Molecular cloning and characterization of cDNA for the precursor of rat pituitary adenylate cyclase activating polypeptide (PACAP)

Ogi, Kazuhiro; Kimura, Chiharu; Onda, Haruo; Arimura, Akira; Fujino, Masahiko

doi:10.1016/s0006-291x(05)80924-6

Cited by 219 publications

(67 citation statements)

References 19 publications

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“…The signal peptide of the salmon GHRHPACAP precursor has a hydrophobic core and has two amino acids less than the signal peptide of the ovine [8], human [l, 81 and rat [9] PACAP precursors ( Fig. S2).…”

Section: Organization Of the Ghrwpacap Precursormentioning

confidence: 99%

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Two salmon neuropeptides encoded by one brain cDNA are structurally related to members of the glucagon superfamily

Parker

Coe

Dixon

et al. 1993

European Journal of Biochemistry

111

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A cDNA that codes for two peptides in the glucagon superfamily has been isolated from sockeye salmon brain. The first peptide is related to growth hormone-releasing hormone (GHRH), which has high sequence similarity with PACAP-related peptide. The second peptide is structurally related to vasoactive intestinal peptide, which is also related to a newly identified peptide in mannals, pituitary adenylate-cyclase-activating polypeptide (PACAP). The salmon precursor contains 173 amino acids and has dibasic and monobasic enzyme-processing sites for cleavage of a 45-aminoacid GHRH-like peptide with a free C-terminus and a 38-amino-acid PACAP with an amidated C-terminus. The salmon GHRH-like peptide has 40% amino acid sequence identity with the human GHRH and 56% identity with human PACAP-related peptide. The 38-amino-acid salmon PACAP is highly conserved (89-92% identity) with only three or four amino acid substitutions compared with the human, ovine and rat 38-amino-acid PACAP.Not previously reported for mammalian species, a short precursor coding for only one peptide exists in salmon in addition to the long precursor coding for two peptides. In the short precursor, the coding region for GHRH is deleted leaving the PACAP-coding region in a correct reading frame. This provides one possible control mechanism for an increased expression of one peptide (PACAP) without the concomitant increase in the other peptide (GHRH) as occurs in a double-peptide precursor. The importance of the 3' non-translated region of the salmon GHRWPACAP precursor in the regulation of translation is suggested by its 70% nucleotide sequence identity to the 3' non-translated regions of the mammalian PACAP precursors. The structural organization of the salmon GHRW PACAP precursor provides a possible evolutionary scheme for precursors that contain tandem peptides in the glucagon superfamily.The glucagon superfamily includes glucagon, vasoactive intestinal polypeptide (VIP), peptide histidine methionine (PHM), peptide histidine isoleucine (PHI), secretin, gastric inhibitory peptide, growth hormone-releasing hormone (GHRH), helospectin and helodermin. Recently, two new candidates, pituitary adenylate-cyclase-activating polypeptide (PACAP) and PACAP-related peptide (PRP) were identified in mammals. Structurally, they resemble VIP and GHRH, respectively. PACAP has been classified as a member of the glucagon superfamily not only because of the close sequence similarity with VIP and GHRH [l], but also because of the similarity of the PACAP-gene structure [2] to that of the VIP gene Abbreviations. ACTH, adrenocorticotropic hormone ; FSH. follicle stimulating hormone; GH, growth hormone; GHRH, growthhormone-releasing hormone ; human, h; LIB, library; PACAP, pituitary adenylate-cyclase-activating polypeptide; PCR, polymerase chain reaction ; PHI, peptide histidine isoleucine; PHM, peptide histidine methionine; PRP, PACAP-related peptide; RACE rapid amplification of cDNA ends; VIP, vasoactive intestinal peptide.Note. The novel nucleotide sequence data publish...

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Section: Organization Of the Ghrwpacap Precursormentioning

confidence: 99%

“…The cDNA has been cloned from ovine hypothalamus [8], human testis [l, 81 and rat brain [9]. The human gene has also been studied [2].…”

mentioning

confidence: 99%

Two salmon neuropeptides encoded by one brain cDNA are structurally related to members of the glucagon superfamily

Parker

Coe

Dixon

et al. 1993

European Journal of Biochemistry

111

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“…cDNA cloning of the PACAP precursor from ovine, rat and human sources revealed that the primary structures of human [3] and rat [4] PACAP molecules are identical to the ovine peptide, suggesting a highly conserved and crucial role as a neuropeptide and/or as a gastrointestinal hormone. In superfused rat pituitary cells, PACAP stimulates the release of adrenocorticotropin, growth hormone, prolactin and luteinizing hormone [2].…”

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confidence: 99%

Characterization of a guanosine‐nucleotide‐binding‐protein‐coupled receptor for pituitary adenylate‐cyclase‐activating polypeptide on plasma membranes from rat brain

Schäfer

Schwarzhoff

Creutzfeldt

et al. 1991

European Journal of Biochemistry

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Pituitary adenylate-cyclase-activating polypeptide (PACAP), a novel brain-gut hormone, was isolated from ovine hypothalami and represents the latest mammalian member of the secretinglucagon peptide family. PACAP exists in two C-terminally amidated molecular forms, PACAP(1-27) and PACAP(1-38), comprising 27 or 38 amino acid residues, respectively. In order to identify a specific receptor for PACAP, we studied binding of '251-labelled PACAP(1-27) to plasma membranes from rat brain. We identified a single high-affinity binding site (Kd, 340 pM and B,,,, 3.34 pmol/mg), specific for synthetic PACAP(1-38) and PACAP(1-27). Hormone binding was reversible and time, protein and temperature dependent. In contrast, neither the analogues PACAP(1 -23), and PACAP(3 -25), nor vasoactive intestinal peptide (VIP), secretin and growth-hormone-releasing factor (GRF) revealed significant binding at concentrations up to 1 FM. A specific receptor protein, with an apparent molecular mass of 60 kDa, was identified by means of affinity cross-linking with disuccinimidyl suberate (DSS) and ethylene glycol disuccinimidyl suberate (EGS). PACAP receptors are associated with a GTP-binding protein as determined by the influence of different nucleotides on PACAP binding. PACAP-binding activity was solubilized with the detergents 3-[(3-cholamidopropyl)dimethylammonio]2-hydroxy-l -propane sulfonate (Chapso) or Triton X-100 and was characterized as a high-molecular-mass receptor complex (400 kDa) by nonreducing size-exclusion chromatography on Sepharose CL-6B. These data imply the following: high-affinity PACAP receptors are expressed abundantly on rat-brain plasma membranes; PACAP receptors are specific for PACAP and show no affinity for VIP, secretin and GRF; the PACAP receptor molecule has an apparent molecular mass of 60 kDa; the PACAP receptor complex is associated with a GTP-binding protein. Pituitaryadenylate-cyclase-activating polypeptide (PACAP) has been recently isolated from ovine hypothalamic extracts [l]. This C-terminally amidated peptide comprises 38 or 27 amino acid residues and reveals a high potency for adenylate-cyclase activation on rat pituitary cells [2]. PACAP(1-27) possesses full biological activity and shows 68% similarity to vasoactive intestinal peptide (VIP). Therefore, PACAP is regarded as a novel member of the secretin- Dedication. This publication is dedicated to Prof. Dr Norbert Hilschmann, Max-Planck-Institute for Experimental Medicine, Gottingen on the occasion of his 60th birthday. glucagon family, a group of structurally related regulatory peptides.cDNA cloning of the PACAP precursor from ovine, rat and human sources revealed that the primary structures of human [3] and rat [4] PACAP molecules are identical to the ovine peptide, suggesting a highly conserved and crucial role as a neuropeptide and/or as a gastrointestinal hormone. In superfused rat pituitary cells, PACAP stimulates the release of adrenocorticotropin, growth hormone, prolactin and luteinizing hormone [2]. However, the regional distribution of PACA...

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“…The PACAP cDNA has been cloned in several mammalian Ogi et al 1990;Okazaki et al 1995) and non-mammalian vertebrates (McRory et al 1995;McRory and Sherwood 1997;Alexandre et al 2000;Fradinger and Sherwood 2000). PACAP and growth hormone-releasing hormone (GRF) are encoded within the same gene in non-mammalian vertebrates including birds.…”

Section: Introductionmentioning

confidence: 99%

Pituitary adenylate cyclase activating peptide (PACAP) immunoreactivity and mRNA expression in the duck gastrointestinal tract

Mirabella

Squillacioti

Colitti

et al. 2002

Cell and Tissue Research

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The presence and distribution of pituitary adenylate cyclase activating peptide (PACAP) immunoreactivity were studied in the duck gastrointestinal tract using immunohistochemistry and radioimmunoassays. Expression and distribution of PACAP mRNA were also studied using reverse transcriptase polymerase chain reaction (RT-PCR) and hybridization techniques. In addition, a partial coding sequence (cds) of the duck growth hormone-releasing hormone (GRF)/PACAP gene was identified. The presence of both PACAP-38 and PACAP-27 was demonstrated, the former being the predominant form. PACAP immunoreactivity was found in neurons and fibers of the enteric nervous system (ENS), in endocrine cells and in the gut associated lymphoid tissue (GALT). Double immunostaining showed that PACAP is almost completely colocalized with vasoactive intestinal peptide (VIP) in the ENS. Moreover, PACAP was also found in nitric oxide synthase (NOS)-containing neurons and nerve fibers. Radioimmunoassay (RIA) performed on denervated gut showed that more than one-half of the duodenal PACAP is extrinsic in origin. RT-PCR, Northern blot analysis and in situ hybridization confirmed the immunohistochemical data. The findings of the present study suggest that, in birds, PACAP may have multiple roles in regulating gastrointestinal functions.

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Molecular cloning and characterization of cDNA for the precursor of rat pituitary adenylate cyclase activating polypeptide (PACAP)

Cited by 219 publications

References 19 publications

Two salmon neuropeptides encoded by one brain cDNA are structurally related to members of the glucagon superfamily

Two salmon neuropeptides encoded by one brain cDNA are structurally related to members of the glucagon superfamily

Characterization of a guanosine‐nucleotide‐binding‐protein‐coupled receptor for pituitary adenylate‐cyclase‐activating polypeptide on plasma membranes from rat brain

Pituitary adenylate cyclase activating peptide (PACAP) immunoreactivity and mRNA expression in the duck gastrointestinal tract

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