Document Detail

Characterization of atrial natriuretic factor receptors in human glomerular epithelial and mesangial cells.
MedLine Citation:
PMID:  2171358     Owner:  NLM     Status:  MEDLINE    
To evaluate the distribution and functions of receptors of atrial natriuretic factor (ANF) in human glomeruli, we studied the binding sites of ANF-(1-28) in homogeneous populations of human glomerular epithelial cells or mesangial cells. 125I-labeled ANF bound specifically to both cell types. Equilibrium saturation binding curves suggested one group of receptor sites in mesangial cells (Kd = 99 +/- 32 pmol/l, Bmax = 15.3 +/- 3.5 fmol/mg) but multiple groups in glomerular epithelial cells. Binding was greater at 37 than at 4 degrees C in mesangial cells. The reverse was observed in glomerular epithelial cells due to marked degradation of the tracer at 37 degrees C. The fractions of undisplaceable tracer in a hypertonic acid medium after 60 min incubation were 45 and 16% at 37 degrees C for glomerular epithelial and mesangial cells, respectively. ANF-(1-28) and C-ANF-(4-23), a specific ligand of clearance receptors, similarly inhibited 125I-ANF binding to mesangial cells, whereas [Ala7-Ala23]-ANF, a linear analogue, was slightly less potent. In epithelial cells, C-ANF-(4-23) competitively inhibited 125I-ANF binding but with a lower potency than ANF, whereas linear ANF at low concentrations (10-100 pmol/l) stimulated 125I-ANF binding. In addition, linear ANF markedly inhibited the degradation of 125I-ANF in the incubation medium of epithelial and mesangial cells, whereas thiorphan, an inhibitor of enkephalinase, was inactive. ANF-(1-28) stimulated cGMP production in glomerular epithelial cells but not in mesangial cells. Both analogues were inactive in both cell types and did not modify ANF-(1-28)-dependent cGMP synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)
D Chansel; P Pham; M P Nivez; R Ardaillou
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The American journal of physiology     Volume:  259     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1990 Oct 
Date Detail:
Created Date:  1990-11-19     Completed Date:  1990-11-19     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  F619-27     Citation Subset:  IM    
Institut National de la Santé et de la Recherche Médicale, Unité 64, Hôpital Tenon, Paris, France.
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MeSH Terms
Atrial Natriuretic Factor / metabolism
Cells, Cultured
Cyclic GMP / metabolism
Epithelial Cells
Epithelium / metabolism
Glomerular Mesangium / cytology,  metabolism*
Kidney Glomerulus / cytology,  metabolism*
Receptors, Atrial Natriuretic Factor
Receptors, Cell Surface / metabolism*
Reg. No./Substance:
0/NPPA protein, human; 0/Receptors, Cell Surface; 7665-99-8/Cyclic GMP; 85637-73-6/Atrial Natriuretic Factor; EC, Atrial Natriuretic Factor

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