Galanin and Pancreastatin Inhibit Stimulated Insulin Secretion in the Mouse: Comparison of Effects

Lindskog, Stefan; Åhrén, Bo

doi:10.1159/000181010

Cited by 21 publications

(14 citation statements)

References 16 publications

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“…We previously produced Gal monoclonal antibodies that can discriminate immunoreactive Gal from other structurally related peptides. 2 In the study we used four kinds of new antisera against Gal (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15), rat Gal , rat Gal (20)(21)(22)(23)(24)(25)(26)(27)(28)(29), and preproGal(89-124) with the COOH-terminal 89-124 sequence of rat Gal mRNA-associated peptide, respectively. These antisera were extremely valuable for detection of Gal-containing nerve fibers (FIG.…”

Section: Immunoreactive Galmentioning

confidence: 99%

“…Gal stimulates the release of growth hormone (GH), 7,8 prolactin, 9 and luteinizing hormone either from dispersed pituitary cells or at the hypothalamic level modulating dopamine, vasoactive intestinal polypeptide, (VIP), somatostatin, opioid, and GnRH release into the portal circulation 10-13 and inhibits insulin release. [14][15][16][17][18][19][20][21][22][23] In this review, we describe structure-function studies of the endocrine and gastrointestinal action of Gal.…”

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confidence: 99%

“…Rabbits were bled from the marginal ear vein at 10 days after each immunization. Anti-Gal(1-15) serum, anti-rat Gal(1-29) serum, anti-rat Gal (20)(21)(22)(23)(24)(25)(26)(27)(28)(29) serum, and anti-preproGal(89-124) thus obtained were used in the study.…”

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confidence: 99%

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Endocrine and Gastrointestinal Action of Galanin

Yanaihara

Mochizuk

Kuwahara

et al. 1998

Annals of the New York Academy of Sciences

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apid advances in the field of peptide chemistry and gene technology have resulted in a burst of determinations about the molecular structures not only of regulatory peptides such as galanins (Gal) of various species but also of their precursors and receptors. Based on information about mature peptides and precursor structures, Gal-related peptides and other peptides with related amino acid sequences were synthesized. Certain specifically designed synthetic peptides have enabled the investigation of such questions as the molecular basis of receptor binding and the active role of peptides. 1 Synthetic replicates of Gal of various species and its precursor-related peptides provide us with important immunogens for producing region-specific antibodies. Specific antibodies against Gal or its precursor-related peptides demonstrate well the posttranslational biosynthetic processing in cells and identify steps in the metabolite pathway of the regulatory peptide in tissues and tissue fluids. 2,3 Exogenous administration of Gal has been shown to contract smooth muscle preparations 3-6 and to inhibit neurally induced smooth muscle contractility. Gal stimulates the release of growth hormone (GH), 7,8 prolactin, 9 and luteinizing hormone either from dispersed pituitary cells or at the hypothalamic level modulating dopamine, vasoactive intestinal polypeptide, (VIP), somatostatin, opioid, and GnRH release into the portal circulation 10-13 and inhibits insulin release. [14][15][16][17][18][19][20][21][22][23] In this review, we describe structure-function studies of the endocrine and gastrointestinal action of Gal. PEPTIDES AND ANTISERAPeptides. All peptides used in the study were synthesized by solid phase methodology with BOC-or Fmoc-strategy using an automated peptide synthesizer (model 430A, Applied Biosystems, or model 9050, Perseptive, USA). The crude peptide was purified by reverse-phase HPLC on a column of YMC-Pack D-ODS-5 (2.0 × 25.0 cm) using 0.01 N HCl/CH 3 CN. Purity of the peptides was assessed by analytic HPLC on a column of YMC

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Section: Immunoreactive Galmentioning

confidence: 99%

mentioning

confidence: 99%

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Endocrine and Gastrointestinal Action of Galanin

Yanaihara

Mochizuk

Kuwahara

et al. 1998

Annals of the New York Academy of Sciences

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“…Porcine pancreastatin and the C-terminal fragment [33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49] were reported to enhance memory retention after peripheral administration of the peptide in mice via an undefined mechanism (75).…”

Section: Other Biological Activitiesmentioning

confidence: 99%

“…An initial biological screening revealed that natural porcine pancreastatin [ 1 -491 inhibited glucose-induced insulin release from the isolated perfused rat pancreas ( I). This activity, which was observed on the first phase and to a lesser degree on the second phase of insulin release, could be assigned to the C-terminal part of the molecule since pancreastatin [ 14-491 and pancreastatin [33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49], derived by proteolytic cleavage of the parent molecule at single basic residues. showed equal or slightly higher potency (1).…”

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Pancreastatin—A Novel Regulatory Peptide?

Schmidt

Creutzfeldt

1991

Acta Oncologica

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Pancreastatin is a 49 amino acid peptide originally isolated from porcine pancreas on the basis of its C-terminal glycinamide as isolation criterion. It is derived by proteolytic processing from chromogranin A, an acidic protein component of secretory granules in endocrine and neuronal cells. The primary structures of human, porcine. bovine and rat pancreastatin have been determined on the protein or cDNA level and show 70% sequence homology. By immunocytochemistry, pancreastatin has been detected in the pituitary, adrenal gland, pancreas, CNS and throughout the gastrointestinal tract. In pancreatic islets, pancreastatin is co-localized with insulin, glucagon and somatostatin. The principle biological activities of this peptide are: inhibition of insulin release and of exocrine pancreatic secretion. These effects which can be assigned to the amidated C-terminal part of the molecule have been demonstrated in several species. Whether or not pancreastatin can be classified as a novel peptide hormone that under physiological conditions plays a role in the regulation of the endocrine and exocrine pancreas, is still a matter of controversy.Ke! w r d s : Pancreastatin, gastrointestinal peptide, regulatory peptide, chromogranin, insulin secretion, exocrine pancreatic secretion.Pancreastatin, a 49 amino acid residues comprising peptide with a C-terminal glycinamide, was isolated from porcine pancreatic extracts by Tatemoto and coworkers ( I ) . using a chemical detection assay for C-terminal amino acid amides as isolation method (2). Using this strategy a number of previously unknown peptide hormones and neuropeptides. i t . PHI, PYY, NPY and galanin, possessing this characteristic C-terminal structure, have been isolated from brain and intestinal extracts by Tatemoto & Mutt without any knowledge of their respective biological effects or physiological role (3-7). An initial biological screening revealed that natural porcine pancreastatin [ 1 -491 inhibited glucose-induced insulin release from the isolated perfused rat pancreas ( I). This activity, which was observed on the first phase and to a lesser degree on the second phase of insulin release, could be assigned to the C-terminal part of the molecule since pancreastatin [ 14-491 and pancreastatin [ 33-49], derived by proteolytic cleavage of the parent molecule at single basic residues. showed equal or slightly higher potency (1). The authors implicated by the name 'pancreastatin' that this 49-residue peptide may represent a novel regulatory pancreatic hormone with a physiological role in the control of insulin secretion and carbohydrate metabolism. Structure and molecular formsSoon it was recognized that porcine pancreastatin shows striking sequence homology to the central part of the cDNA-derived amino acid sequence of bovine chromogranin A, an acidic protein present in the secretory granules of endocrine and neuronal cells (8-10). It was speculated that chromogranin A may represent the prohormone precursor for pancreastatin ( 1 I , 12). This hypothesis was pr...

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