The effect of rat galanin in rats

Be, Dunning; Gj, Taborsky

doi:10.1007/bf00401053

Cited by 6 publications

(10 citation statements)

References 3 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%

“…2). Immunostainings of IR-galanin containing cells in rat pyloric sphincter on serial sections using anti-rat preprogalanin(89-124) serum RY193(1:14,000 dilution) (top), anti-rat galanin serum Y182 (1:8,000 dilution) (middle), and anti-rat galanin (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29) serum Y183 (bottom).…”

Section: Immunoreactive Galmentioning

confidence: 99%

“…[16][17][18] Gal also inhibits basal and stimulated insulin secretion in the mouse 19,20 and rat. [21][22][23] We investigated the correlation between the structure of Gal and its activity on insulin release by the use of various synthetic Gal fragments. Gal lacking Gly 1 did not inhibit insulin (IRI) release from the isolated perfused rat pancreas.…”

Section: Effects Of Gal and Its Fragments On Insulin Releasementioning

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.…”

mentioning

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.…”

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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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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