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Interaction of adrenal cell membrane receptors with dimers of corticotropin fragments and with poly-L-lysine.

作者信息

Stolz M B, Capponi A M, Sargent D F, Vallotton M B, Fauchère J L

机构信息

Institute of Biotechnology, Swiss Federal Institute of Technology, Zurich, Switzerland.

出版信息

J Recept Res. 1990;10(3-4):191-203. doi: 10.3109/10799899009064665.

DOI:10.3109/10799899009064665
PMID:2175813
Abstract

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.

摘要

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