Characterization of high affinity receptor sites for atrial natriuretic factor in anterior pituitary gland: evidence for the existence of two receptor forms.

The present study shows that in rat anterior pituitary tissue atrial natriuretic factor (ANF) binds to two distinct receptor forms, with apparent molecular weights of about 166K and 58K. Binding assays carried out with (125I)-ANF revealed specific and high affinity non-interacting binding sites, with Ko values of 1-1.7 nM and a density of 10-15,000 sites/cell. rANF fragments (5-25), (5-27) and (5-28) exhibited apparent equipotency in displacing tracer binding, while fragment (13-28) and various other peptides were ineffective. ANF (5-25) was about 100-times less potent than ANF (8-33) in stimulating half-maximum pituitary cGMP production. These data indicate the presence of multiple binding sites for ANF in the pituitary gland and suggest that only part of these sites may be coupled to activation of guanylate cyclase.