Abstract
The dynamics of the guanylate cyclase receptor of atrial natriuretic factor (GCA-ANF receptor) were investigated in cultured glomerular mesangial and renomedullary interstitial cells from the rat. In these cells, the GCA-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 GCA-ANF receptors was rapidly dissociated at 37 °C (koff > 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 GCA-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 GCA-ANF receptors results from a physiological process that leads to rapid dissociation of receptor-ligand complexes. The unique dynamics of GCA-ANF receptor-ligand complexes are likely to contribute importantly to stimulus-response homeostasis ofANF.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 11987-11994 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 267 |
| Issue number | 17 |
| State | Published - Jun 15 1992 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Dynamics of atrial natriuretic factor-guanylate cyclase receptors and receptor-ligand complexes in cultured glomerular mesangial and renomedullary interstitial cells. / Koh, Gou Y.; Nussenzveig, Daniel R.; Okolicany, Juraj; Price, Deborah A.; Maack, Thomas.
In: Journal of Biological Chemistry, Vol. 267, No. 17, 15.06.1992, p. 11987-11994.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dynamics of atrial natriuretic factor-guanylate cyclase receptors and receptor-ligand complexes in cultured glomerular mesangial and renomedullary interstitial cells
AU - Koh, Gou Y.
AU - Nussenzveig, Daniel R.
AU - Okolicany, Juraj
AU - Price, Deborah A.
AU - Maack, Thomas
PY - 1992/6/15
Y1 - 1992/6/15
N2 - The dynamics of the guanylate cyclase receptor of atrial natriuretic factor (GCA-ANF receptor) were investigated in cultured glomerular mesangial and renomedullary interstitial cells from the rat. In these cells, the GCA-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 GCA-ANF receptors was rapidly dissociated at 37 °C (koff > 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 GCA-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 GCA-ANF receptors results from a physiological process that leads to rapid dissociation of receptor-ligand complexes. The unique dynamics of GCA-ANF receptor-ligand complexes are likely to contribute importantly to stimulus-response homeostasis ofANF.
AB - The dynamics of the guanylate cyclase receptor of atrial natriuretic factor (GCA-ANF receptor) were investigated in cultured glomerular mesangial and renomedullary interstitial cells from the rat. In these cells, the GCA-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 GCA-ANF receptors was rapidly dissociated at 37 °C (koff > 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 GCA-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 GCA-ANF receptors results from a physiological process that leads to rapid dissociation of receptor-ligand complexes. The unique dynamics of GCA-ANF receptor-ligand complexes are likely to contribute importantly to stimulus-response homeostasis ofANF.
UR - http://www.scopus.com/inward/record.url?scp=0026769374&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026769374&partnerID=8YFLogxK
M3 - Article
C2 - 1351054
AN - SCOPUS:0026769374
VL - 267
SP - 11987
EP - 11994
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 17
ER -