## Abstract Synthetic peptide, corresponding to the amino acid sequence 11β24 of human adrenocorticotropic hormone (ACTH), was labeled with tritium (specific activity of 22 Ci/mmol). [^3^H]ACTH (11β24) was found to bind to rat adrenal cortex membranes with high affinity and specificity (__K__~d~ =
Adrenal neuropeptides: Regulation and interaction with ACTH and other adrenal regulators
β Scribed by E.J. Whitworth; O. Kosti; D. Renshaw; J.P. Hinson
- Book ID
- 102334488
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 133 KB
- Volume
- 61
- Category
- Article
- ISSN
- 1059-910X
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β¦ Synopsis
Abstract
It is now well accepted that both the cortex and medulla of the mammalian adrenal gland receive a rich innervation. Many different transmitter substances have been identified in nerves supplying both cortex and medulla and, as well as catecholamines, a wide range of neuropeptides has been found in the adrenal gland. There have been several studies on the affects of age, sodium intake, stress, ACTH, and splanchnic nerve activity on the regulation of adrenal neuropeptide content. There is evidence that the abundance of each of these peptides is actively regulated. Although there have been many studies addressing the individual actions of various neurotransmitters on steroid secretion, adrenal blood flow, and adrenal growth, few have attempted to determine the nature of any interaction between neurotransmitters and the classical adrenal stimulants. There are, however, some significant interactions, particularly in the regulation of zona glomerulosa function. This review necessarily focuses on vasoactive intestinal peptide (VIP) and neuropeptide Y (NPY), as these are the most abundant transmitter peptides in the adrenal gland and the majority of studies have investigated their regulation and actions. However, substance P, calcitonin geneβrelated peptide (CGRP), neurotensin, and the enkephalins are included where appropriate. Finally, it has been suggested that certain neurotransmitters, particularly VIP, may interact with classical hormone receptors in the adrenal, notably the ACTH receptor. This review attempts to evaluate our current state of knowledge in each of these areas. Microsc. Res. Tech. 61:259β267, 2003. Β© 2003 WileyβLiss, Inc.
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