Bryothamnion seaforthii lectin relaxes vascular smooth muscle: involvement of endothelium and NO synthase

Protein Pept Lett. 2010 Mar;17(3):305-10. doi: 10.2174/092986610790780332.

Abstract

Bryothamnion seaforthii lectin (BSL) induced reversible concentration-related relaxation of endothelized aorta, maximal at 30 microg/ml (IC(50)= 4.8 +/- 0.6 microg/ml). This effect was inhibited by L-NAME and reversed by mucin, probably via interaction with a specific lectin-binding site on the endothelium activating nitric oxide synthase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algal Proteins / chemistry*
  • Analysis of Variance
  • Animals
  • Aorta / metabolism
  • Endothelium, Vascular / drug effects*
  • Endothelium, Vascular / enzymology
  • Lectins / pharmacology*
  • Male
  • Muscle Relaxation / drug effects
  • Muscle, Smooth, Vascular / drug effects
  • Myocardial Contraction / drug effects
  • NG-Nitroarginine Methyl Ester / pharmacology
  • Nitric Oxide Synthase / metabolism*
  • Rats
  • Rats, Wistar
  • Rhodophyta / chemistry*

Substances

  • Algal Proteins
  • Lectins
  • Nitric Oxide Synthase
  • NG-Nitroarginine Methyl Ester