Dynamics of atrial natriuretic factor-guanylate cyclase receptors and receptor-ligand complexes in cultured glomerular mesangial and renomedullary interstitial cells

Gou Y. Koh, Daniel R. Nussenzveig, Juraj Okolicany, Deborah A. Price, Thomas Maack

Research output: Contribution to journalArticle

55 Scopus citations

Abstract

The dynamics of the guanylate cyclase receptor of atrial natriuretic factor (GC(A)-ANF receptor) were investigated in cultured glomerular mesangial and renomedullary interstitial cells from the rat. In these cells, the GC(A)-ANF receptor did not mediate internalization and lysosomal hydrolysis of 125I-ANF1-28 and did not undergo ligand-induced endocytosis. Glomerular mesangial cells were able, however, to mediate internalization and lysosomal hydrolysis of 125I-ANF1-28 via clearance ANF (C-ANF) receptors and to promote rapid receptor-mediated internalization and lysosomal hydrolysis of 125I-(Sar1) angiotensin II. Radioligand specifically bound to surface GC(A)-ANF receptors was rapidly dissociated at 37 °C (k(off) > 0.8 min-1), with a Q10 (30-37 °C) > 6. The dissociation was markedly slower at subphysiological temperatures (Q10(4-30 °C), 2-3) or in the presence of 0.5 mM amiloride. The results demonstrate that the GC(A)-ANF receptor, contrary to C-ANF receptors and most other polypeptide hormone receptors, is a membrane resident protein that does not mediate internalization and lysosomal hydrolysis of ligand. The termination of the interaction of ANF with GC(A)-ANF receptors results from a physiological process that leads to rapid dissociation of receptor-ligand complexes. The unique dynamics of GC(A)-ANF receptor-ligand complexes are likely to contribute importantly to stimulus-response homeostasis of ANF.

Original languageEnglish (US)
Pages (from-to)11987-11994
Number of pages8
JournalJournal of Biological Chemistry
Volume267
Issue number17
StatePublished - 1992

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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