Interaction of adrenal cell membrane receptors with dimers of corticotropin fragments and with poly-L-lysine.
Polycationic peptides are demonstrated to interact with the membrane receptors of the adrenal cell as judged from their effect on steroidogenesis. The corticotropin fragments ACTH7-24 and ACTH11-24, when covalently dimerized at their C-termini, strongly antagonize both corticotropin- and angiotensin II -induced steroidogenesis, while dimerized ACTH1-24 behaves as a mixed agonist/antagonist. A quantitative analysis of the antagonistic potencies shows that the measured effects are consistent with the prediction that electrostatically controlled accumulation of the charged ligand at the cell surface is an important factor in the overall ligand/receptor interaction. Similar antagonizing effects of poly-L-lysine provide further support for this hypothesis.
Stolz
M B
MB
Institute of Biotechnology, Swiss Federal Institute of Technology, Zurich, Switzerland.
Capponi
A M
AM
Sargent
D F
DF
Vallotton
M B
MB
Fauchère
J L
JL
D000311:Adrenal Glands / Q000187:drug effects* / Q000378:metabolism; D000324:Adrenocorticotropic Hormone / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D000804:Angiotensin II / Q000037:antagonists & inhibitors; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003345:Corticosterone / Q000096:biosynthesis; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology*; D018043:Receptors, Corticotropin; D011979:Receptors, Pituitary Hormone / Q000187:drug effects*
D010446:Peptide Fragments; D018043:Receptors, Corticotropin; D011979:Receptors, Pituitary Hormone; D000804:Angiotensin II; D011107:Polylysine; D000324:Adrenocorticotropic Hormone; D003345:Corticosterone