scholarly journals Pituitary adenylate cyclase-activating polypeptide, vasoactive intestinal polypeptide and their receptors: distribution and involvement in the secretion of Podarcis sicula adrenal gland

2007 ◽  
Vol 196 (2) ◽  
pp. 291-303 ◽  
Author(s):  
Salvatore Valiante ◽  
Marina Prisco ◽  
Rosaria Sciarrillo ◽  
Maria De Falco ◽  
Anna Capaldo ◽  
...  
Keyword(s):  
Adrenal Gland ◽  
Adenylate Cyclase ◽  
Vasoactive Intestinal Polypeptide ◽  
Chromaffin Cells ◽  
Adrenal Glands ◽  
Podarcis Sicula ◽  
Adrenal Cell ◽  
Adrenal Cells ◽  
Pituitary Adenylate Cyclase

Vasoactive intestinal polypeptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) are regulatory neuropeptides of the hypothalamus–hypophyseal–adrenal axis, acting via the common receptors VPAC1 and VPAC2 and the selective PACAP receptor PAC1. In the adrenal glands of the Italian wall lizard, Podarcis sicula, the presence of VIP in chromaffin cells, and the VIP-stimulated release of catecholamine and aldosterone in vivo, was previously shown. To examine the localization of both peptides and receptors and their mRNAs in the adrenal gland of P. sicula, immunohistochemistry and in situ hybridization were performed: PACAP and its mRNA were detected in chromaffin cells, VPAC1 was found associated with steroidogenic tissue, VPAC2 and PAC1 with chromaffin tissue. Using ‘far western blot’ technique, we showed the presence of specific binding sites for VIP/PACAP in the adrenal glands of the lizard. The effects of both VIP and PACAP on the adrenal cells of the lizard were examined in vitro in adrenal cell co-cultures: both VIP and PACAP enhanced catecholamine, corticosterone and aldosterone release from adrenal cell co-culture in a time- and dose-dependent manner. The catecholamine release was inhibited by PAC1 antagonist and in VPAC2 immunoneutralized adrenal cells. The effects of VIP and PACAP on aldosterone secretion were counteracted by VPAC1 antagonist administration in vitro. Corticosterone secretion elicited by VIP was not blocked by VPAC1 antagonist, while the PACAP-induced release of corticosterone was blocked by the antagonist. Overall, our investigations indicate that these neuropeptides of the secretin superfamily can act not only as neurotransmitters but also as autocrine and paracrine regulators on chromaffin and cortical cells, being important mediators of the non-cholinergic system in the lizard adrenal gland.

Pituitary adenylate cyclase-activating polypeptide stimulates both adrenocortical cells and chromaffin cells in the frog adrenal gland.

Endocrinology ◽  
1994 ◽  
Vol 135 (6) ◽  
pp. 2749-2758 ◽  
Author(s):  
L Yon ◽  
N Chartrel ◽  
M Feuilloley ◽  
S De Marchis ◽  
A Fournier ◽  
...  
Keyword(s):  
Adrenal Gland ◽  
Adenylate Cyclase ◽  
Chromaffin Cells ◽  
Adrenocortical Cells ◽  
Pituitary Adenylate Cyclase

Localization, characterization and activity of pituitary adenylate cyclase-activating polypeptide in the frog adrenal gland

1993 ◽  
Vol 139 (2) ◽  
pp. 183-NP ◽  
Author(s):  
L. Yon ◽  
M. Feuilloley ◽  
N. Chartrel ◽  
A. Arimura ◽  
A. Fournier ◽  
...  
Keyword(s):  
Adrenal Gland ◽  
Adenylate Cyclase ◽  
High Performance ◽  
Reversed Phase ◽  
Molecular Forms ◽  
Dependent Manner ◽  
Adrenal Steroidogenesis ◽  
Pituitary Adenylate Cyclase ◽  
Corticosteroid Secretion

ABSTRACT Pituitary adenylate cyclase-activating polypeptide (PACAP) has recently been isolated from the frog brain and the sequence of the peptide appears to be strikingly similar to that of mammalian PACAP. In the present study, we have investigated the localization of PACAP in the frog interrenal (adrenal) gland by immunocytochemistry using antisera directed against PACAP 38 or PACAP 27. Two types of PACAP-immunoreactive fibres were observed: thick varicose fibres coursing between adrenal cells and thin processes located in the walls of blood vessels irrigating the gland. Bilateral transection of the splanchnic nerves did not affect the intensity and distribution of PACAP immunoreactivity. The mean ± s.e.m. concentration of PACAP, measured by radioimmunoassay in crude adrenal extracts, was 0·65 ± 0·16 nmol/g wet tissue. Two molecular forms of PACAP in the adrenal gland were characterized by reversed phase high-performance liquid chromatography combined with radioimmunoassay quantification. The elution profiles revealed the existence of two peaks exhibiting the same retention times as synthetic frog PACAP 38 (fPACAP 38) and PACAP 27, the predominant form being PACAP 38. The possible involvement of PACAP in the regulation of adrenal steroidogenesis was investigated in vitro using a perifusion system for frog adrenal slices. Graded doses of fPACAP 38 (0·1–10 μmol/l) increased the secretion of both corticosterone and aldosterone in a dose-dependent manner. Administration of repeated pulses of fPACAP 38 (1 μmol/l), at 120-min intervals, led to a reproducible stimulation of corticosteroid secretion without any tachyphylaxis. Prolonged infusion (2 h) of the peptide induced a rapid increase in corticosterone and aldosterone output, followed by a gradual decline in the secretion rate, suggesting the occurrence of a desensitization phenomenon. Synthetic porcine vasoactive intestinal peptide, which is structurally related to PACAP, was about ten times less potent than fPACAP 38 in stimulating steroidogenesis while the [Des-His1]-fPACAP 38 analogue was 100 times less effective. These results demonstrate that a peptide closely related to fPACAP 38 is present in fibres innervating the frog adrenal gland and could participate in the regulation of corticosteroid secretion, particularly during neurogenic stress. Journal of Endocrinology (1993) 139, 183–194

UTILIZATION OF [26-14C]CHOLESTEROL BY HUMAN FOETAL ADRENAL GLANDS IN VITRO

1978 ◽  
Vol 79 (3) ◽  
pp. 393-394 ◽  
Author(s):  
R. GUNASEGARAM ◽  
K. L. PEH ◽  
P. C. T. CHEW ◽  
S. M. M. KARIM ◽  
S. S. RATNAM
Keyword(s):  
Adrenal Gland ◽  
Steroid Hormones ◽  
Adrenal Glands ◽  
De Novo ◽  
Obstetrics And Gynaecology ◽  
Perfusion Studies

Department of Obstetrics and Gynaecology, University of Singapore, Kandang Kerbau Hospitalfor Women, Singapore 8, Republic of Singapore (Received 3 May 1978) From the previous studies of Bloch & Benirschke (1959, 1962) and Plotz, Kabara, Davis, LeRoy & Gould (1968) it appears that at mid-term, human foetal adrenal glands are capable of synthesizing C21- and C19-steroids de novo from acetate and cholesterol. Villee, Engel, Loring & Villee (1961), however, incubated slices and homogenates of foetal adrenal gland with [2-14C]acetate or [4-14C]cholesterol and could not demonstrate the incorporation of radioactivity into these steroids. Moreover, perfusion studies by three groups of investigators indicated only minute conversions of the same radioactive substrates into neutral steroids in the foetal adrenal glands (Solomon, Bird, Ling, Iwamiya & Young, 1967; Telegdy, Weeks, Archer, Wiqvist & Diczfalusy, 1970a; Telegdy, Weeks, Lerner, Stakemann & Diczfalusy, 1970b). It is widely believed that steroid hormones are normally synthesized from acetate via

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