Journal articles: 'Peptide effects/adrenal cortex'

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Hinson, JP, and S. Kapas. "Actions of vasoactive intestinal peptide on the rat adrenal zona glomerulosa." Journal of Endocrinology 161, no. 1 (April 1, 1999): 51–57. http://dx.doi.org/10.1677/joe.0.1610051.

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Previous studies, by this group and others, have shown that vasoactive intestinal peptide (VIP) stimulates aldosterone secretion, and that the actions of VIP on aldosterone secretion by the rat adrenal cortex are blocked by beta adrenergic antagonists, suggesting that VIP may act by the local release of catecholamines. The present studies were designed to test this hypothesis further, by measuring catecholamine release by adrenal capsular tissue in response to VIP stimulation. Using intact capsular tissue it was found that VIP caused a dose-dependent increase in aldosterone secretion, with a concomitant increase in both adrenaline and noradrenaline release. The effects of VIP on aldosterone secretion were inhibited by atenolol, a beta1 adrenergic antagonist, but not by ICI-118,551, a beta2 adrenergic antagonist. Binding studies were carried out to investigate VIP receptors. It was found that adrenal zona glomerulosa tissue from control rats contained specific VIP binding sites (Bmax 853+/-101 fmol/mg protein; Kd 2.26+/-0.45 nmol/l). VIP binding was not displaced by ACTH, angiotensin II or by either of the beta adrenergic antagonists. The response to VIP in adrenals obtained from rats fed a low sodium diet was also investigated. Previous studies have found that adrenals from animals on a low sodium diet exhibit increased responsiveness to VIP. Specific VIP binding sites were identified, although the concentration or affinity of binding sites in the low sodium group was not significantly different from the controls. In the low sodium group VIP was found to increase catecholamine release to the same extent as in the control group, however, in contrast to the control group, the adrenal response to VIP was not altered by adrenergic antagonists in the low sodium group. These data provide strong support for the hypothesis that VIP acts by the local release of catecholamines in adrenal zona glomerulosa tissue in normal animals. It does not appear that VIP acts through the same mechanism in animals maintained on a low sodium diet. The mechanism by which VIP stimulates aldosterone in this group remains to be determined.

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Thomson, LM, S. Kapas, M. Carroll, and JP Hinson. "Autocrine role of adrenomedullin in the human adrenal cortex." Journal of Endocrinology 170, no. 1 (July 1, 2001): 259–65. http://dx.doi.org/10.1677/joe.0.1700259.

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Previous studies from our laboratory have reported that adrenomedullin is synthesised in rat zona glomerulosa cells. In the present studies, it was found that the human adrenocortical cell line H295R expresses the gene encoding adrenomedullin, and that immunoreactive adrenomedullin is released into the culture medium. Furthermore, it was found that secretion of adrenomedullin is regulated by angiotensin II and forskolin. Studies on the actions of adrenomedullin and calcitonin gene-related peptide (CGRP) revealed a stimulatory effect of adrenomedullin, but not of CGRP, on aldosterone and cortisol secretion. These data suggest that adrenomedullin is not acting by a CGRP receptor-mediated mechanism in the H295R cell line. Adrenomedullin was also found to increase cAMP production, suggesting that in the adrenal, as in other cell types, cAMP is a second messenger for adrenomedullin action. However, the effects of adrenomedullin were not fully mimicked by forskolin, possibly suggesting a role for an additional second messenger. The presence of mRNA encoding both the putative adrenomedullin receptors, L1 and calcitonin receptorlike receptor/receptor-associated modulatory protein 2 (CRLR/RAMP-2), was demonstrated in H295R cells, but RAMP-1 was not detected, suggesting that these cells do not express the CGRPI receptor CRLR/RAMP-1. Taken together, these data have demonstrated that adrenomedullin is synthesised and secreted by H295R cells. The observed rate of adrenomedullin synthesis suggests that this peptide exerts a paracrine/autocrine effect in this adrenocortical cell line, probably acting through a specific adrenomedullin receptor, to stimulate steroidogenesis and increase aldosterone synthase expression.

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Hinson, J. P., L. A. Cameron, and S. Kapas. "Neuropeptide Y modulates the sensitivity of the rat adrenal cortex to stimulation by ACTH." Journal of Endocrinology 145, no. 2 (May 1995): 283–89. http://dx.doi.org/10.1677/joe.0.1450283.

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Abstract Neuropeptide Y (NPY) has been identified in nerves supplying the adrenal cortex of several mammalian species, although its function in this tissue is unknown. The present studies, employing adrenocortical cells prepared by collagenase digestion, have shown that NPY, in the absence of other stimulants, has no effect on steroid secretion by the rat adrenal over a range of peptide concentrations (10−11 to 10 −6 mol/l). However, in the presence of physiological concentrations of ACTH, which are submaximal for the stimulation of aldosterone secretion, NPY (10−6 mol/l) significantly enhanced the secretion rate of aldosterone by rat zona glomerulosa cells in response to ACTH. This effect was specific to the rat zona glomerulosa as NPY had no effect on the response to ACTH in rat zona fasciculata cells. The effect of NPY appears to be biphasic, however, as NPY significantly attenuated the steroidogenic response to supramaximal ACTH concentrations: in rat zona glomerulosa cells the aldosterone response to 10 −8 mol ACTH/l was significantly inhibited by NPY. The effect of NPY on the ACTH response appeared to be mediated by changes in the cAMP response. NPY had no effect on the steroidogenic response to potassium ions (K+), but enhanced the response to angiotensin II. NPY (10 −6 mol/l) significantly stimulated inositol 1,4,5-trisphosphate (InsP3) production although this concentration of peptide had no effect on steroid secretion. The effects of NPY on InsP3 production were additive with those of angiotensin II. These results suggest that the role of NPY in the adrenal cortex may be to regulate the sensitivity of the zona glomerulosa to peptide stimulation. Journal of Endocrinology (1995) 145, 283–289

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Coll, Anthony P., Martin Fassnacht, Steffen Klammer, Stephanie Hahner, Dominik M. Schulte, Sarah Piper, Y. C. Loraine Tung, et al. "Peripheral administration of the N-terminal pro-opiomelanocortin fragment 1–28 to Pomc−/− mice reduces food intake and weight but does not affect adrenal growth or corticosterone production." Journal of Endocrinology 190, no. 2 (August 2006): 515–25. http://dx.doi.org/10.1677/joe.1.06749.

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Pro-opiomelanocortin (POMC) is a polypeptide precursor that undergoes extensive processing to yield a range of peptides with biologically diverse functions. POMC-derived ACTH is vital for normal adrenal function and the melanocortin α-MSH plays a key role in appetite control and energy homeostasis. However, the roles of peptide fragments derived from the highly conserved N-terminal region of POMC are less well characterized. We have used mice with a null mutation in the Pomc gene (Pomc−/−) to determine the in vivo effects of synthetic N-terminal 1–28 POMC, which has been shown previously to possess adrenal mitogenic activity. 1–28 POMC (20 μg) given s.c. for 10 days had no effect on the adrenal cortex of Pomc−/− mice, with resultant cortical morphology and plasma corticosterone levels being indistinguishable from sham treatment. Concurrent administration of 1–28 POMC and 1–24 ACTH (30 μg/day) resulted in changes identical to 1–24 ACTH treatment alone, which consisted of upregulation of steroidogenic enzymes, elevation of corticosterone levels, hypertrophy of the zona fasciculate, and regression of the X-zone. However, treatment of corticosterone-depleted Pomc−/− mice with 1–28 POMC reduced cumulative food intake and total body weight. These anorexigenic effects were ameliorated when the peptide was administered to Pomc−/− mice with circulating corticosterone restored either to a low physiological level by corticosterone-supplemented drinking water (CORT) or to a supraphysiological level by concurrent 1–24 ACTH administration. Further, i.c.v. administration of 1–28 POMC to CORT-treated Pomc−/− mice had no effect on food intake or body weight. In wild-type mice, the effects of 1–28 POMC upon food intake and body weight were identical to sham treatment, but 1–28 POMC was able to ameliorate the hyperphagia induced by concurrent 1–24 ACTH treatment. In a mouse model which lacks all endogenous POMC peptides, s.c. treatment with synthetic 1–28 POMC alone can reduce food intake and body weight, but has no impact upon adrenal growth or steroidogenesis.

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Andreis, P. G., G. Neri, T. Prayer-Galetti, G. P. Rossi, G. Gottardo, L. K. Malendowicz, and G. G. Nussdorfer. "Effects of Adrenomedullin on the Human Adrenal Glands: An in Vitro Study." Journal of Clinical Endocrinology & Metabolism 82, no. 4 (April 1, 1997): 1167–70. http://dx.doi.org/10.1210/jcem.82.4.3854.

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Abstract Numerous lines of evidence indicate that adrenal medulla exerts a paracrine control on the secretory activity of the cortex by releasing catecholamines and several regulatory peptides. Adrenomedullin (ADM) is contained in adrenal medulla of several mammalian species, including humans. Thus, we investigated whether human ADM1–52 exerts a modulatory action on steroid secretion of human adrenal cortex in vitro. Dispersed adrenocortical cells (obtained from the gland tail deprived of chromaffin cells) and adrenal slices (including both capsule and medulla) were employed. ADM specifically inhibited angiotensin II-stimulated aldosterone secretion of dispersed cells and enhanced basal aldosterone production by adrenal slices, minimal effective concentrations being 10−7 and 10−9 mol/L, respectively. These effects of ADM were suppressed by the CGRP1 receptor antagonist CGRP8–37 (10−5 mol/L). Neither basal and ACTH-stimulated aldosterone secretion of dispersed cells nor agonist-enhanced aldosterone production by adrenal slices were affected by ADM, which also did not alter cortisol secretion of both types of adrenal preparations. ADM (10−6 mol/L) blunted the aldosterone secretagogue action of the Ca2+ ionophore A23187 (10−5 mol/L) on dispersed cells and adrenal slices. Theβ -adrenoceptor antagonist l-alprenolol (10−6 mol/L) suppressed aldosterone response of adrenal slices to 10−7 mol/L isoprenaline and ADM. ADM concentration dependently raised epinephrine and norepinephrine release by adrenal slices, minimal effective concentration being 10−9 mol/L. Collectively, these findings suggest that ADM, acting via the CGRP1 receptor subtype, exerts a direct inhibitory effect on angiotensin II-stimulated aldosterone secretion, which, when the integrity of adrenal tissue is preserved, is overcome and reversed by an indirect stimulatory action, conceivably involving the release of catecholamines by adrenal chromaffin cells.

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Kapas, S., A. Martinez, F. Cuttitta, and JP Hinson. "Local production and action of adrenomedullin in the rat adrenal zona glomerulosa." Journal of Endocrinology 156, no. 3 (March 1, 1998): 477–84. http://dx.doi.org/10.1677/joe.0.1560477.

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This study was designed to investigate the synthesis and action of adrenomedullin in the rat adrenal gland. The results obtained from in situ hybridization and immunocytochemical studies suggest that adrenomedullin is synthesized not only in the medulla, but also within the zona glomerulosa of the rat adrenal cortex. Findings from in situ hybridization and binding studies also suggested that specific adrenomedullin receptors are expressed in the zona glomerulosa, and that low levels are present in the inner zones of the cortex. The Kd of the zona glomerulosa adrenomedullin receptor (5.5 nmol/l) suggests that it may respond to locally produced adrenomedullin rather than circulating concentrations of the peptide, which are in a lower range. It was found that adrenomedullin acted on zona glomerulosa cells in vitro to stimulate aldosterone release and cAMP formation, but in this tissue did not stimulate inositol phosphate turnover. The effect of adrenomedullin on aldosterone secretion was significantly attenuated by a protein kinase A inhibitor, suggesting that cAMP mediates the effects of adrenomedullin on aldosterone secretion. Adrenomedullin did not significantly affect the response of zona glomerulosa cells to stimulation by either ACTH or angiotensin II. Adrenomedullin did not affect the release of catecholamines, either adrenaline or noradrenaline, by intact adrenal capsular tissue. These data suggest that both adrenomedullin and its specific receptor are expressed in the rat adrenal zona glomerulosa, leading to the hypothesis that adrenomedullin may have an autocrine/paracrine role in the regulation of the rat adrenal zona glomerulosa.

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7

Hinson, J. P., S. Kapas, C. D. Orford, and G. P. Vinson. "Vasoactive intestinal peptide stimulation of aldosterone secretion by the rat adrenal cortex may be mediated by the local release of catecholamines." Journal of Endocrinology 133, no. 2 (May 1992): 253–58. http://dx.doi.org/10.1677/joe.0.1330253.

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ABSTRACT The effects of vasoactive intestinal peptide (VIP) on adrenocortical function were investigated using several different preparations of adrenocortical tissue. VIP caused a significant increase in perfusion medium flow rate and in aldosterone and corticosterone secretion by the isolated perfused rat adrenal gland, with a threshold of 1 pmol in 200 μl, but did not affect basal steroid secretion by collagenase-dispersed adrenocortical cells at any concentration used, from 10 pmol/l to 10 μmol/l. The presence of VIP (100 nmol/l) had no significant effect on the response of zona glomerulosa cells to stimulation by ACTH at any concentration. In incubations of intact adrenal capsular tissue, VIP (10 μmol/l) caused a significant stimulation of aldosterone secretion, and also induced a significant release of adrenaline into the incubation medium. Addition of (−)alprenolol (100 nmol/l), a βadrenergic antagonist, to the incubation medium significantly attenuated the response of capsular tissue to VIP. It is concluded that the effects of VIP on aldosterone, which are only seen when the architecture of the zona glomerulosa is preserved, may be mediated by the local release of adrenaline. Journal of Endocrinology (1992) 133, 253–258

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8

Karteris, Emmanouil, Rachel J. Machado, Jing Chen, Sevasti Zervou, Edward W. Hillhouse, and Harpal S. Randeva. "Food deprivation differentially modulates orexin receptor expression and signaling in rat hypothalamus and adrenal cortex." American Journal of Physiology-Endocrinology and Metabolism 288, no. 6 (June 2005): E1089—E1100. http://dx.doi.org/10.1152/ajpendo.00351.2004.

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Although starvation-induced biochemical and metabolic changes are perceived by the hypothalamus, the adrenal gland plays a key role in the integration of metabolic activity and energy balance, implicating feeding as a major synchronizer of rhythms in the hypothalamic-pituitary-adrenal (HPA) axis. Given that orexins are involved in regulating food intake and activating the HPA axis, we hypothesized that food deprivation, an acute challenge to the systems that regulate energy balance, should elicit changes in orexin receptor signaling at the hypothalamic and adrenal levels. Food deprivation induced orexin type 1 (OX1R) and 2 (OX2R) receptors at mRNA and protein levels in the hypothalamus, in addition to a fivefold increase in prepro-orexin mRNA. Cleaved peptides OR-A and OR-B are also elevated at the protein level. Interestingly, adrenal OX1R and OX2R levels were significantly reduced in food-deprived animals, whereas there was no expression of prepro-orexin in the adrenal gland in either state. Food deprivation exerted a differential effect on OXR-G protein coupling. In the hypothalamus of food deprived rats compared with controls, a significant increase in coupling of orexin receptors to Gq, Gs, and Go was demonstrated, whereas coupling to Gi was relatively less. However, in the adrenal cortex of the food-deprived animal, there was decreased coupling of orexin receptors to Gs, Go, and Gq and increased coupling to Gi. Subsequent second-messenger studies (cAMP/IP3) have supported these findings. Our data indicate that food deprivation has differential effects on orexin receptor expression and their signaling characteristics at the hypothalamic and adrenocortical levels. These findings suggest orexins as potential metabolic regulators within the HPA axis both centrally and peripherally.

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9

Delarue, C., JM Conlon, I. Remy-Jouet, A. Fournier, and H. Vaudry. "Endothelins as local activators of adrenocortical cells." Journal of Molecular Endocrinology 32, no. 1 (February 1, 2004): 1–7. http://dx.doi.org/10.1677/jme.0.0320001.

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Besides the classical corticotropic hormones, ACTH and angiotensin II, various regulatory peptides produced by the adrenal gland are thought to participate in the control of corticosteroid secretion. Here, we review the evidence that endothelins (ETs) synthesized within the adrenal cortex may act as autocrine and/or paracrine factors to regulate adrenocortical cell activity. The expression of ETs has been detected in normal, hyperplastic and neoplastic adrenocortical cells. The occurrence of ET receptors has been described in the different zones of the cortex. ETs stimulate the secretion of both glucocorticoids and mineralocorticoids, and modulate the proliferation of adrenocortical cells. The effects of ETs on steroidogenic cells are mediated through the activation of various signaling mechanisms including stimulation of phospholipase C, phospholipase A2 and adenylyl cyclase activity, as well as calcium influx through plasma channels. These observations suggest that locally produced ETs may play an important role in the regulation of corticosteroid secretion and in the control of mitogenesis in normal and tumoral adrenocortical cells.

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Giuliani, Luisa, Livia Lenzini, Michele Antonello, Enrico Aldighieri, Anna S. Belloni, Ambrogio Fassina, Celso Gomez-Sanchez, and Gian Paolo Rossi. "Expression and Functional Role of Urotensin-II and Its Receptor in the Adrenal Cortex and Medulla: Novel Insights for the Pathophysiology of Primary Aldosteronism." Journal of Clinical Endocrinology & Metabolism 94, no. 2 (February 1, 2009): 684–90. http://dx.doi.org/10.1210/jc.2008-1131.

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Abstract Context: The involvement of urotensin II, a vasoactive peptide acting via the G protein-coupled urotensin II receptor, in arterial hypertension remains contentious. Objective: We investigated the expression of urotensin II and urotensin II receptor in adrenocortical and adrenomedullary tumors and the functional effects of urotensin II receptor activation. Design: The expression of urotensin II and urotensin II receptor was measured by real time RT-PCR in aldosterone-producing adenoma (n = 22) and pheochromocytoma (n = 10), using histologically normal adrenocortical (n = 6) and normal adrenomedullary (n = 5) tissue as control. Urotensin II peptide and urotensin II receptor protein were investigated with immunohistochemistry and immunoblotting. To identify urotensin II-related and urotensin II receptor-related pathways, a whole transcriptome analysis was used. The adrenocortical effects of urotensin II receptor activation were also assessed by urotensin II infusion with/without the urotensin II receptor antagonist palosuran in rats. Results: Urotensin II was more expressed in pheochromocytoma than in aldosterone-producing adenoma tissue; the opposite was seen for the urotensin II receptor expression. Urotensin II receptor activation in vivo in rats enhanced (by 182 ± 9%; P < 0.007) the adrenocortical expression of immunoreactive aldosterone synthase. Conclusions: Urotensin II is a putative mediator of the effects of the adrenal medulla and pheochromocytoma on the adrenocortical zona glomerulosa. This pathophysiological link might account for the reported causal relationship between pheochromocytoma and primary aldosteronism.

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Kapas, S., A. Purbrick, and J. P. Hinson. "Action of opioid peptides on the rat adrenal cortex: stimulation of steroid secretion through a specific μ opioid receptor." Journal of Endocrinology 144, no. 3 (March 1995): 503–10. http://dx.doi.org/10.1677/joe.0.1440503.

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Abstract While there have been several studies on the actions of opioid peptides on adrenocortical steroidogenesis, the results of these studies have failed to resolve the question as to whether these peptides exert a direct action on the adrenal cortex. The present studies were designed to address this question directly, using collagenase-dispersed rat zona glomerulosa and zonae fasciculata/reticularis cells incubated in vitro. The results obtained clearly show that the opioid peptides tested (β-endorphin, Leu-enkephalin, Met-enkephalin, and its long-acting analogue, DALA) all exerted a significant stimulatory effect on aldosterone secretion by zona glomerulosa cells and all, except Leuenkephalin, stimulated corticosterone secretion by inner zone cells. The response was shown to be inhibited by naloxone. There did not appear to be a significant interaction between the effects of ACTH and the opioid peptides on adrenocortical cells. Studies using specific agonists for opioid receptor subtypes (DAMGO, DPDPE and U-50488H, specific for μ, δ and κ receptors respectively) showed that the effect of opioid peptides on the zona glomerulosa appeared to be mediated exclusively by μ receptors while the response of inner zone cells was mediated by both μ and, to a lesser extent, κ receptors. Finally, studies on the second messenger systems activated by the opioid peptides and the receptor agonists showed that these peptides act to increase labelling of inositol trisphosphate, and strongly suggest that, in the rat adrenal cortex, both μ and κ opioid receptors are linked to the activation of phospholipase C. Journal of Endocrinology (1995) 144, 503–510

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Kapas, S., A. Purbrick, and J. P. Hinson. "Role of tyrosine kinase and protein kinase C in the steroidogenic actions of angiotensin II, α-melanocyte-stimulating hormone and corticotropin in the rat adrenal cortex." Biochemical Journal 305, no. 2 (January 15, 1995): 433–38. http://dx.doi.org/10.1042/bj3050433.

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The role of protein kinases in the steroidogenic actions of alpha-melanocyte-stimulating hormone (alpha-MSH), angiotensin II (AngII) and corticotropin (ACTH) in the rat adrenal zona glomerulosa was examined. Ro31-8220, a potent selective inhibitor of protein kinase C (PKC), inhibited both AngII- and alpha-MSH-stimulated aldosterone secretion but had no effect on aldosterone secretion in response to ACTH. The effect of Ro31-8220 on PKC activity was measured in subcellular fractions. Basal PKC activity was higher in cytosol than in membrane or nuclear fractions. Incubation of the zona glomerulosa with either alpha-MSH or AngII resulted in significant increases in PKC activity in the nuclear and cytosolic fractions and decreases in the membrane fraction. These effects were all inhibited by Ro31-8220. ACTH caused a significant increase in nuclear PKC activity only, and this was inhibited by Ro31-8220 without any significant effect on the steroidogenic response to ACTH, suggesting that PKC translocation in response to ACTH may be involved in another aspect of adrenal cellular function. Tyrosine phosphorylation has not previously been considered to be an important component of the response of adrenocortical cells to peptide hormones. Both AngII and alpha-MSH were found to activate tyrosine kinase, but ACTH had no effect, observations that have not been previously reported. Tyrphostin 23, a specific antagonist of tyrosine kinases, inhibited aldosterone secretion in response to AngII and alpha-MSH, but not ACTH. These data confirm the importance of PKC in the adrenocortical response to AngII and alpha-MSH, and, furthermore, indicate that tyrosine kinase may play a critical role in the steroidogenic actions of AngII and alpha-MSH in the rat adrenal zona glomerulosa.

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Mazzocchi, Giuseppina, Francesco Aragona, Ludwik K. Malendowicz, and Gastone G. Nussdorfer. "PTH and PTH-related peptide enhance steroid secretion from human adrenocortical cells." American Journal of Physiology-Endocrinology and Metabolism 280, no. 2 (February 1, 2001): E209—E213. http://dx.doi.org/10.1152/ajpendo.2001.280.2.e209.

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Parathyroid hormone (PTH) and PTH-related peptide (PTH-RP) are two hypercalcemic hormones that share a common receptor subtype, the PTH/PTH-RP receptor. PTH and PTH-RP concentration dependently enhanced basal aldosterone and cortisol secretion from dispersed human adrenocortical cells, with a maximal effective concentration (∼2-fold increase) of 10−8 M. The secretagogue effect of 10−8 M PTH or PTH-RP was abolished by the PTH/PTH-RP receptor antagonist [Leu11,d-Trp12]-PTH-RP-(7–34)-amide (10−6 M). PTH and PTH-RP (10−8 M) raised cAMP and inositol-triphosphate release by dispersed adrenocortical cells, and these effects were blocked by the adenylate cyclase inhibitor SQ-22536 (10−4 M) and the phospholipase C (PLC) inhibitor U-73122 (10−5 M), respectively. SQ-22536 (10−4 M) and U-73122 (10−5 M) partially inhibited aldosterone and cortisol response to 10−8 M PTH and PTH-RP; when added together, they abolished it. Similar results were obtained by using the protein kinase (PK)A and PKC inhibitors H-89 and calphostin C (10−5 M). It is concluded that PTH and PTH-RP exert a sizeable secretagogue action on the human adrenal cortex, probably acting through the PTH/PTH-RP receptor coupled with both adenylate cyclase/PKA- and PLC/PKC-dependent signaling cascades.

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Nesher, Maoz, Moran Dvela, Vincent U. Igbokwe, Haim Rosen, and David Lichtstein. "Physiological roles of endogenous ouabain in normal rats." American Journal of Physiology-Heart and Circulatory Physiology 297, no. 6 (December 2009): H2026—H2034. http://dx.doi.org/10.1152/ajpheart.00734.2009.

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Endogenous ouabain (EO)-like compounds are synthesized in and released from the adrenal gland. Although EO has been implicated in several pathological states such as hypertension and heart and kidney failure, its physiological roles in normal animal have not been elucidated. To address this issue, we studied the effects of reduction in plasma EO resulting from antiouabain antibody administration. Normal rats were treated for 28 days with antiouabain antibodies or rabbit IgG as control. Infusions were delivered through a jugular vein cannula by osmotic pumps, and blood pressure was monitored by tail-cuff plethysmography. The animals were housed in metabolic cages to measure water and food consumption and urine excretion. After 28 days, the thoracic aorta was isolated and used to study phenylephrine-induced contraction and atrial natriuretic peptide (ANP)-induced vasorelaxation. The adrenal gland cortex was enlarged in the antiouabain antibody-treated rats. Moreover, on the second day of treatment, there was a significant transient reduction in natriuresis in the antiouabain antibody-treated rats, suggesting that EO is a natriuretic hormone. Reduction in natriuresis was also observed when EO levels were reduced by active immunization resulting from sequential injection of ouabain-albumin. Furthermore, following 28 days of treatment, the response to phenylephrine was significantly lowered and that to ANP was significantly increased in aortic rings from antiouabain antibody-treated rats. These findings show for the first time that circulatory ouabain plausibly originating in the adrenal has physiological roles controlling vasculature tone and sodium homeostasis in normal rats.

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Oki, Kenji, Phillip G. Kopf, William B. Campbell, Milay Luis Lam, Takeshi Yamazaki, Celso E. Gomez-Sanchez, and Elise P. Gomez-Sanchez. "Angiotensin II and III Metabolism and Effects on Steroid Production in the HAC15 Human Adrenocortical Cell Line." Endocrinology 154, no. 1 (January 1, 2013): 214–21. http://dx.doi.org/10.1210/en.2012-1557.

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Aldosterone is synthesized in the zona glomerulosa of the adrenal cortex under primary regulation by the renin-angiotensin system. Angiotensin II (A-II) acts through the angiotensin types 1 and 2 receptors (AT1R and AT2R). A-II is metabolized in different tissues by various enzymes to generate two heptapeptides A-III and angiotensin 1-7, which can then be catabolized into smaller peptides. A-II was more potent than A-III in stimulating aldosterone secretion in the adrenocortical cell line HAC15, and A-II, but not A-III, stimulated cortisol secretion. A-II stimulated mRNA expression of steroidogenic acute regulatory protein, 3β-hydroxysteroid dehydrogenase, CYP11B1, and CYP11B2, whereas A-III stimulated 3β-hydroxysteroid dehydrogenase, CYP11B1, and CYP11B2 but decreased the expression of CYP17A1 required for cortisol synthesis. The stimulation of aldosterone secretion by A-II and A-III was blocked by the AT1R receptor blocker, losartan, but not by an AT2R blocker. A-II was rapidly metabolized by the HAC15 cells to mainly to angiotensin 1-7, but not to A-III, and disappeared from the supernatant within 6 h. A-III was metabolized rapidly and disappeared within 1 h. In conclusion, A-II was not converted to A-III in the HAC15 cell and is the more potent stimulator of aldosterone secretion and cortisol of the two. A-III stimulated aldosterone secretion but not cortisol secretion.

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Yoshimura, Michihiro, Hirofumi Yasue, and Hisao Ogawa. "Pathophysiological significance and clinical application of ANP and BNP in patients with heart failure." Canadian Journal of Physiology and Pharmacology 79, no. 8 (August 1, 2001): 730–35. http://dx.doi.org/10.1139/y01-039.

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Plasma levels of ANP and BNP increase in accordance with the severity of the heart failure. In severe cases, the amount of BNP secreted surpasses that of ANP. The main secretion site of BNP is the ventricles, and that of ANP is the atria. However, ANP is also secreted from the ventricles as heart failure advances, and thus the ventricles are important sites for both BNP and ANP. It is well known that myocardial stretch is a key factor in the stimulation of the secretion of ANP and BNP, although neurohumoral factors also play a role in the secretion mechanism. The major physiological effects of ANP and BNP are vasodilation, natriuresis, and inhibition of the renin-angiotensin-aldosterone (RAA) and the sympathetic nervous systems; all of which are supposed to suppress the progression of heart failure. The inhibitory action of ANP and BNP on the RAA system has been considered to be an extra-cardiac effect. We recently reported the activation of an angiotensin-converting enzyme and aldosterone production in failing human hearts. ANP and BNP, however, would inhibit aldosterone production, not only in the adrenal cortex but also in cardiac tissue. ANP, and especially BNP, are useful markers of the heart's status during treatment for heart failure. The infusion of synthetic ANP (hANP) or BNP (Nesiritide®) is effective in the treatment of acute heart failure. In Japan, BNP occupies an important position in the diagnosis of chronic heart failure, as ANP does in the treatment of acute heart failure.Key words: natriuretic peptide, heart failure, myocardial infarction, cardiomyopathy, aldosterone.

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Janssens, Cecile JJG, Frans A. Helmond, and Victor M. Wiegant. "Chronic stress and pituitary–adrenocortical responses to corticotropin-releasing hormone and vasopressin in female pigs." European Journal of Endocrinology 132, no. 4 (April 1995): 479–86. http://dx.doi.org/10.1530/eje.0.1320479.

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Janssens CJJG, Helmond FA, Wiegant VM. Chronic stress and pituitary–adrenocortical responses to corticotropin-releasing hormone and vasopressin in female pigs. Eur J Endocrinol 1995;132:479–86. ISSN 0804–4643 Effects of long-term tethered housing (a condition of chronic stress) on pituitary-adrenocortical responsiveness to exogenous corticotropin-releasing hormone (CRH) and lysine8-vasopressin (LVP) were investigated in female pigs. Intravenous administration of CRH (dose range 10–440 pmol/kg body wt) or LVP (10–880 pmol/kg body wt) elicited transient and dose-related increases in plasma concentrations of adrenocorticotropic hormone (ACTH) and cortisol. Comparison of the responses induced by the peptides indicated that CRH is a more potent ACTH secretagogue than LVP. Treatment with LVP produced a fivefold greater plasma cortisol/ACTH ratio than treatment with CRH, suggesting that in addition to stimulating pituitary ACTH release it enhanced the ability of the adrenal cortex to secrete cortisol in response to ACTH. Whereas concomitant administration of 10 pmolCRH/kg body wt and 20 pmol LVP/kg body wt revealed an additive effect on ACTH release, synergism between both peptides was found with respect to their cortisol-releasing effect. Ten to thirteen weeks of chronic stress did not alter significantly the absolute ACTH and cortisol responses to the two peptides. In tethered pigs, the cortisol/ACTH ratio after CRH treatment, calculated from the area under the curve, was twofold that in loose-housed pigs. From these observations we conclude that after chronic stress the sensitivity of the adrenocortex to circulating ACTH was increased, whereas the sensitivity of the pituitary to CRH and/or LVP remained unaltered. Frans A Helmond, Department of Human and Animal Physiology, Wageningen Agricultural University, Haarweg 10, 6709 PJ Wageningen, The Netherlands

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Ho, Mei Mei, and Gavin P. Vinson. "Peptide growth factors and the adrenal cortex." Microscopy Research and Technique 36, no. 6 (March 15, 1997): 558–68. http://dx.doi.org/10.1002/(sici)1097-0029(19970315)36:6<558::aid-jemt12>3.0.co;2-n.

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Higuchi, Kazumi, Takashi Hashiguchi, Masao Ohashi, Ryoichi Takayanagi, Masafumi Haji, Hisayuki Matsuo, and Hajime Nawata. "Porcine brain natriuretic peptide receptor in bovine adrenal cortex." Life Sciences 44, no. 13 (January 1989): 881–86. http://dx.doi.org/10.1016/0024-3205(89)90588-2.

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Pignatelli, Duarte, Marta Maia, M. Jose Bento, Susana Sousa, M. Eugenia Azevedo, Manuel M. Magalhaes, M. Conceicao Magalhaes, and Gavin P. Vinson. "Captopril Effects on the Rat Adrenal Cortex." Endocrine Research 26, no. 4 (January 2000): 965–72. http://dx.doi.org/10.3109/07435800009048624.

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Lu, Shin-Tsu, Susanne Pettit, Shwu-Jen Lu, and Sol M. Michaelson. "Effects of Microwaves on the Adrenal Cortex." Radiation Research 107, no. 2 (August 1986): 234. http://dx.doi.org/10.2307/3576811.

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22

Nuglozeh, Edem, Majambu Mbikay, Duncan J. Stewart, and Louis Legault. "Gene expression of natriuretic peptide receptors in rats with DOCA-salt hypertension." American Journal of Physiology-Cell Physiology 273, no. 4 (October 1, 1997): C1427—C1434. http://dx.doi.org/10.1152/ajpcell.1997.273.4.c1427.

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In our previous studies, we found that the atrial natriuretic peptide (ANP) binding and guanylyl cyclase activity of A-type natriuretic peptide receptors (NPR-A) were upregulated in renal papillae but downregulated in vascular tissues and glomeruli of rats with deoxycorticosterone acetate (DOCA)-salt hypertension [E. Nuglozeh, G. Gauquelin, R. Garcia, J. Tremblay, and E. L. Schiffrin. Am. J. Physiol. 259 ( Renal Fluid Electrolyte Physiol. 28): F130–F137, 1990]. To further understand the molecular significance of these regulations, we measured the relative abundance of the transcripts of NPR-A and NPR-B by Northern blot in the aorta, mesenteric arteries, adrenal cortex, renal papillae, and lungs in DOCA-salt hypertensive and control rats. In renal papillae we also examined the translation and transcription of NPR-A by ribosome loading and run-on assay. Compared with controls, the steady-state levels of mRNA for NPR-A were increased in the aorta and mesenteric arteries but were decreased in the adrenal cortex and renal papillae in DOCA-salt-treated rats. NPR-B mRNA was decreased in the aorta, mesenteric arteries, and adrenal cortex in hypertensive rats. In lungs the mRNA for both receptors was unchanged. Translation of NPR-A mRNA, as assessed by ribosome loading, was reduced in renal papillae. Transcriptional activity of its gene was not detectable in these tissues. Guanosine 3′,5′-cyclic monophosphate levels generated by NPR-A in renal papillae and by NPR-A and NPR-B in the adrenal cortex, aorta, and mesenteric arteries of DOCA-salt-treated rats remained increased in hypertension. The higher NPR-A activity in the presence of a lower level of its mRNA in renal papillae and the higher NPR-B activity in the presence of a lower level of its mRNA in the vasculature, adrenal cortex, and lungs can alternatively be explained by receptor stabilization or increased receptor recycling.

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Nekrasova, Y. N., Y. A. Zolotarev, and E. V. Navolotskaya. "Interaction of the synthetic peptide octarphin with rat adrenal cortex membranes." Biochemistry (Moscow) 77, no. 12 (December 2012): 1377–81. http://dx.doi.org/10.1134/s000629791212005x.

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Pignatelli, Duarte, Marta Maia, Ana Rita Castro, Maria da Conceicao Magalhaes, Josiane Vivier, and Genevieve Defaye. "Chronic Stress Effects on the Rat Adrenal Cortex." Endocrine Research 26, no. 4 (January 2000): 537–44. http://dx.doi.org/10.3109/07435800009048567.

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Faraci, F. M., W. M. Chilian, J. K. Williams, and D. D. Heistad. "Effects of reflex stimuli on blood flow to the adrenal medulla." American Journal of Physiology-Heart and Circulatory Physiology 257, no. 2 (August 1, 1989): H590—H596. http://dx.doi.org/10.1152/ajpheart.1989.257.2.h590.

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The goal of this study was to examine changes in blood flow to the adrenal medulla during reflex stimuli that release catecholamines. Adrenal blood flow was measured with microspheres during exercise in conscious dogs and during bicuculline-induced seizures in anesthetized dogs. In awake dogs, blood flow to the adrenal cortex and adrenal medulla was 310 +/- 48 and 1,613 +/- 258 (SE) ml.min-1.100 g-1, respectively. Blood flow to the cortex and medulla was not affected by moderate exercise. Anesthesia (pentobarbital sodium) reduced blood flow to the adrenal cortex and medulla to 158 +/- 12 and 243 +/- 24 ml.min-1.100 g-1, respectively. In anesthetized dogs, seizures markedly increased blood flow to the adrenal medulla (282 +/- 68 to 1,257 +/- 128 ml.min-1.100 g-1), and this response was blocked by sectioning the greater splanchnic nerve. Vasodilator responses of the adrenal medulla to adenosine were not impaired by adrenal denervation. Blood flow to the adrenal cortex was not affected by seizures but increased in response to intravenous adenosine. These findings suggest that 1) anesthesia decreases adrenal blood flow, particularly to the adrenal medulla, and 2) reflex stimuli that release catecholamines can produce selective increases in blood flow to the adrenal medulla.

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Totsune, Kazuhito, Kazuhiro Takahashi, Osamu Murakami, Fumitoshi Satoh, Masahiko Sone, Makoto Ohneda, Yukio Miura, and Toraichi Mouri. "Immunoreactive brain natriuretic peptide in human adrenal glands and adrenal tumors." European Journal of Endocrinology 135, no. 3 (September 1996): 352–56. http://dx.doi.org/10.1530/eje.0.1350352.

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Totsune K, Takahashi K, Murakami O, Satoh F, Sone M, Ohneda M. Miura Y. Mouri T. Immunoreactive brain natriuretic peptide in human adrenal glands and adrenal tumors. Eur J Endocrinol 1996;135:352–6. ISSN 0804–4643 The presence of brain natriuretic peptide (BNP) in tissues of human adrenal glands and adrenal tumors was investigated by radioimmunoassay. Immunoreactive BNP concentrations were 0.203 ± 0.061 pmol/g wet tissue (mean ± sem) in normal parts of adrenal glands (cortex and medulla. N = 8), 0.205 ± 0.037 pmol/g wet tissue in pheochromocytomas (N = 8), 0.230 ± 0.062 pmol/g wet tissue in aldosteronomas (N = 11) and 0.180 ± 0.054 pmol/g wet tissue in adrenocortical adenomas with Cushing's syndrome (N = 4). Sephadex G-50 superfine column chromatography and reverse-phase high-performance liquid chromatography showed that most (> 70%) of the immunoreactive BNP in the normal part of adrenal glands was eluted in the position of human BNP-32. Sephadex G-50 superfine column chromatography of immunoreactive BNP in the pheochromocytoma and aldosteronoma showed four peaks: one in the position ofγ-BNP, one in the position of BNP-32, one between γ-BNP and BNP-32 and one in the smaller molecular weight region. The present study has shown that immunoreactive BNP is present both in normal human adrenal glands and in adrenal tumors. Multiple molecular forms of BNP were found to be present in the tumor tissues of pheochromocytoma and aldosteronoma. Kazuhiro Takahashi. Department of Applied Physiology and Molecular Biology, Tohoku University School of Medicine, 2–1 Seiryo-machi, Aoba-ku. Sendai 980–77, Japan

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Renshaw, D., A. T. Cruchley, S. Kapas, and J. P. Hinson. "Receptors for calcitonin gene-related peptide (CGRP) in the rat adrenal cortex." Endocrine Research 24, no. 3-4 (January 1998): 773–76. http://dx.doi.org/10.3109/07435809809032686.

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Kapas, Supriya, Derek Renshaw, Mark Carroll, and Joy P. Hinson. "Adrenomedullin and calcitonin gene-related peptide receptors in the rat adrenal cortex." Peptides 22, no. 11 (November 2001): 1903–7. http://dx.doi.org/10.1016/s0196-9781(01)00516-2.

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Shimada, Hiroki, Erika Noro, Susumu Suzuki, Jun Sakamoto, Ikuko Sato, Rehana Parvin, Atsushi Yokoyama, and Akira Sugawara. "Effects of Adipocyte-derived Factors on the Adrenal Cortex." Current Molecular Pharmacology 13, no. 1 (January 15, 2020): 2–6. http://dx.doi.org/10.2174/1874467212666191015161334.

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Background and Objective: Obesity is highly complicated by hypertension and hyperglycemia. In particular, it has been proposed that obesity-related hypertension is caused by adipocyte-derived factors that are recognized as undetermined proteins secreted from adipocytes. Adipocyte-derived factors have been known to be related to aldosterone secretion in the adrenal gland. So far, Wnt proteins, CTRP-1, VLDL, LDL, HDL and leptin have been demonstrated to stimulate aldosterone secretion. In contrast, it has not yet been clarified whether adipocyte-derived factors also affect adrenal cortisol secretion. Methods and Results: In the present study, we investigated the effect of adipocyte-derived factors on cortisol synthase gene CYP11B1 mRNA expression in vitro study using adrenocortical carcinoma H295R cells and mouse fibroblast 3T3-L1cells. Interestingly, adipocyte-derived factors were demonstrated to have the ability to stimulate CYP11B1 mRNA expression. Conclusion: Since CYP11B1 is well known as a limiting enzyme of cortisol synthesis, our study suggests that adipocyte-derived factors may stimulate cortisol secretion, as well as aldosterone secretion. Taken together, adipocyte-derived factors may be the cause of metabolic syndrome due to their stimulating effects on aldosterone/cortisol secretion. Therefore, the innovation of novel drugs against them may possibly be a new approach against metabolic syndrome.

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Macedo, Lilian Alves, Adriana Aparecida Ferraz Carbonel, Ricardo Santos Simões, Luiz Fernando Portugal Fuchs, Vinicius Cestari do Amaral, Tommaso Simoncini, Manuel Jesus Santos Simões, Edmund Chada Baracat, and José Maria Soares. "Effects of metformin on the adrenal cortex of androgenized rats." Gynecological Endocrinology 31, no. 8 (June 10, 2015): 609–12. http://dx.doi.org/10.3109/09513590.2015.1019342.

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31

Rossi, G. "Effects of endothelin-1[1-31] on human adrenal cortex." American Journal of Hypertension 14, no. 11 (November 2001): A68. http://dx.doi.org/10.1016/s0895-7061(01)01668-5.

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Cockerill, David, Louis W. Chang, Aubrey Hough, and Frank Bivins. "Effects of trimethyltin on the mouse hippocampus and adrenal cortex." Journal of Toxicology and Environmental Health 22, no. 2 (October 1987): 149–61. http://dx.doi.org/10.1080/15287398709531059.

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33

Bicknell, Andrew B. "60 YEARS OF POMC: N-terminal POMC peptides and adrenal growth." Journal of Molecular Endocrinology 56, no. 4 (May 2016): T39—T48. http://dx.doi.org/10.1530/jme-15-0269.

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The peptide hormones contained within the sequence of proopiomelanocortin (POMC) have diverse roles ranging from pigmentation to regulation of adrenal function to control of our appetite. It is generally acknowledged to be the archetypal hormone precursor, and as its biology has been unravelled, so too have many of the basic principles of hormone biosynthesis and processing. This short review focuses on one group of its peptide products, namely, those derived from the N-terminal of POMC and their role in the regulation of adrenal growth. From a historical and a personal perspective, it describes how their role in regulating proliferation of the adrenal cortex was identified and also highlights the key questions that remain to be answered.

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Ehrhart-Bornstein, Monika, Stefan R. Bornstein, Werner A. Scherbaum, Ernst F. Pfeiffer, and Jens J. Holst. "Role of the Vasoactive Intestinal Peptide in a Neuroendocrine Regulation of the Adrenal Cortex." Neuroendocrinology 54, no. 6 (1991): 623–28. http://dx.doi.org/10.1159/000125969.

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35

Petrovic-Kosanovic, Dragana, V. Ajdzanovic, Maja Cakic-Milosevic, Vesna Koko, and Verica Milosevic. "The effects of acute heat stress on proliferative and apoptotic processes in the rat adrenal cortex." Archives of Biological Sciences 65, no. 3 (2013): 905–9. http://dx.doi.org/10.2298/abs1303905k.

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Hyperthermia can cause significant structural and functional reorganization of tissues and organs. The proliferative and apoptotic processes of rat adrenal cortex were analyzed by light and electron microscopy after an acute exposure to high ambient temperature. Animals were divided in two groups. The first group consisted of intact controls. The rats from the second group were exposed to a high ambient temperature of 38?C for 60 min. Mitotic chromosomes and the largest number of immunoreactive nuclei for the Ki-67 were observed in the zona reticularis (ZR) of the control animals. The relative number of mitoses after heat stress showed a significant decrease in the zona glomerulosa (ZG; 66.8%), zona fasciculata (ZF; 27.8%) and ZR (86.7%) (for all zones p<0.05), while in the whole adrenal cortex the after-treatment decrease was 61.9% (p<0.05) compared to the controls. Under heat stress numerous apoptotic nuclei were seen at the light and ultrastructural levels in all the zones of the adrenal cortex. Such dynamics of mitosis/apoptosis events seriously affect adrenal cortex morphology.

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Jousselin-Hosaja, M. "Effects of transplantation on mouse adrenal chromaffin cells." Journal of Endocrinology 116, no. 1 (January 1988): 149—NP. http://dx.doi.org/10.1677/joe.0.1160149.

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ABSTRACT The effects of long-term transplantation on the ultrastructure of adrenaline- and noradrenaline-storing cells from the adrenal medulla were determined using morphometric methods. Mouse adrenal medulla were freed from the adrenal cortex and grafted into the occipital cortex of the brain. Two types of chromaffin cells were identified by electron microscopy in grafts fixed with glutaraldehyde and osmium tetroxide. Noradrenaline-type cells were predominant and formed 70–80% of the surviving population of grafted chromaffin cells. A minority of the chromaffin cells contained medium-sized granules (140–210 nm in diameter) (medium granule cell; MGC) with finely granular moderately electron dense cores. Morphometric analysis of noradrenaline phenotype cells and MGC cells in transplants showed no significant differences compared with the noradrenaline-storing cells of normal adrenal glands. In contrast, noradrenaline-type cells and MGC cells in the grafts had areas of secretory vesicles which were significantly (P<0·01) larger and areas of rough endoplasmic reticulum which were significantly (P<0 ·01) smaller than those of the adrenaline-storing cells of normal adrenal glands. It was concluded that long-term transplantation caused no degenerative changes in the ultrastructure of mouse adrenal chromaffin cells. J. Endocr. (1988) 116, 149–153

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Nunez, D. J. R., A. P. Davenport, and M. J. Brown. "Atrial natriuretic factor mRNA and binding sites in the adrenal gland." Biochemical Journal 271, no. 2 (October 15, 1990): 555–58. http://dx.doi.org/10.1042/bj2710555.

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The factor inhibiting aldosterone secretion produced by the adrenal medulla may be atrial natriuretic factor (ANF), since the latter abolishes aldosterone release in response to a number of secretagogues, including angiotensin II and K+. In this study we have shown that cells in the adrenal medulla contain ANF mRNA and therefore have the potential to synthesize this peptide. The presence of binding sites for ANF predominantly in the adrenal zona glomerulosa suggests that, if ANF is synthesized in the medulla and transferred to the cortex, it may affect mineralocorticoid status.

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Bodnar, M., A. Sarrieau, C. F. Deschepper, and C. D. Walker. "Adrenal vasoactive intestinal peptide participates in neonatal corticosteroid production in the rat." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 273, no. 3 (September 1, 1997): R1163—R1172. http://dx.doi.org/10.1152/ajpregu.1997.273.3.r1163.

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Neonatal rats (3-14 days old) exhibit a period of adrenal hyporesponsiveness characterized by blunted corticosterone (B) responses to stress and reduced adrenal sensitivity to adrenocorticotropic hormone (ACTH). Several adrenomedullary peptidergic systems like vasoactive intestinal peptide (VIP) are postulated to influence cortical function. VIP is known to stimulate corticosterone secretion in vitro and to be released from the adrenal medulla following splanchnic nerve stimulation. Here, we tested whether 1) accelerated sympathetic innervation of the adrenal gland by daily L-thyroxine (T4) treatment modified the ontogeny of adrenal VIP and 2) an increase in VIP synthesis could prematurely increase adrenal sensitivity and corticosteroid output during neonatal life. Immunohistochemical VIP staining revealed a different ontogenetic pattern between adrenal regions from days 2-18 and different sensitivities to T4 treatment. Capsular staining was most abundant at all ages and increased with T4 treatment, whereas medullary staining was seen by day 18 and was not affected by T4. Throughout development, VIP receptors were detected mostly in the capsular region, but not in the adrenal cortex. Although receptor levels were not modified by T4 injections, T4 significantly enhanced VIP mRNA levels in the whole adrenal at all ages. In vivo administration of VIP (0.1-2.0 mg/kg body wt ip) to 9- to 12-day-old neonates increased pituitary ACTH, adrenal B, and aldosterone secretion significantly. Corticotropin-releasing factor immunoneutralization before VIP injection diminished VIP-induced ACTH release but still produced small but significant B and aldosterone secretion. Our results show that 1) VIP innervation of the adrenal capsule is present soon after birth and is increased by sympathetic activity whereas VIP appears only much later in the medulla and does not coincide with the onset of splanchnic innervation and 2) exogenous VIP stimulates ACTH, B, and aldosterone release during development and the effect of VIP on steroidogenic secretion is occurring through ACTH secretion, but also, at least in part, directly at the level of the adrenal gland.

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Milovanović, Tatjana, Mirela Budec, Ljiljana Balint-Perić, Vesna Koko, and Vera Todorović. "Effects of acute administration of ethanol on the rat adrenal cortex." Journal of Studies on Alcohol 64, no. 5 (September 2003): 662–68. http://dx.doi.org/10.15288/jsa.2003.64.662.

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40

Nanmoku, Toru, Kazumasa Isobe, Takeshi Sakurai, Akihiro Yamanaka, Kazuhiro Takekoshi, Yasushi Kawakami, Katsutoshi Goto, and Toshiaki Nakai. "Effects of orexin on cultured porcine adrenal medullary and cortex cells." Regulatory Peptides 104, no. 1-3 (March 2002): 125–30. http://dx.doi.org/10.1016/s0167-0115(01)00356-1.

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41

Wernert, N., A. Antalffy, and G. Dhom. "Effects of estradiol on adrenal cortex and medulla of the rat." Pathology - Research and Practice 181, no. 5 (October 1986): 551–57. http://dx.doi.org/10.1016/s0344-0338(86)80148-0.

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42

Bozzo, Aída Andrea, Carlos Alberto Soñez, Ignacio Monedero Cobeta, Rodolfo Avila, Alicia Nélida Rolando, María Cristina Romanini, Mario Lazarte, Héctor Fernando Gauna, and María Teresa Mugnaini. "Chronic Stress Effects on Adrenal Cortex Cellular Proliferation in Pregnant Rats." International Journal of Morphology 29, no. 4 (December 2011): 1148–57. http://dx.doi.org/10.4067/s0717-95022011000400013.

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43

Lesniewska, B., M. Nowak, B. Miskowiak, G. G. Nussdorfer, and L. K. Malendowicz. "Long-term effects of neuropeptide-Y on the rat adrenal cortex." Neuropeptides 16, no. 1 (May 1990): 9–13. http://dx.doi.org/10.1016/0143-4179(90)90023-r.

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44

McCarty, Richard, Robert F. Kirby, and Robert M. Carey. "Effects of dietary sodium on dopamine content of rat adrenal cortex." Physiology & Behavior 37, no. 5 (January 1986): 785–89. http://dx.doi.org/10.1016/0031-9384(86)90185-x.

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Colby, H. D. "Adrenal Gland Toxicity: Chemically Induced Dysfunction." Journal of the American College of Toxicology 7, no. 1 (January 1988): 45–69. http://dx.doi.org/10.3109/10915818809078702.

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Among the endocrine organs, the adrenal cortex appears to be the most vulnerable to chemically induced injury. A wide variety of chemicals has been found to cause morphological or functional lesions in the gland. Some of the lesions are highly localized to specific anatomical zones of the adrenal cortex, and the resulting functional deficits depend on the physiological role(s) of the zone affected. In addition, metabolic activation is an important factor contributing to the gland's vulnerability to chemical injury. For example, carbon tetrachloride (CCl4) causes adrenocortical necrosis, but only of the innermost zone of the gland, the zona reticularis. The apparent reason for the localized effect of CCl4 in the adrenal cortex is that only the cells of the zona reticularis have the enzymatic capacity to activate CCl4, resulting in lipid peroxidation and covalent binding to cellular macromolecules. By contrast, the mineralocorticoid antagonist, spironolactone, causes functional lesions in the adrenal cortex that are limited to the middle zone of the gland, the zona fasciculata. The explanation again involves metabolic activation; only the zona fasciculata converts spironolactone to a highly reactive metabolite that effects the destruction of several enzymes that are required for steroid hormone synthesis. These findings indicate that bioactivation plays a critical role in the mechanism(s) of action of various toxic agents on the adrenal cortex and also may be responsible for the anatomically localized effects of many chemicals.

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Doreian, Bryan W., Tiberiu G. Fulop, Robert L. Meklemburg, and Corey B. Smith. "Cortical F-Actin, the Exocytic Mode, and Neuropeptide Release in Mouse Chromaffin Cells Is Regulated by Myristoylated Alanine-rich C-Kinase Substrate and Myosin II." Molecular Biology of the Cell 20, no. 13 (July 2009): 3142–54. http://dx.doi.org/10.1091/mbc.e09-03-0197.

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Adrenal medullary chromaffin cells are innervated by the sympathetic splanchnic nerve and translate graded sympathetic firing into a differential hormonal exocytosis. Basal sympathetic firing elicits a transient kiss-and-run mode of exocytosis and modest catecholamine release, whereas elevated firing under the sympathetic stress response results in full granule collapse to release catecholamine and peptide transmitters into the circulation. Previous studies have shown that rearrangement of the cell actin cortex regulates the mode of exocytosis. An intact cortex favors kiss-and-run exocytosis, whereas disrupting the cortex favors the full granule collapse mode. Here, we investigate the specific roles of two actin-associated proteins, myosin II and myristoylated alanine-rich C-kinase substrate (MARCKS) in this process. Our data demonstrate that MARCKS phosphorylation under elevated cell firing is required for cortical actin disruption but is not sufficient to elicit peptide transmitter exocytosis. Our data also demonstrate that myosin II is phospho-activated under high stimulation conditions. Inhibiting myosin II activity prevented disruption of the actin cortex, full granule collapse, and peptide transmitter release. These results suggest that phosphorylation of both MARCKS and myosin II lead to disruption of the actin cortex. However, myosin II, but not MARCKS, is required for the activity-dependent exocytosis of the peptide transmitters.

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Zheng, Huifei Sophia, Jeff Daniel, Chad David Foradori, Robert J. Kemppainen, and Chen-Che Jeff Huang. "Acute Transcriptional Effects of Dexamethasone on Mouse Adrenal Gland Transcriptome." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A65. http://dx.doi.org/10.1210/jendso/bvab048.131.

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Abstract Researchers have long known that dexamethasone causes cellular and functional changes in the adrenal gland. For example, long-term dexamethasone treatment leads to reversible adrenal cortex atrophy. In the adrenal medulla, dexamethasone treatment alters the maturation and function of the neural crest-derived chromaffin cells. Here we aim to study the acute transcriptional effect of dexamethasone on mouse adrenal gland at the transcriptome level. Our data suggested that a one-hour dexamethasone treatment had a cell type-specific effect on the adrenal transcriptome. There were 922 dexamethasone-induced genes and 853 dexamethasone-suppressed genes. GO analysis showed that the upregulated genes were primarily linked to neuronal cell function. Clustered heatmaps further showed that many genes involved in the catecholamine synthesis were upregulated by dexamethasone treatment, whereas most genes involved in the steroidogenesis pathway were downregulated. Interestingly, steroidogenic factor 1 (SF1, encoded by Nr5a1), the critical transcription factor that regulates steroidogenesis, had a >2-fold decrease under the one-hour dexamethasone treatment, suggesting a possible mechanism of the acute suppression of steroidogenic activity. Our findings indicate that the acute effects of dexamethasone stimulate catecholamine synthesis in the medulla, whereas steroidogenesis in the cortex is suppressed by dexamethasone.

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Whitnall, M. H., Y. C. Lee, W. J. Driscoll, and C. A. Strott. "Immunocytochemical localization of the 34 KD pregnenolone-binding protein to fasciculata and reticularis cells and a novel 32 KD protein specific for reticularis cells in guinea pig adrenal cortex." Journal of Histochemistry & Cytochemistry 38, no. 11 (November 1990): 1607–14. http://dx.doi.org/10.1177/38.11.2170503.

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Two proteins were isolated and purified from guinea pig adrenal cortex: a 34 KD protein that specifically binds pregnenolone (product of the rate-limiting step in steroidogenesis), and a novel co-purifying 32 KD protein that has not been characterized. Specific antisera were generated and used for immunocytochemical analysis. The 34 KD and 32 KD proteins were specific for the adrenal cortex and were absent from other tissues, including the testis. The 34 KD pregnenolone binding protein (PBP) was localized to zona fasciculata and zona reticularis cells and absent from zona glomerulosa cells. Thus, the PBP was absolutely correlated with ACTH-regulated steroidogenic cells, whereas steroidogenic cells regulated by other peptide hormones did not contain the PBP. This finding suggests a functional relationship between the PBP and ACTH. A second interesting finding was that a novel 32 KD co-purifying protein localized to the zona reticularis and was absent from the zona glomerulosa and the zona fasciculata. The 32 KD protein can therefore serve as an excellent marker for the reticularis cell of the adrenal cortex.

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Zieleniewski, Wojciech. "The stimulatory effect of endothelin-1 on regenerating adrenal cortex is reversed by nifedipine." European Journal of Endocrinology 136, no. 1 (January 1997): 121–22. http://dx.doi.org/10.1530/eje.0.1360121.

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Abstract Endothelin-1 (ET-1), a potent vasoconstrictor, was found to act in non-vascular tissues, for example it enhanced aldosterone output from adrenal zona glomerulosa. As the adrenal cortex is capable of regeneration after enucleation, it seemed of interest to study the effects of ET-1 on adrenocortical regeneration. The study was performed on adult rats subjected to left adrenal enucleation combined with contralateral adrenalectomy. Mitotic index was employed to assess the proliferation of regenerating adrenal cortex cells. Plasma corticosterone was measured by a standard RIA kit. ET-1 significantly raised the mitotic index of regenerating rat adrenal cortex by six days after surgery. On the other hand, nifedipine reduced the proliferation ratio and abolished the stimulatory influence of ET-1. Similarly, ET-1 enhanced corticosterone output from the regenerating adrenal cortex, and this could be prevented by the addition of nifedipine. This study has shown that ET-1 might act as a regulatory factor on the regenerating adrenal cortex via calcium channels. European Journal of Endocrinology 136 121–122

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NISHIKAWA, TETSUO, KEIJI MIKAMI, AKIKO YOSHIDA, MASAO OMURA, YASUSHI TAMURA, and YASUSHI SAITO. "Regulation of Cholesterol Metabolism in Adrenal Cortex: Effects of Apoproteins on Cholesterol Esterase in Rat Adrenal Glands." Endocrine Journal 40, no. 2 (1993): 221–25. http://dx.doi.org/10.1507/endocrj.40.221.

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Journal articles on the topic 'Peptide effects/adrenal cortex'

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