binds alpha 1-proteinase inhibitor, antithrombin III and heparin cofactor II.

Publication ,  Journal Article
Pizzo, SV; Mast, AE; Feldman, SR; Salvesen, G
Published in: Biochim Biophys Acta
November 17, 1988

The in vivo catabolism of 125I-labeled alpha 1-antichymotrypsin was studied in our previously described mouse model. Native alpha 1-antichymotrypsin cleared with an apparent t1/2 of 85 min, but alpha 1-antichymotrypsin in complex with chymotrypsin or cathepsin G cleared with a t1/2 of 12 min. Clearance of the complex was blocked by a large molar excess of unlabeled complexes of proteinases with either alpha 1-antichymotrypsin or alpha 1-proteinase inhibitor. These studies indicate that the clearance of alpha 1-antichymotrypsin-proteinase complexes utilizes the same pathway as complexes with the homologous inhibitor alpha 1-proteinase inhibitor. Previous studies have demonstrated that this pathway is also responsible for the catabolism of two other serine proteinase inhibitors, antithrombin III and heparin cofactor II. This pathway is thus responsible for removing several proteinases involved in coagulation and inflammation from the circulation, thereby decreasing the likelihood of adventitious proteolysis.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

November 17, 1988

Volume

967

Issue

2

Start / End Page

158 / 162

Location

Netherlands

Related Subject Headings

  • alpha 1-Antitrypsin
  • alpha 1-Antichymotrypsin
  • Serine Endopeptidases
  • Protease Inhibitors
  • Humans
  • Heparin Cofactor II
  • Half-Life
  • Glycoproteins
  • Electrophoresis, Polyacrylamide Gel
  • Cathepsins
 

Citation

APA
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ICMJE
MLA
NLM
Pizzo, S. V., Mast, A. E., Feldman, S. R., & Salvesen, G. (1988). In vivo catabolism of alpha 1-antichymotrypsin is mediated by the Serpin receptor which binds alpha 1-proteinase inhibitor, antithrombin III and heparin cofactor II. Biochim Biophys Acta, 967(2), 158–162. https://doi.org/10.1016/0304-4165(88)90005-0
Pizzo, S. V., A. E. Mast, S. R. Feldman, and G. Salvesen. “In vivo catabolism of alpha 1-antichymotrypsin is mediated by the Serpin receptor which binds alpha 1-proteinase inhibitor, antithrombin III and heparin cofactor II.Biochim Biophys Acta 967, no. 2 (November 17, 1988): 158–62. https://doi.org/10.1016/0304-4165(88)90005-0.
Pizzo, S. V., et al. “In vivo catabolism of alpha 1-antichymotrypsin is mediated by the Serpin receptor which binds alpha 1-proteinase inhibitor, antithrombin III and heparin cofactor II.Biochim Biophys Acta, vol. 967, no. 2, Nov. 1988, pp. 158–62. Pubmed, doi:10.1016/0304-4165(88)90005-0.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

November 17, 1988

Volume

967

Issue

2

Start / End Page

158 / 162

Location

Netherlands

Related Subject Headings

  • alpha 1-Antitrypsin
  • alpha 1-Antichymotrypsin
  • Serine Endopeptidases
  • Protease Inhibitors
  • Humans
  • Heparin Cofactor II
  • Half-Life
  • Glycoproteins
  • Electrophoresis, Polyacrylamide Gel
  • Cathepsins