Zymogen activation, inhibition, and ectodomain shedding of matriptase

Front Biosci. 2008 Jan 1:13:621-35. doi: 10.2741/2707.

Abstract

Matriptase is a member of an expanding group of type II transmembrane serine proteases. Recently, much has been learned about the biochemistry, cellular biology, normal tissue physiology, and human pathology of this protease, and of its inhibitor, termed the hepatocyte growth factor inhibitor-1 (HAI-1). This review examines the recent literature that has characterized the regulation of matriptase and HAI-1 with an emphasis on the molecular mechanisms governing its zymogen activation, inhibition by HAI-1, and ectodomain shedding.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Antibodies, Monoclonal / chemistry
  • Cytosol / metabolism
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Lysophospholipids / chemistry
  • Membrane Glycoproteins / metabolism
  • Neoplasms / immunology
  • Neoplasms / metabolism
  • Protein Conformation
  • Proteinase Inhibitory Proteins, Secretory / chemistry*
  • Proteinase Inhibitory Proteins, Secretory / metabolism
  • Serine Endopeptidases / chemistry*
  • Suramin / chemistry

Substances

  • Antibodies, Monoclonal
  • Lysophospholipids
  • Membrane Glycoproteins
  • Proteinase Inhibitory Proteins, Secretory
  • SPINT1 protein, human
  • Suramin
  • Serine Endopeptidases
  • matriptase