Molecular cloning, characterization of cDNA, and distribution of mRNA encoding the frog prohormone convertase PC1

Gangnon, Françoise; Danger, Jean-Michel; Jégou, Sylvie; Vieau, Didier; Seidah, Nabil G.; Vaudry, Hubert

doi:10.1002/(sici)1096-9861(19990308)405:2<160::aid-cne2>3.0.co;2-y

Cited by 17 publications

(16 citation statements)

References 80 publications

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“…All four peptides shared the C-terminal sequence LPXRF motif (with X representing L in nLPXRFa-2, and Q in nLPXRFa-1, -3 and -4). In the frog, it has been demonstrated that the proprotein convertases PC1 and PC2, which are responsible for the processing of neuropeptide precursors, are abundantly expressed in the brain, including the hypothalamus (Vieau et al 1998, Gangnon et al 1999. Several proprotein convertases (PCs) are usually considered to recognize and cleave a precursor polypeptide at the Lys/Arg-(Xaa) n -Lys/ Arg sequence (nZ0, 2, 4 or 6; reviewed in Seidah & Chretien (1999)).…”

Section: Discussionsupporting

confidence: 87%

Identification, localization and expression of LPXRFamide peptides, and melatonin-dependent induction of their precursor mRNA in the newt brain

Chowdhury¹,

Ubuka²,

Osugi³

et al. 2011

Journal of Endocrinology

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The existence of RFamide peptides with a C-terminal LPXRFamide (XZL or Q) motif has been identified in the brain of various vertebrate species. However, the presence of LPXRFamide peptides in the urodele brain is not yet known. In this study, we cloned a cDNA encoding the precursor of LPXRFamide peptides from the newt brain by a combination of 3 0 and 5 0 rapid amplification of cDNA ends. The deduced LPXRFamide peptide precursor consisted of 233 amino acid residues, encoding four putative LPXRFamide peptides. All the peptide sequences were flanked by a glycine C-terminal amidation signal and basic amino acid on each end as an endoproteolytic site. Mass spectrometric analyses detected a nonapeptide, two decapeptides and an octapeptide produced from the precursor polypeptide in the brain as endogenous ligands. In situ hybridization further revealed the cellular localization of newt LPXRFamide (nLPXRFa) precursor mRNA in the suprachiasmatic nucleus (SCN) in the newt hypothalamus. Immunocytochemistry showed a cluster of cell bodies restricted to the SCN and their terminals in the median eminence. To understand the regulatory mechanism of nLPXRFa peptide expression, we further analyzed the effect of melatonin on the expression of nLPXRFa precursor mRNA. Melatonin administration to newts increased the expression of nLPXRFa precursor mRNA in the diencephalon. These results indicate that the urodele hypothalamus possesses LPXRFamide peptides and the expression of LPXRFamide peptides is regulated by melatonin. The localization of nLPXRFa peptides further suggests that these peptides may be involved in the regulation of pituitary hormone release in newts.

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Section: Discussionsupporting

confidence: 87%

Identification, localization and expression of LPXRFamide peptides, and melatonin-dependent induction of their precursor mRNA in the newt brain

Chowdhury¹,

Ubuka²,

Osugi³

et al. 2011

Journal of Endocrinology

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“…Similar results were obtained with Rana ridibunda (Vieau et al, 1998;Gangnon et al, 1999). An in situ hybridization experiment with the antisense RNA of Xenopus PC2 also revealed that PC2 mRNAs were predominantly expressed in the pars intermedia of the Xenopus pituitary (Braks et al, 1992).…”

Section: Comparative Aspect Of Prohormone Convertasessupporting

confidence: 92%

“…The amino acid sequence homology between the bullfrog PC1 and R. ridibunda (Gangnon et al ., 1999), human (Creemers et al ., 1992), mouse , rat (Hakes et al ., 1991), anglerfish (Roth et al ., 1993), Amphioxus , Aplysia (Gorham et al ., 1990), and Hydra (Chan et al ., 1992) PC1 was 95.6%, 62.7%, 67.2%, 66.8%, 68.1%, 56.1%, 53.5%, and 41.5%, respectively. Similarly, the amino acid sequence homology between the bullfrog PC2 and R. ridibunda (Vieau et al ., 1998), Xenopus (Braks et al ., 1992), human (Smeekens et al ., 1990), mouse , rat (Hakes et al ., 1991), Amphioxus , ascidian (AB086187), Aplysia (Chun et al ., 1994), and snail (Smit et al ., 1992) PC2 was 95.5%, 90.4%, 85.9%, 84.2%, 84.2%, 71.6%, 64.6%, 60.2%, and 61.0%, respectively.…”

Section: Comparative Aspect Of Prohormone Convertasesmentioning

confidence: 99%

“…Amphioxus PC1 and PC2 are considered to be involved in the processing of many neuropeptides including pro-insulin-like peptide (a homologue of mammalian insulin/insulin-like growth factor), but the substrate-specificity of these convertases and (Gangnon et al ., 1999), human (Creemers et al ., 1992), mouse , rat (Hakes et al ., 1991), anglerfish (Roth et al ., 1993), Amphioxus , Aplysia (Gorham et al ., 1990), and Hydra (Chan et al ., 1992) PC1s are shown. From Yaoi et al .…”

Section: Comparative Aspect Of Prohormone Convertasesmentioning

confidence: 99%

“…This finding is mostly consistent with the reports concerning mammalian species (Seidah et al, 1990;Vieau et al, 1998;Gangnon et al, 1999). It is of interest that only PC1 mRNA was expressed in the bullfrog stomach and intestine, whereas PC2 mRNA was the only type in the testis.…”

Section: Comparative Aspect Of Prohormone Convertasesmentioning

confidence: 99%

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Molecular Cloning and Expression of Prohormone Convertases PC1 and PC2 in the Pituitary Gland of the Bullfrog, Rana catesbeiana

et al. 2003

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Ontogeny of pituitary adenylate cyclase-activating polypeptide (PACAP) in the frog (Rana ridibunda) tadpole brain: Immunohistochemical localization and biochemical characterization

et al. 2001

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The anatomic distribution and biochemical characteristics of the neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) were investigated in the central nervous system of the frog, Rana ridibunda, during development. Three to four days after hatching, at stages IV-VII, PACAP-immunoreactive perikarya were detected in the dorsal thalamus within the anterior ventral area, and a few fibers were found in the medial pallium. Positive cell bodies were first observed in the hypothalamus at stages VIII-IX, at the level of the dorsal and ventral infundibular nuclei. In these regions, the number of positive perikarya increased during ontogeny. In tadpoles, during the mid- and late premetamorphosis, a more complex organization of the PACAP-immunoreactive system was found in the thalamus with the appearance, at stages IX-XII, of two additional groups of positive neurons in the ventrolateral area and posterocentral nucleus. At stages XIII-XVIII of larval development and subsequent larval stages, PACAP-immunoreactive fibers were found in the median eminence. In newly metamorphosed animals, several additional groups of positive perikarya appeared in the medial pallium, the preoptic nucleus, the torus semicircularis, the tegmentum of the mesencephalon, and the cerebellum. The immunoreactive peptide contained in the tadpole brain was characterized by high performance liquid chromatography analysis combined with radioimmunoassay quantification. At all stages investigated, the predominant form of PACAP-immunoreactive material coeluted with synthetic frog PACAP38. The occurrence of PACAP soon after hatching indicates that the peptide may exert neurotrophic activities. The existence of immunoreactive elements in several thalamic regions at mid- and late premetamorphic stages suggests that PACAP may act as a neurotransmitter, neuromodulator, or both, during ontogenesis. Finally, the presence of PACAP-immunoreactive perikarya in hypothalamic nuclei and nerve fibers in the median eminence supports the view that PACAP may play a role in the control of pituitary hormone secretion during larval development.

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Molecular cloning, characterization of cDNA, and distribution of mRNA encoding the frog prohormone convertase PC1

Cited by 17 publications

References 80 publications

Identification, localization and expression of LPXRFamide peptides, and melatonin-dependent induction of their precursor mRNA in the newt brain

Identification, localization and expression of LPXRFamide peptides, and melatonin-dependent induction of their precursor mRNA in the newt brain

Molecular Cloning and Expression of Prohormone Convertases PC1 and PC2 in the Pituitary Gland of the Bullfrog, Rana catesbeiana

Ontogeny of pituitary adenylate cyclase-activating polypeptide (PACAP) in the frog (Rana ridibunda) tadpole brain: Immunohistochemical localization and biochemical characterization

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