Specific receptors for atrial natriuretic polypeptide on basolateral membranes isolated from rat renal cortex.
The binding of alpha-human atrial natriuretic polypeptide (alpha-hANP) to brush border and basolateral membranes isolated from the rat renal cortex was studied at 0 degree C by a rapid filtration technique. Specific binding of 125I-alpha-hANP to basolateral membranes reached a steady state at 4 hr. The binding to brush border membranes was maximal at 5-15 min and then rapidly decreased. The analysis of incubation mixtures with basolateral membranes revealed little degradation of 125I-alpha-hANP during the 4-hr incubation, while there was extensive degradation of the ligand with brush border membranes during the 30-min incubation. High affinity binding of 125I-alpha-hANP was demonstrated on basolateral membranes but not on brush border membranes. These data suggest that specific receptors for alpha-hANP are localized on basolateral membranes of the renal cortex.
Hori
R
R
Inui
K
K
Saito
H
H
Matsukawa
Y
Y
Okumura
K
K
Nakao
K
K
Morii
N
N
Imura
H
H
D000818:Animals; D009320:Atrial Natriuretic Factor; D001485:Basement Membrane / Q000032:analysis; D001665:Binding Sites; D003080:Cold Temperature; D006801:Humans; D007672:Kidney Cortex / Q000648:ultrastructure*; D008297:Male; D008871:Microvilli / Q000032:analysis; D009124:Muscle Proteins / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D017461:Receptors, Atrial Natriuretic Factor; D011956:Receptors, Cell Surface / Q000032:analysis*; D013379:Substrate Specificity; D013997:Time Factors
D009124:Muscle Proteins; D011956:Receptors, Cell Surface; D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor