Neuropeptide Y in the intermediate lobe of the frog pituitary acts as an α-MSH-release inhibiting factor

Danger, Jean-Michel; Leboulenger, F.; Guy, Jocelyne; Tonon, Marie‐Christine; Benyamina, M.; Martel, Jean-Claude; Saint-Pierre, Serge; Pelletier, Georges; Vaudry, Hubert

doi:10.1016/0024-3205(86)90350-4

Cited by 85 publications

(43 citation statements)

References 33 publications

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“…Moreover, intra-aortic injection of synthetic NPY to freely moving Xenopus causes skin bleaching in black background-adapted animals (D. Boujard, J.-M.D., and H.V., unpublished work). These observations, together with the occurrence of a dense network of nerve fibers exhibiting NPY-like immunoreactivity in the pars intermedia of amphibians (18,19), support the concept that the peptide isolated from frog brain tissue plays a physiological role in the regulation of pituitary melanotrophs.…”

Section: Resultssupporting

confidence: 67%

“…This suggests that the peptide we have isolated actually corresponds to authentic frog NPY. This hypothesis is supported by physiological studies which showed that porcine NPY is a potent inhibitor of a-melanotropin release from pituitary melanotrophs in frog (18) and toad (19). Biologically, frog melanostatin and the closely related mammalian NPY species exhibit many properties expected of a putative melanotropin-release-inhibiting factor.…”

Section: Resultsmentioning

confidence: 85%

“…Although the pars intermedia of various species is richly innervated by oxytocincontaining (14) or mesotocin-containing (15,16) fibers, neither oxytocin (17) nor mesotocin (16) can account for the inhibitory control of pituitary melanotrophs. In contrast, porcine neuropeptide Y (NPY) appears to be a potent inhibitor of a-melanotropin release in frog (18) and toad (19). Several other regulatory peptides characterized from hypothalamic extracts have been proposed as potential regulators of melanotropin release (20)(21)(22).…”

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confidence: 99%

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Characterization of melanotropin-release-inhibiting factor (melanostatin) from frog brain: homology with human neuropeptide Y.

Chartrel¹,

Conlon²,

Danger³

et al. 1991

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

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A polypeptide was purified from frog brain extracts on the basis of its ability to inhibit a-melanotropin release from perifused frog neurointermediate lobes. Based on Edman degradation, amino acid analysis, and peptide mapping, the primary structure of this frog melanotropin-releaseinhibiting factor (melanostatin) was determined to be H-TyrPro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-GluAsp-Met-Ala-Lys-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-AsnLeu-Ile-Thr-Arg-Gln-Arg-Tyr-NH2. Frog melanostatin belongs to the pancreatic polypeptide/neuropeptide Y/peptide YY family, and the structure of this peptide differs from that of human neuropeptide Y by only one amino acid substitution in position 19. A synthetic replicate of frog melanostatin is coeluted with the native peptide on HPLC and is highly potent in inhibiting a-melanotropin secretion in vitro (IC50 = 60 nM).Both the anterior lobe and the intermediate lobe of the pituitary are regulated by hypophysiotropic factors originating from the hypothalamus (1, 2). Five families of hypothalamic neuropeptides involved in the control of anterior pituitary hormone secretion have now been characterized, namely, thyrotropin-releasing hormone (3, 4), gonadotropinreleasing hormone (5), somatostatin (6), corticotropinreleasing hormone (7), and growth hormone-releasing hormone (8,9 (20)(21)(22). However, many studies failed to demonstrate that these peptides meet the criteria expected of a physiological melanotropin-release-inhibiting factor (melanostatin) (23)(24)(25). We report here the purification, sequence analysis, and total synthesis of a 36-residue peptide that is highly potent in inhibiting the secretion of a-melanotropin from frog neurointermediate lobe in vitro. MATERIALS AND METHODSPurification Procedure. Adult frogs (Rana ridibunda) were obtained from a commercial source (Coudtard, St-Hilaire de Riez, France). The brains from 1200 animals (94.5 g, wet weight) were collected on dry ice and kept frozen. The tissue was boiled for 15 min in 0.5 M acetic acid and homogenized in a Waring blendor. After centrifugation (10,000 x g for 30 min at 40C), the supernatant was pumped at a flow rate of 2 ml/min through ten Sep-Pak C18 cartridges (Waters Associates) connected in series. Bound material was eluted with 70% (vol/vol) acetonitrile in water and lyophilized. The dry extract was dissolved in 10 ml of 1% (vol/vol) trifluoroacetic acid and chromatographed on a 2.5 x 100-cm column of Sephacryl S-100 (Pharmacia-LKB) equilibrated with 1 M acetic acid at a flow rate of 2 ml/min. Fractions (10 ml) were collected and absorbance was measured at 280 nm (Fig. 1A).The fractions exhibiting melanotropin-release-inhibiting activity were pooled and 50% of the total material was analyzed by HPLC.The active fraction was pumped at a flow rate of 2 ml/min onto a 1 x 25-cm Vydac 218 TP510 C18 column (The Separations Group) equilibrated with 0.1% trifluoroacetic acid and eluted at a flow rate of 2 ml/min, using the gradient indicated in Fig. 1B. Absorbance was measured at 214 and 280 ...

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Section: Resultssupporting

confidence: 67%

Section: Resultsmentioning

confidence: 85%

mentioning

confidence: 99%

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Characterization of melanotropin-release-inhibiting factor (melanostatin) from frog brain: homology with human neuropeptide Y.

Chartrel¹,

Conlon²,

Danger³

et al. 1991

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

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“…Recent studies have revealed that NPY is also a very potent blocker of spontaneously occurring intracellular Ca2+ oscillations in isolated Xenopus melanotropes kept in vitro (25,27). Several studies in central and peripheral tissues indicate that NPY acts in both mammals and nonmammals (6,18,22), generally acting via in hibition of adenylyl cyclase activity (1,18,19,29,34). For Xeno pus melanotropes it was found that spontaneous Ca2+ oscillations depend on Ca2+ influx through cj-conotoxin-sensitive Ca2+ chan nels (24,28).…”

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confidence: 99%

Neuropeptide Y inhibits Ca2+ oscillations, cyclic AMP, and secretion in melanotrope cells of Xenopus laevis via a Y1 receptor

et al. 1995

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“…We report here the isolation, characterization, and total synthesis of a 36-residue polypeptide, which shows 94% identity with R. ridibunda PYY (33). We also show that the synthetic replicate inhibits melanotropin (a-melanocytestimulating hormone, a-MSH) release from frog pars intermedia in very much the same way as NPY (32,36,37). This peptide has been called skin peptide tyrosine-tyrosine (SPYY).…”

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confidence: 99%

Skin peptide tyrosine-tyrosine, a member of the pancreatic polypeptide family: isolation, structure, synthesis, and endocrine activity.

Mor

Chartrel

Vaudry

et al. 1994

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

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Pancreatic polypeptide, peptide tyrosinetyrosine (PYY), and neuropeptide tyrosine (NPY), three members of a family of structurally related peptides, are mainly expressed in the endocrine pancreas, in endocrine cells of the gut, and in the brain, respectively. In the present study, we have isolated a peptide of the pancreatic polypeptide family from the skin of the South American arboreal frg Phylomedusa bicolor. The primary structure of the peptide was established as Tyr-Pro-Pro-Lys-Pro-Glu-Ser-Pro-Gly-Glu'O-AspAla-Ser-Pro-Glu-Glu-Met-Asn-Lys-Tyr2O-Leu-Thr-Ala-LeuArg-His-Tyr-Be-Asn-Leu3O-Val-Thr-Arg-Gln-Arg-Tyr-NH2. (2). These peptides generally belong to families of biologically active peptides, which have their counterparts in mammals, such as tachykinins (3, 4), bradykinins (5, 6), angiotensin (7), caerulein/cholecystokinin (8), bombesin/gastrin-releasing peptide (9), opioid peptides (10), antimicrobial peptides (11,12), and hypophysiotropic neuropeptides (13,14). Although the physiological role of the various peptides synthesized and released by dermatous granular glands remains largely unknown, most of these peptides are produced in such enormous quantities that it is often possible to isolate enough material from a single skin to determine the amino acid sequence (15,16).The pancreatic polypeptide (PP) family consists of three members of structurally related peptides, which all possess 36 amino acid residues, exhibit a C-terminal tyrosine amide moiety, and share common features of tertiary structure: (i) PP, originally discovered in the chicken pancreas (17), is exclusively localized in endocrine cells of pancreatic islets (18); (ii) peptide tyrosine-tyrosine (PYY), initially isolated from pig intestine (19), is primarily synthesized in gut endocrine cells (20) as well as in brainstem neurons (18) (23)(24)(25)(26)(27)(28)(29), suggesting that the genes encoding these two peptides arose from early duplication of an ancestral gene (30). In contrast, PP-like peptide is absent in fish and, therefore, it has been proposed that the PP gene arose from duplication of the PYY gene at the time of emergence of amphibians (30). The primary structures of all three members of the PP family have recently been determined in the frogs Rana catesbeiana (31) and Rana ridibunda (32, 33). However, the occurrence of PP-related peptides has never been reported in the skin of amphibians.We have recently undertaken the purification of a series of unusual polypeptides from the skin of the frog Phyllomedusa bicolor, using their antifungal activity as a biological test (34,35). We report here the isolation, characterization, and total synthesis of a 36-residue polypeptide, which shows 94% identity with R. ridibunda PYY (33). We also show that the synthetic replicate inhibits melanotropin (a-melanocytestimulating hormone, a-MSH) release from frog pars intermedia in very much the same way as NPY (32,36,37). This peptide has been called skin peptide tyrosine-tyrosine (SPYY). MATERIALS AND METHODSPurification of SPYY from Frog S...

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Neuropeptide Y in the intermediate lobe of the frog pituitary acts as an α-MSH-release inhibiting factor

Cited by 85 publications

References 33 publications

Characterization of melanotropin-release-inhibiting factor (melanostatin) from frog brain: homology with human neuropeptide Y.

Characterization of melanotropin-release-inhibiting factor (melanostatin) from frog brain: homology with human neuropeptide Y.

Neuropeptide Y inhibits Ca2+ oscillations, cyclic AMP, and secretion in melanotrope cells of Xenopus laevis via a Y1 receptor

Skin peptide tyrosine-tyrosine, a member of the pancreatic polypeptide family: isolation, structure, synthesis, and endocrine activity.

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