Cloning and Expression of a cDNA Encoding a Prolactin Receptor of the Japanese Red-Bellied Newt, Cynops pyrrhogaster

Yamamoto, Takashi; Nakayama, Yuki; Matsuda, Yoshiko; Abe, Shinichi

doi:10.2108/zsj.15.741

Cited by 23 publications

(19 citation statements)

References 35 publications

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“…To investigate the N-glycosylation of C. ensicauda PRLR expressed in the COS-7 cells, we have treated extracts with glycopeptidase F. When such extracts are subjected to Western blot analysis, the immunoreactive bands appear at positions of approximately 90 and 67 kDa. The size of the 67-kDa band is similar to the molecular weight of the putative newt PRLR calculated from the amino acid sequence deduced from newt PRLR cDNA (Matsukawa et al 2004;Yamamoto et al 1998). This suggests that the newt PRLR generated in COS-7 cells is glycosylated.…”

Section: Discussionsupporting

confidence: 62%

“…Western blot analysis with extracts of COS-7 cells in which C. ensicauda PRLR had been transiently expressed has revealed several immunoreactive bands ranging from 75 kDa to 100 kDa. As judged from the deduced amino acid sequences of newt PRLRs (both C. ensicauda and C. pyrrhogaster), these PRLRs have three potential N-glycosylation sites in their extracellular domain (Matsukawa et al 2004;Yamamoto et al 1998). To investigate the N-glycosylation of C. ensicauda PRLR expressed in the COS-7 cells, we have treated extracts with glycopeptidase F. When such extracts are subjected to Western blot analysis, the immunoreactive bands appear at positions of approximately 90 and 67 kDa.…”

Section: Discussionmentioning

confidence: 99%

“…C. ensicauda (Matsukawa et al 2004) and C. pyrrhogaster (Yamamoto et al 1998) PRL receptor (PRLR) cDNAs have recently been cloned. The deduced amino acid sequences of these two PRLRs consist of 626 amino acid residues with extremely high homology (98.9%).…”

Section: Introductionmentioning

confidence: 99%

“…The deduced amino acid sequences of these two PRLRs consist of 626 amino acid residues with extremely high homology (98.9%). PRLR mRNA has been detected in the brain of these two species, by use of Northern blot and reverse transcription/polymerase chain reaction (RT-PCR) techniques (Matsukawa et al 2004;Yamamoto et al 1998). However, the exact localization of PRLR in the newt brain remains unclear.…”

Section: Introductionmentioning

confidence: 99%

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Localization of prolactin receptor in the newt brain

et al. 2005

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In the male newt Cynops pyrrhogaster, prolactin (PRL) acts directly on the central nervous system and induces courtship behavior. As a step to elucidate the localization of neurons on which PRL acts, we developed a polyclonal antibody against an oligopeptide having a sequence completely identical with a part of the sequence of PRL receptors (PRLRs) of two species of newts, C. pyrrhogaster and C. ensicauda, and performed an immunohistochemical study with this antibody. PRLR-immunoreactive cells were observed in the medial amygdala, anterior preoptic area, magnocellular preoptic nucleus, suprachiasmatic nucleus, nucleus of the periventricular organ, ventral hypothalamic nucleus, and choroid plexus. We also performed in situ hybridization with a (35)S-labeled newt PRLR antisense RNA probe and detected signals in the preoptic area and choroid plexus. Colocalization of both PRLR-like immunoreactivity and arginine vasotocin-like or mesotocin-like immunoreactivity was demonstrated in the magnocellular preoptic nucleus. This is the first report of PRLR localization in the amphibian brain.

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Section: Discussionsupporting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Localization of prolactin receptor in the newt brain

et al. 2005

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“…PRLRs have also been cloned in an amphibian (Yamamoto et al, 1998), in a euryhaline teleost, Nile tilapia (Oreochromis niloticus) (tiPRLR) (Sandra et al, 1995), and in a fresh water teleost, the goldfish (Carassius auratus) (gf PRLR) (Tse et al, 2000). In tilapia there is a single transcript of 3.2 kb which shares greatest similarity with the long forms of mammalian PRLRs, although the overall homology is low (37%) (Sandra et al, 1995(Sandra et al, , 2000.…”

Section: Introductionmentioning

confidence: 99%

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Santos

Ingleton²,

Cavaco

et al. 2001

General and Comparative Endocrinology

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The prolactin receptor (PRLR) was cloned and its tissue distribution characterized in adults of the protandrous hermaphrodite marine teleost, the sea bream (Sparus aurata). An homologous cDNA probe for sea bream PRLR (sbPRLR) was obtained by RT-PCR using gill mRNA. This probe was used to screen intestine and kidney cDNA libraries from which two overlapping clones (1100 and 2425 bp, respectively) were obtained. These clones had 100% sequence identity in the overlapping region (893 bp) and were used to deduce the complete amino acid sequence of sbPRLR. The receptor spans 2640 bp and encodes a protein of 537 amino acids. Features characteristic of PRLR, two pairs of cysteines, WS box, hydrophobic transmembrane domain, box 1, and box 2, were identified and showed a high degree of sequence identity to PRLRs from other vertebrate species. SbPRLR is 29 and 32% identical to tilapia (Oreochromis niloticus) and goldfish (Carassius auratus) PRLRs, respectively. In the sea bream two PRLR transcripts of 2.8 and 3.2 kb were detected in the intestine, kidney, and gills and a single transcript of 2.8 kb was detected in skin and pituitary by Northern blot. Spermiating gonads (more than 95% male tissue; gonado-somatic index of 0.6) contained, in addition to the 2.8-kb transcript, three more transcripts of 1.9, 1.3, and 1.1 kb. RT-PCR, which is a far more sensitive method than Northern blot, detected PRLR mRNA in gills, intestine, brain, pituitary, kidney, liver, gonads, spleen, head-kidney, heart, muscle, and bone. Immunohistochemistry using specific polyclonal antibodies raised against an oligopeptide from the extracellular domain of sbPRLR detected PRLR in several epithelial tissues of juvenile sea bream, including the anterior gut, renal tubule, choroid membrane of the third ventricle, saccus vasculosus, branchial chloride cells, and branchial cartilage.

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Identification and characterization of newtrad (ras associated with diabetes), a gene specifically expressed in regenerating limb muscle

2001

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Formation of the blastema is a key event for limb regeneration in urodele amphibians, and skeletal muscle has been thought to be a major origin of the multipotent blastemal mesenchyme. In the present study, we used differential display to identify the genes expressed differentially in the muscle at the amputation site. We have isolated a cDNA clone that was upregulated during limb regeneration of the Japanese newt, Cynops pyrrhogaster. Deduced amino acid sequence revealed that the cloned cDNA was a newt homolog of rad (ras associated with diabetes), a gene overexpressed in skeletal muscle of Type II diabetic patients. Expression of newt rad (nrad) was not observed in unamputated normal limb muscle, increased within 4 hr after amputation, and then decreased to the level of normal muscle between 11 and 21 days after amputation. In situ hybridization showed that the transcripts of nrad were localized around most of the nuclei of skeletal muscle near the amputation site, indicating the expression of nrad in the multinucleate myotubes. This expression gradually decreased along the distal to proximal axis. No signals were observed in apical epidermal cap or blastemal mesenchyme. However, reverse transcription‐PCR analysis detected a very low level of nrad expression in blastema, suggesting the carry‐over of nrad expression in blastema from muscle. Administration of retinoic acid, which has been shown to cause an enhanced dedifferentiation in the regenerating limbs, increased nrad expression in more proximally located limb muscle tissues and prolonged the expression period. Thus, it was strongly suggested that the nrad expression is correlated with the dedifferentiation of myotubes of regenerating limbs. We also analyzed the expression of nrad during development. Transcripts were observed in immature oocytes, seen faintly or not seen thereafter until stage 57 when its expression increased again. These results indicated that nrad may play a role(s) in the developmental process as well as limb regeneration. © 2001 Wiley‐Liss, Inc.

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Cloning and Expression of a cDNA Encoding a Prolactin Receptor of the Japanese Red-Bellied Newt, Cynops pyrrhogaster

Abstract: BioOne Complete (complete.BioOne.org) is a full-text database of 200 subscribed and open-access titles in the biological, ecological, and environmental sciences published by nonprofit societies, associations, museums, institutions, and presses.

Cited by 23 publications

References 35 publications

Localization of prolactin receptor in the newt brain

Localization of prolactin receptor in the newt brain

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Identification and characterization of newtrad (ras associated with diabetes), a gene specifically expressed in regenerating limb muscle

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