High and low affinity binding sites for endothelin on cultured rat glomerular mesangial cells

Kamal F. Badr, Karen A. Munger, Masanori Sugiura, Rudolf M. Snajdar, Mindy Schwartzberg, Tadashi Inagami

Research output: Contribution to journalArticlepeer-review

Abstract

Endothelin contracts glomerular mesangial cells, thereby influencing glomerular size and filtration rate. Here, we demonstrate the presence of two ET-specific binding sites on cultured rat mesangial cells with Kds of 0.76 and 44.70 nM, and maximal binding capacity (Bmax) values of 6.78×102 and 27.60×102 binding sites/cell, respectively. Binding of [125I]-ET was maximal at 120 min at 4°C, stable for the subsequent 60 min, and selective. No competition for binding was observed with >1000-fold concentrations of atrial natriuretic peptide, angiotensin II, arginine vasopressin, nicardipine, or nifedipine. The presence of specific receptors for ET on glomerular mesangial cells suggests a major role for this peptide in the regulation of glomerular filtration rate.

Original languageEnglish (US)
Pages (from-to)776-781
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume161
Issue number2
DOIs
StatePublished - Jun 15 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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