Specific binding of atrial natriuretic peptide increases cyclic GMP levels in human astrocytoma cells.
Specific high-affinity binding sites (dissociation constant 100 pmol/l) for atrial natriuretic peptide (ANP) have been identified in the clone D384 derived from the human astrocytoma cell line G-CCM. Unrelated peptides such as angiotensin II, vasopressin and bradykinin did not compete for these sites. Of the atrial natriuretic peptides studied, both the human and rat ANP competed equally, while peptides with either C- or N-terminal residue missing or with no internal -S-S-bond either competed less effectively or did not compete at all. Human ANP stimulated the cells to increase their intracellular level of cyclic GMP in a time- and dose-dependent manner with maximum stimulation being approached but not reached at concentrations of 1 mumol/l. These results support both the notion that ANP has an important functional role within the brain and the concept of neurotransmitter/neuromodulator communication between neurones and glia.
Lyall
F
F
MRC Blood Pressure Unit, Western Infirmary, Glasgow.
Balmforth
A J
AJ
Morton
J J
JJ
D001254:Astrocytoma / Q000378:metabolism*; D009320:Atrial Natriuretic Factor / Q000378:metabolism*; D001665:Binding Sites; D001932:Brain Neoplasms / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism*; D006801:Humans; D017461:Receptors, Atrial Natriuretic Factor; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014407:Tumor Cells, Cultured / Q000378:metabolism
D011956:Receptors, Cell Surface; D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor; D006152:Cyclic GMP