Evidence for alternative splicing of the chicken vasoactive intestinal polypeptide gene transcript

Talbot, Richard; Dunn, Ian; Wilson, Peter W.F.; Sang, Helen; Sharp, P J

doi:10.1677/jme.0.0150081

Cited by 38 publications

(21 citation statements)

References 29 publications

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“…As yet, there is no evidence for the presence of these processing mechanisms in mammals. In contrast, differential splicing occurs in chicken and turkey, in which the majority of the PHI exon is spliced away from the transcript (40,43). In this study, a novel splice variant (clone 13A) was isolated from goldfish, which revealed an in-frame 132-bp deletion resulting in the loss of the VIP-encoding exon containing also part of the bridging peptide (Fig.…”

Section: Structural Characterization Of Goldfish Prepro-vip/phi and Pmentioning

confidence: 83%

“…a glycine residue followed by two basic amino acid residues (39), indicating that the goldfish VIP is amidated at the C terminus. However, similar to the case in chicken (40), the C terminus of the goldfish PHI is not amidated because it lacks a glycine residue to act as an amide donor.…”

Section: Isolation Of Goldfish Prepro-phi/vip Cdnamentioning

confidence: 93%

“…Interestingly, the structures of goldfish PHIs appear to be more closely related to those of mammalian PHI/PHM (74 -78% identity) than those of avian PHI (59% identity). In chicken and turkey, the major form of transcripts is prepro-VIP (98%), which lacks the PHI-encoding region (40,43). A longer transcript, prepro-PHI/VIP, also exists but at much lower levels (about 2%).…”

Section: Structural Characterization Of Goldfish Prepro-vip/phi and Pmentioning

confidence: 99%

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Identification of a Potential Receptor for Both Peptide Histidine Isoleucine and Peptide Histidine Valine

Tse

2002

Endocrinology

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Peptide histidine isoleucine (PHI), peptide histidine valine (PHV), and vasoactive intestinal polypeptide (VIP) are cosynthesized from the same precursor and share high levels of structural similarities with overlapping biological functions. In this study, the first PHI/PHV receptor was isolated and characterized in goldfish. To study this receptor using homologous peptides, we have also characterized the goldfish prepro-PHI/VIP, and, surprisingly, a shorter transcript lacking the VIP coding region was isolated. A PHI/VIP precursor without the VIP coding sequence has never before been reported. peptide histidine isoleucine (PHI) are members of the pituitary adenylate cyclase-activating polypeptide (PACAP)/ glucagon family. These peptides share many structural and biological similarities. They are cosynthesized from a common precursor; colocalized in the central nervous, gastrointestinal, reproductive, and respiratory systems; and coreleased in response to stimulation (1-7). It is interesting to note that similar to PACAP-27 and PACAP-38, a C-terminally extended form of PHI, known as peptide histidine valine (PHV), is also present in high concentrations in the circulation (8), although the function of this peptide is still unclear.VIP and PHI mediate a number of similar physiological actions in many systems, but the potencies of PHI are one to three orders of magnitude lower than those of VIP in various studies (5, 9 -13). Thus, PHI has been considered a weak agonist for VIP. In the gastrointestinal system, they both augment water and electrolyte transport in the jejunum (9, 14) and glucagon release from the pancreas (15). In the neuroendocrine system, they stimulate the secretion of PRL in the pituitary (10) and increase melatonin synthesis in the pineal gland (12). In the reproductive system, both peptides inhibit fallopian smooth muscle activity (5). In the vascular system, they produce an increase in vertebral artery blood flow (13).The biological effects of VIP are mediated through at least two receptor subtypes, termed VPAC1-R (16) and VPAC2-R (17), that exhibit high affinity for both VIP and PACAP. A third receptor, termed PAC1-R, that possesses high affinity for PACAP but a much lower affinity for VIP has been characterized (18). Up to now, a selective PHI receptor has not been identified, and it was generally accepted that the effects of PHI were mediated through VIP receptors. As a matter of fact, there is evidence that PHI shares common receptors with VIP: 1) PHI has been reported to bind VIP-preferring sites in many preparations (19 -21); 2) maximal doses of PHI and VIP do not produce additive effects (5, 10 -13, 16); and 3) cross-desensitization of PHI and VIP has been demonstrated (11,12,21). Thus, it is likely that at least some of the actions of PHI are mediated by binding to VIP-preferring sites. However, there are examples indicating that the biological responses to PHI are distinct from those evoked by VIP: 1) PHI injection in the preoptic area of rats facilitates LH secretion, whereas VIP inj...

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Section: Structural Characterization Of Goldfish Prepro-vip/phi and Pmentioning

confidence: 83%

Section: Isolation Of Goldfish Prepro-phi/vip Cdnamentioning

confidence: 93%

Section: Structural Characterization Of Goldfish Prepro-vip/phi and Pmentioning

confidence: 99%

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Identification of a Potential Receptor for Both Peptide Histidine Isoleucine and Peptide Histidine Valine

Tse

2002

Endocrinology

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“…The gene of the vasoactive intestinal peptide (VIP) is alternatively spliced into a large form encoding both VIP and peptide histidine isoleucine (PHI) 1-27 in the same protein product. The shorter form of chicken and turkey VIP mRNA encodes a protein that does not contain PHI (36,37). The prepro-tachykinin gene encodes several tachykinin peptides (SP, neurokinin A, neuropeptide P, and neuropeptide K) with distinct pharmacological properties (38).…”

Section: Discussionmentioning

confidence: 99%

“…Plasma extravasation was used as an index of inflammatory edema formation and measured as previously described (49). Briefly, test agents [SP, CGRP, galanin, GALP (1-60), GALP (19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37), alarin , and alarin (3-25)] were diluted in Tyrode's solution and stored on ice. 125 I-BSA (45 kBq in 100 l of saline) was administered i.v.…”

Section: Methodsmentioning

confidence: 99%

Alarin is a vasoactive peptide

Santic¹,

Schmidhuber²,

Lang

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Galanin-like peptide (GALP) is a hypothalamic neuropeptide belonging to the galanin family of peptides. The GALP gene is characterized by extensive differential splicing in a variety of murine tissues. One splice variant excludes exon 3 and results in a frame shift leading to a novel peptide sequence and a stop codon after 49 aa. In this peptide, which we termed alarin, the signal sequence of the GALP precursor peptide and the first 5 aa of the mature GALP are followed by 20 aa without homology to any other murine protein. Alarin mRNA was detected in murine brain, thymus, and skin. In accordance with its vascular localization, the peptide exhibited potent and dose-dependent vasoconstrictor and anti-edema activity in the cutaneous microvasculature, as was also observed with other members of the galanin peptide family. However, in contrast to galanin peptides in general, the physiological effects of alarin do not appear to be mediated via the known galanin receptors. Alarin adds another facet to the surprisingly high-functional redundancy of the galanin family of peptides.galanin-like peptide ͉ regulatory peptide ͉ splicing ͉ plasma extravasation ͉ cutaneous microvasculature

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Sites of gene expression for vasoactive intestinal polypeptide throughout the brain of the chick (Gallus domesticus)

et al. 1997

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The peptide neurotransmitter vasoactive intestinal polypeptide (VIP) has several important functions in vertebrates, particularly, influencing the neuroendocrine and autonomic nervous systems both in developing and in adult animals. To document potential brain areas that might play significant functional roles, the distribution of VIP mRNA was examined throughout the entire chick brain by using in situ hybridization histochemistry (ISHH). In addition, a VIP binding-site study was completed that focused on the lateral septal organ (LSO), a circumventricular organ of potential significance in avian species. The areas where VIP message was found included the olfactory bulbs, posterior hippocampus, parahippocampal area, hyperstriatum, archistriatum/nucleus (n.) taenia (amygdala), medial part of the LSO, organum vasculosum of the lamina terminalis, medial preoptic region, bed n. of the pallial commissure, anterior hypothalamic (hypo.) n., lateral hypo. area (most extensive and dense message), periventricular hypo. n., lateral to the paraventricular n., ventromedial hypo. n., stratum cellulare externum, inferior hypo. n., infundibular hypo. n., median eminence, three layers within the stratum griseum et fibrosum superficiale, area ventralis of Tsai, n. tegmenti pedunculopontinus pars compacta (substantia nigra), intercollicular n., central gray, locus ceruleus, parabrachial n., ventrolateral medulla, reticular pontine area, in and about the n. vestibularis descendens. When compared with immunocytochemistry that detected the presence of the peptide product VIP, more areas of the brain were found to contain perikarya expressing VIP by using ISHH, particularly in the telencephalon and the mesencephalon. VIP binding sites were found in the lateral portion of the LSO where the blood-brain barrier is not fully developed. Hence, the LSO was found to contain neural elements that synthesize as well as bind VIP. VIP appears to be a useful peptide for defining major components of the visceral forebrain system in birds.

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Evidence for alternative splicing of the chicken vasoactive intestinal polypeptide gene transcript

Cited by 38 publications

References 29 publications

Identification of a Potential Receptor for Both Peptide Histidine Isoleucine and Peptide Histidine Valine

Identification of a Potential Receptor for Both Peptide Histidine Isoleucine and Peptide Histidine Valine

Alarin is a vasoactive peptide

Sites of gene expression for vasoactive intestinal polypeptide throughout the brain of the chick (Gallus domesticus)

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