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

Yaoi, Yuichi; Suzuki, Masakazu; Tomura, Hideaki; Kikuyama, Sakaé; Tanaka, Shigeyasu

doi:10.2108/zsj.20.1139

Cited by 10 publications

(15 citation statements)

References 90 publications

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“…POMC, PC1, and PC2 genes were actively expressed in the pars intermedia of the pituitary gland, where they are involved in the processing of POMC, both in mammals and in anurans. 2,[6][7][8] This report demonstrates for the first time the presence of a POMC gonadal system in two amphibian models.…”

Section: Resultsmentioning

confidence: 54%

“…PCR products corresponding in length (base pairs, bp) to the primer-delimiting region were sequenced. 2,4…”

Section: Sequence Analysismentioning

confidence: 99%

“…1 In mammals as well as in anurans, PC1 and PC2 convertases are responsible for the cleavage of POMC in pituitary cells, where the expression of POMC, PC1, and PC2 genes was demonstrated. 2 Moreover, in the anuran Rana esculenta, the expression of a POMC gene and the presence of POMC-related peptides were found in gonads. 3,4 For Xenopus laevis, no data regarding gonadal POMC and its processing are available.…”

Section: Introductionmentioning

confidence: 99%

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Expression of Proopiomelanocortin and Its Cleavage Enzyme Genes in Rana esculenta and Xenopus laevis Gonads

Carotti¹,

Nabissi²,

Mosconi³

et al. 2005

Annals of the New York Academy of Sciences

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Proopiomelanocortin (POMC) is the precursor protein of different hormones and neuropeptides, and the POMC-derived peptides are produced through proteolytic cleavage. Prohormone convertase PC1 and PC2 are enzymes responsible for the cleavage of the POMC prohormone. The coexpression of POMC, PC1, and PC2 genes was previously described in the brain and the pituitary gland of Rana esculenta and Xenopus laevis, but no data are available for the gonad. The present work demonstrates a gonadal POMC convertase gene expression in Rana esculenta and Xenopus laevis.

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Section: Resultsmentioning

confidence: 54%

“…PCR products corresponding in length (base pairs, bp) to the primer-delimiting region were sequenced. 2,4…”

Section: Sequence Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression of Proopiomelanocortin and Its Cleavage Enzyme Genes in Rana esculenta and Xenopus laevis Gonads

Carotti¹,

Nabissi²,

Mosconi³

et al. 2005

Annals of the New York Academy of Sciences

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“…In a recent study, we created a cDNA library from bullfrog ( Rana cabesbeiana ) pituitary glands to clone and sequence 2 cDNAs encoding PC1 and PC2 (Yaoi et al ., 2003). Both PCs were structurally characterized as having a signal peptide, a prosegment, a catalytic region, a Pdomain, and a variable C-terminal region (Figs.…”

Section: Comparative Aspect Of Prohormone Convertasesmentioning

confidence: 99%

Comparative Aspects of Intracellular Proteolytic Processing of Peptide Hormone Precursors: Studies of Proopiomelanocortin Processing

Tanaka

2003

Zoological Science

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In this review, the mechanisms underlying the intracellular processing of peptide hormone precursors, with a focus on proopiomelanocortin (POMC), were discussed on the basis of recent information. POMC as well as other prohormones is processed to active peptides through proteolytic cleavage by prohormone convertases PC1 and/or PC2. However, the cleavage-specificity of PC1 and PC2 in mammals is somewhat different from that in amphibians. From the comparative endocrinological point of view, expression and tissue distribution of PC1 and PC2 were discussed here. In mammals, proteolytic processing of POMC occurs coordinately with the maturation of secretory granules. Studies using immunoelectron microscopy with DAMP (3-[2,4-dinitroanilino]-3'-amino-N-methyldipropylamine) as a pH probe revealed that the acidic pH in the secretory granules, generated by vacular type-H+-ATPase, provides a favorable environment for activating PC1 in AtT-20 cells, a mouse corticotrope tumor cell line. Recent data indicate that the 7B2 protein serves as a chaperone in the regulation of PC2 activation and to control the timing for activating the convertase. Together, secretory granules in endocrine and neuroendocrine cells provide proper sites for biosynthesizing hormones in addition to serving as storage sites and vehicles for the transport of peptide hormones.

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“…Previously, the distribution and expression of PC2 has been studied in the clawed frog [13], bullfrog [43], and medaka [38] by using in situ hybridization. An in situ hybridization experiment with the antisense mRNA in H. asinina PC2 revealed that PC2 mRNA transcripts were present in the cerebral and pleuropedal ganglia [18].…”

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confidence: 99%

Molecular characterization and spatiotemporal expression of prohormone convertase 2 in the Pacific abalone, Haliotis discus hannai

2020

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Prohormone convertases (PCs) are subtilisin-like proteases responsible for the intracellular processing of prohormones and proneuropeptides in vertebrates and invertebrates. The full-length PC2 cDNA sequence was cloned from pleuropedal ganglion of Haliotis discus hannai, consisted of 2254-bp with an open reading frame of 1989-bp and encoded a protein of 662 amino acid residues. The architecture of Hdh PC2 displayed key features of PCs, including a signal peptide, a pro-segment domain with sites for autocatalytic activation, a catalytic domain, and a pro-protein domain (P-domain). It shares the highest homology of its amino acid sequence with the PC2 from H. asinina and to lesser extent with that of Homo sapiens and Rana catesbeiana PC2. Sequence alignment analysis indicated that Hdh PC2 was highly conserved in the catalytic domain, including a catalytic triad of serine proteinases of the subtilisin family at positions Asp-195, His-236, and Ser-412. The cloned sequence contained a canonical integrin binding sequence, and four cysteine residues involved in the formation of an intramolecular disulfide link. Phylogenetic analysis revealed that the Hdh PC2 is robustly clustered with the Has PC2. Quantitative PCR assay demonstrated that the Hdh PC2 was predominantly expressed in the pleuropedal ganglion rather than in other examined tissues. Although PC2 mRNA was expressed throughout the gametogenetic cycle of male and female abalone, the expression level was significantly higher in the ripening stage of female abalone. Also, a significantly higher expression was observed in the pleuropedal ganglion and gonadal tissues at a higher effective accumulative temperature (1000˚C). In situ hybridization revealed that the PC2 mRNA expressing neurosecretory cells were distributed in the cortex region of the pleuropedal ganglion. According to the results, it can be concluded that pleuropedal ganglion is the highest site of PC2 activity, and this enzyme might be involved in the abalone reproduction process.

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

Cited by 10 publications

References 90 publications

Expression of Proopiomelanocortin and Its Cleavage Enzyme Genes in Rana esculenta and Xenopus laevis Gonads

Expression of Proopiomelanocortin and Its Cleavage Enzyme Genes in Rana esculenta and Xenopus laevis Gonads

Comparative Aspects of Intracellular Proteolytic Processing of Peptide Hormone Precursors: Studies of Proopiomelanocortin Processing

Molecular characterization and spatiotemporal expression of prohormone convertase 2 in the Pacific abalone, Haliotis discus hannai

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