Receptors for pituitary adenylate cyclase activating peptides in human pituitary adenomas (original) (raw)
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1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
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1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
,
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
Search for other works by this author on:
1Department of Biochemistry and Nutrition, Erasme Hospital, Medical School, Université Libre de Bruxelles, Belgium.
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Published:
01 November 1993
Cite
P Robberecht, P Vertongen, B Velkeniers, P de Neef, P Vergani, C Raftopoulos, J Brotchi, E L Hooghe-Peters, J Christophe, Receptors for pituitary adenylate cyclase activating peptides in human pituitary adenomas, The Journal of Clinical Endocrinology & Metabolism, Volume 77, Issue 5, 1 November 1993, Pages 1235–1239, https://doi.org/10.1210/jcem.77.5.8077316
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Abstract
The presence of pituitary adenylate cyclase activating polypeptide (PACAP) receptors coupled to adenylate cyclase was investigated in four types of human pituitary adenomas: three null adenomas and five gonadotropin-, three ACTH-, four GH-, and four PRL-producing adenomas. In all samples, except in prolactinomas, PACAP(1-27) and PACAP(1-38) stimulated adenylate cyclase activity equally well and potently (K(act) around 3 nmol). Vasoactive intestinal polypeptide (VIP) was systematically 100- to 300-fold less potent than both PACAPs. In prolactinomas, PACAP(1-27), PACAP(1-38), and VIP were inactive despite a response of the enzyme to guanosine 5'-triphosphate, Gpp(NH)p, forskolin, and fluoride. [125I-AcHis1]PACAP(1-27) binding was detected in all samples except in prolactinomas. In addition, a detailed analysis of receptors was feasible in all five gonadotropin- and in two ACTH-producing adenomas, confirming the existence of selective PACAP receptors that recognized PACAP(1-27) and PACAP(1-38) with similar high affinity (IC50 0.8-1.5 nmol) and VIP with a low affinity (IC50 100 nmol/L).
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Copyright © 1993 by The Endocrine Society
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