Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes.

Published

Journal Article (Review)

Antithrombin III (ATIII) clearance from blood occurs by redistribution into the extravascular compartment and by binding to the endothelial surface. When, however, ATIII reacts with a proteinase such as alpha-thrombin, the complex is rapidly cleared from the circulation (half-life is approximately five minutes) by a receptor present on hepatocytes. This receptor binds a number of other serine proteinase inhibitors that are members of the class designated as the "serpins." ATIII, alpha 1-proteinase inhibitor, heparin cofactor II, and alpha 1-antichymotrypsin proteinase complexes bind to the same hepatic receptor, now designated as serpin receptor 1. Proteinase complexes with alpha 2-antiplasmin, another member of the serpin class, do not bind to serpin receptor 1. Recent studies suggest that the specificity of the receptor for serpins may reside in the so-called D helix (nomenclature based on the structure of alpha 1-proteinase inhibitor). The presence of ATIII on the surface of endothelial cells offers a unique mechanism for regulating proteinases formed during coagulation. Since this ATIII is probably associated with heparin-like substances and exists in a high-affinity state, the inhibitor rapidly binds proteinases such as alpha-thrombin. Once the complex forms, its affinity for heparinoids is decreased compared with ATIII, allowing the complex to dissociate from the endothelial surface for rapid clearance by the liver.

Full Text

Duke Authors

Cited Authors

  • Pizzo, SV

Published Date

  • September 11, 1989

Published In

Volume / Issue

  • 87 / 3B

Start / End Page

  • 10S - 14S

PubMed ID

  • 2552799

Pubmed Central ID

  • 2552799

International Standard Serial Number (ISSN)

  • 0002-9343

Digital Object Identifier (DOI)

  • 10.1016/0002-9343(89)80524-8

Language

  • eng

Conference Location

  • United States