Activation of leukocyte rolling by the cysteine-rich domain and the hyper-variable region of HF3, a snake venom hemorrhagic metalloproteinase

FEBS Lett. 2008 Nov 26;582(28):3915-21. doi: 10.1016/j.febslet.2008.10.034. Epub 2008 Oct 31.

Abstract

The functionality of the disintegrin-like/cysteine-rich domains of snake venom metalloproteinases (SVMPs) has been shown to reside in the cysteine-rich region, which can interact with VWA-containing proteins. Recently, the hyper-variable region (HVR) of the cysteine-rich domain was suggested to constitute a potential protein-protein adhesive interface. Here we show that recombinant proteins of HF3, a hemorrhagic P-III SVMP, containing the cysteine-rich domain (disintegrin-like/cysteine-rich and cysteine-rich proteins) but not the disintegrin-like protein were able to significantly increase leukocyte rolling in the microcirculation. Peptides from the HVR also promoted leukocyte rolling and this activity was inhibited by anti-alpha(M)/beta2 antibodies. These results show, for the first time, that the cysteine-rich domain and its HVR play a role in triggering pro-inflammatory effects mediated by integrins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bothrops*
  • Catalysis
  • Crotalid Venoms / enzymology*
  • Cysteine / chemistry
  • Leukocyte Rolling / drug effects*
  • Male
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / pharmacology*
  • Mice
  • Mice, Inbred Strains
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / genetics
  • Peptides / pharmacology
  • Protein Structure, Tertiary / genetics

Substances

  • Crotalid Venoms
  • Peptides
  • Metalloendopeptidases
  • hemorrhagic metalloproteinase
  • Cysteine