Effect of Activin A and Follistatin on the Release of Pituitary Hormones in the Bullfrog Rana catesbeiana

Koda, Aya; Yamamoto, Kazutoshi; Uchiyama, Hideho; Vaudry, Hubert; Kikuyama, Sakaé

doi:10.2108/zsj.17.971

Cited by 8 publications

(6 citation statements)

References 36 publications

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“…By the present experiment, fGRP was revealed to be another hypothalamic peptide possessing GHreleasing activity. Interestingly, TRH (39,40) and ghrelin (5) stimulate both GH and PRL release, whereas GHRH, PACAP (2), and fGRP (this experiment) stimulate only GH release. The existence of multiple GH-releasing peptides in the amphibian hypothalamus suggests that GH secretion in amphibians is under the multiple control in response to environmental stimuli and in relation to development, metamorphosis, and growth (41).…”

Section: Discussionmentioning

confidence: 69%

A Novel Amphibian Hypothalamic Neuropeptide: Isolation, Localization, and Biological Activity

et al. 2002

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Neuropeptides similar to the molluscan cardioexcitatory Phe-Met-Arg-Phe-NH2 have been identified in several vertebrates and characterized by the RFa motif at their C terminus (RFa peptides). In this study, we sought to identify an amphibian hypothalamic RFa peptide that may regulate secretion of hormones by the anterior pituitary gland. An acid extract of bullfrog hypothalami was passed through C-18 reversed-phase cartridges, and then the retained material was subjected to HPLC, initially using a C-18 reversed-phase column. RFa immunoreactivity was measured in the eluted fractions by a dot immunoblot assay employing an antiserum raised against RFa. Immunoreactive fractions were subjected to further cation exchange and reversed-phase HPLC purification. The isolated peptide was a novel RFa peptide and shown to have the sequence Ser-Leu-Lys-Pro-Ala-Ala-Asn-Leu-Pro-Leu-Arg-Phe-NH2. The cell bodies and terminals containing this peptide were localized immunohistochemically in the suprachiasmatic nucleus and median eminence, respectively. This RFa peptide stimulated, in a dose-related way, the release of GH from cultured pituitary cells, its threshold concentration ranging between 10(-9) and 10(-8) M. This peptide did not have any appreciable effect on the secretion of PRL and gonadotropins. It was ascertained that the peptide was also effective in elevating the circulating GH level when administered systemically. Thus, the amphibian hypothalamus was revealed to contain a novel functional RFa peptide that stimulates GH release. This peptide was designated frog GH-releasing peptide.

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Section: Discussionmentioning

confidence: 69%

A Novel Amphibian Hypothalamic Neuropeptide: Isolation, Localization, and Biological Activity

et al. 2002

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“…Other hypophysiotropic peptides in amphibians are known to release two hormones simultaneously. Bullfrog ghrelin that was recently isolated (17) as well as TRH (32,33) have a potency to stimulate both GH and PRL from the bullfrog pituitary. It was noted that there is some difference in the responsiveness to fGRP-RP-2 between GH and PRL cells.…”

Section: Discussionmentioning

confidence: 99%

Novel Neuropeptides Related to Frog Growth Hormone-Releasing Peptide: Isolation, Sequence, and Functional Analysis

et al. 2003

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We previously identified in the bullfrog a novel hypothalamic RFamide peptide (SLKPAANLPLRF-NH(2)) that stimulated GH release in vitro and in vivo and therefore was designated frog GH-releasing peptide (fGRP). Molecular cloning of cDNA encoding the deduced fGRP precursor polypeptide further revealed that it encodes fGRP and its related peptides (fGRP-RP-1, -RP-2, and -RP-3). In this study immunoaffinity purification using the antibody against fGRP was therefore conducted to determine whether these three putative fGRP-RPs exist as mature endogenous ligands in the frog brain. The mass peaks of the isolated immunoreactive substances were detected at 535.78, 1034.14, and 1079.71 m/z ([M+2H](2+)), and their sequences, SIPNLPQRF-NH(2), YLSGKTKVQSMANLPQRF-NH(2), and AQYTNHFVHSLDTLPLRF-NH(2), were revealed by the fragmentation, showing mature forms encoded in the cDNA sequences of fGRP-RP-1, -RP-2, and -RP-3, respectively. All of these fGRP-RPs contained a C-terminal -LPXRF-NH(2) (X = L or Q) sequence, such as fGRP. This study further analyzed hypophysiotropic activities of the identified endogenous fGRP-RPs. Only fGRP-RP-2 stimulated, in a dose-related way, the release of PRL from cultured frog pituitary cells; its threshold concentration ranged from less than 10(-7) M. A similar stimulatory action of fGRP-RP-2 on GH release was evident. It was ascertained that fGRP-RP-2 was also effective in elevating the circulating GH and PRL levels when administered systemically. In contrast, fGRP-RPs did not have any appreciable effect on the release of gonadotropins. Thus, fGRP-RP-2 may act as a novel hypothalamic factor on the frog pituitary to stimulate the release of GH and PRL.

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“…In our recent study (Koda et al, 2002), fGRP was revealed to be another hypothalamic peptide that possessed GH‐releasing activity. Interestingly, TRH (Aida, Yamamoto, & Kikuyama, 1999; Koda et al, 2000) and ghrelin (Kaiya et al, 2001) stimulated GH and PRL release, whereas GHRH, PACAP (Montero et al, 2000), and fGRP (Koda et al, 2002) stimulated only GH release. The existence of multiple GH‐releasing peptides in the amphibian hypothalamus suggests that GH secretion in amphibians is under the control of multiple environmental stimuli and is regulated in relation to development, metamorphosis, and growth (Kikuyama et al, 2000).…”

Section: Function Of Lpxrf‐amide Peptidesmentioning

confidence: 99%

A new member of the hypothalamic RF‐amide peptide family, LPXRF‐amide peptides: Structure, localization, and function

Ukena

Tsutsui

2004

Mass Spectrometry Reviews

120

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Recently, we identified a novel hypothalamic neuropeptide with a C-terminal LPLRF-amide sequence in the quail brain. This avian neuropeptide was shown to inhibit gonadotropin release from the cultured anterior pituitary. This peptide is the first hypothalamic peptide that inhibited gonadotropin release reported in vertebrates. We, therefore, termed it gonadotropin-inhibitory hormone (GnIH). After this finding, we found that GnIH-related peptides were present in the brains of other vertebrates, such as mammals, amphibians, and fish. These GnIH-related peptides possessed a LPXRF-amide (X=L or Q) motif at their C-termini in all investigated animals. Mass spectrometric analyses combined with immunoaffinity chromatography were powerful techniques for the identification of mature endogenous LPXRF-amide peptides. The identified LPXRF-amide peptides were found to be localized in the hypothalamus and brainstem areas, and to regulate pituitary hormone release. Subsequently, cDNAs that encode LPXRF-amide peptides were characterized in vertebrate brains. In this review, we summarize the identification, localization, and function of a new member of the hypothalamic RF-amide peptide family, LPXRF-amide peptides in vertebrates. Recent studies on the receptors for LPXRF-amide peptides will also be reviewed.

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Effect of Activin A and Follistatin on the Release of Pituitary Hormones in the Bullfrog Rana catesbeiana

Cited by 8 publications

References 36 publications

A Novel Amphibian Hypothalamic Neuropeptide: Isolation, Localization, and Biological Activity

A Novel Amphibian Hypothalamic Neuropeptide: Isolation, Localization, and Biological Activity

Novel Neuropeptides Related to Frog Growth Hormone-Releasing Peptide: Isolation, Sequence, and Functional Analysis

A new member of the hypothalamic RF‐amide peptide family, LPXRF‐amide peptides: Structure, localization, and function

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