Pituitary adenylate cyclase-activating polypeptide enhances saliva secretion via direct binding to PACAP receptors of major salivary glands in mice

2016 ◽  
Vol 299 (9) ◽  
pp. 1293-1299 ◽  
Author(s):  
Yuko Matoba ◽  
Naoko Nonaka ◽  
Yoshitoki Takagi ◽  
Eisaku Imamura ◽  
Masayuki Narukawa ◽  
...  

2000 ◽  
Vol 78 (3) ◽  
pp. 329-343 ◽  
Author(s):  
Anderson OL Wong ◽  
Wen Sheng Li ◽  
Eric KY Lee ◽  
Mei Yee Leung ◽  
Lai Yin Tse ◽  
...  

Pituitary adenylate cyclase activating polypeptide (PACAP) is a novel member of the secretin-glucagon peptide family. In mammals, this peptide has been located in a wide range of tissues and is involved in a variety of biological functions. In lower vertebrates, especially fish, increasing evidence suggests that PACAP may function as a hypophysiotropic factor regulating pituitary hormone secretion. PACAP has been identified in the brain-pituitary axis of representative fish species. The molecular structure of fish PACAP is highly homologous to mammalian PACAP. The prepro-PACAP in fish, however, is distinct from that of mammals as it also contains the sequence of fish GHRH. In teleosts, the anterior pituitary is under direct innervation of the hypothalamus and PACAP nerve fibers have been identified in the pars distalis. Using the goldfish as a fish model, mRNA transcripts of PACAP receptors, namely the PAC1 and VPAC1 receptors, have been identified in the pituitary as well as in various brain areas. Consistent with the pituitary expression of PACAP receptors, PACAP analogs are effective in stimulating growth hormone (GH) and gonadotropin (GTH)-II secretion in the goldfish both in vivo and in vitro. The GH-releasing action of PACAP is mediated via pituitary PAC1 receptors coupled to the adenylate cyclase-cAMP-protein kinase A and phospholipase C-IP3-protein kinase C pathways. Subsequent stimulation of Ca2+ entry through voltage-sensitive Ca2+ channels followed by activation of Ca2+-calmodulin protein kinase II is likely the downstream mechanism mediating PACAP-stimulated GH release in goldfish. Although the PACAP receptor subtype(s) and the associated post-receptor signaling events responsible for PACAP-stimulated GTH-II release have not been characterized in goldfish, these findings support the hypothesis that PACAP is produced in the hypothalamus and delivered to the anterior pituitary to regulate GH and GTH-II release in fish.Key words: PACAP, VIP, PAC1 receptor, VPAC1 receptor, VPAC2 receptor, growth hormone, gonadotropin-II, cAMP, protein kinase A, protein kinase C, calcium, pituitary cells, goldfish, and teleost.



Peptides ◽  
1994 ◽  
Vol 15 (4) ◽  
pp. 661-665 ◽  
Author(s):  
P. Robberecht ◽  
M.-C. Woussen-Colle ◽  
P. Vertongen ◽  
P. De Neef ◽  
X. Hou ◽  
...  


2020 ◽  
Vol 4 (Supplement_1) ◽  
Author(s):  
Parleen K Pandher ◽  
Ekaterina Filatov ◽  
Sarah L Gray

Abstract Pituitary adenylate cyclase-activating polypeptide (PACAP) is being studied to understand the endocrine regulation of energy balance and has been shown to be important in the regulation of the stress response (1,2). Specifically, PACAP has been shown to regulate thermogenesis, an energy burning process regulated by the sympathetic nervous system that contributes to achieving energy homeostasis in response to cold stress and overfeeding. PACAP is expressed in the sympathetic nervous system and is required at the adrenomedullary synapse to maintain epinephrine secretion from the adrenal medulla in response to physiological stress (3). Across the branches of the sympathetic nervous system, PACAP receptor expression is most well characterized in the superior cervical ganglia (SCG) (4). However, a detailed characterization of PACAP and its receptors has not been performed in ganglia whose postganglionic fibres innervate adipose tissues (stellate and celiac ganglia) in response to thermogenic stress. We hypothesized that PACAP is produced by preganglionic neurons innervating the stellate and celiac ganglia, and act on PACAP receptors expressed on the post-ganglionic neurons, and this expression will be upregulated in response to chronic cold stress. Due to their small and amorphous shape, we have developed a protocol to reliably isolate the stellate and celiac ganglia and validate their identity through the presence of tyrosine hydroxylase mRNA, using adrenal and SCG samples as positive controls. PACAP receptor expression (VPAC1, VPAC2, PAC1) was examined in the ganglia utilizing real-time PCR, and PACAP protein was visualized in the ganglia of transgenic mice that express eGFP under the control of the PACAP promoter (PACAP-eGFP mice) (5). This research demonstrates the expression of PACAP receptors in ganglia whose postganglionic fibres innervate adipose tissue, enhancing our understanding of PACAP’s role in the SNS, and its contribution to the regulation of adaptive thermogenesis. References: (1) Gray et al., Pacap: Regulator of the stress response. In: Fink G, ed. Stress: Physiology, biochemistry, and pathology. 2019:279-291. (2) Mustafa, Adv Pharmacol. San Diego, Calif:445-457. (3) Eiden et al., Pflungers Arch. 2018 Jan;470(1):79-88. (4) Braas et al., J Biol Chem. 1999 Sep 24;274(39):27702-27710. (5) Condro et al., J Comp Neurol. 2016 Dec 15; 524(18):3827-3848.



2002 ◽  
Vol 69 (3) ◽  
pp. 1213-1218 ◽  
Author(s):  
M. C. Olianas ◽  
A. Ingianni ◽  
V. Sogos ◽  
P. Onali


Endocrinology ◽  
2006 ◽  
Vol 147 (2) ◽  
pp. 791-803 ◽  
Author(s):  
E. R. Gillard ◽  
M. León-Olea ◽  
S. Mucio-Ramírez ◽  
C. G. Coburn ◽  
E. Sánchez-Islas ◽  
...  

Central release of vasopressin (VP) by the magnocellular neuroendocrine cells (MNCs) responsible for systemic VP release is believed to be important in modulating the activity of these neurons during dehydration. Central VP release from MNC somata and dendrites is stimulated by both dehydration and pituitary adenylate cyclase activating polypeptide (PACAP). Although PACAP is expressed in MNCs, its potential role in the magnocellular response to dehydration is unexplored. The current study demonstrates that prolonged dehydration increases immunoreactivity for PACAP-27, PACAP-38, and the type I PACAP receptor in the supraoptic nucleus (SON) of the rat. In addition, PACAP stimulates local VP release in the euhydrated rat SON in vitro, and this effect is reduced by the PACAP receptor antagonist PAC6–27 (100 nm), suggesting the participation of PACAP receptors. Concomitant with its effects on local VP release, PACAP also reduces basal glutamate and aspartate release in the euhydrated rat SON. Furthermore, somatodendritic VP release elicited by acute dehydration is blocked by PAC6–27, suggesting that endogenous PACAP participates in this response. Consistent with this, RIA revealed that local PACAP-38 release within the SON is significantly elevated during acute dehydration. These results suggest that prolonged activation of hypothalamic MNCs is accompanied by up-regulation of PACAP and the type I PACAP receptor in these cells and that somatodendritic VP release in response to acute dehydration is mediated by activation of PACAP receptors by endogenous PACAP released within the SON. A potential role for PACAP in promoting efficient, but not exhaustive, systemic release of VP from MNCs during physiological challenge is discussed.





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