Identification of second and third calcitonin receptor-stimulating peptides in porcine brain

Katafuchi, Tetsuro; Hamano, Kazumasa; Kikumoto, Katsuro; Minamino, Naoto

doi:10.1016/s0006-291x(03)01413-x

Cited by 26 publications

(10 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Calcitonin (CT) is a 32-amino acid peptide belonging to a small family of peptides also including a-CT gene-related peptide (a-CGRP), b-CGRP, amylin, adrenomedullin, intermedin and CT receptor-stimulating peptide (Wimalawansa 1997, Katafuchi et al 2000, 2004. CT was discovered as an acute hypocalcaemic hormone released from the parathyroid glands (Copp & Cheney 1962), but shortly thereafter shown to be secreted by thyroid C-cells (Foster et al 1964, Zaidi et al 2002.…”

Section: Introductionmentioning

confidence: 99%

Calcitonin inhibits osteoclast formation in mouse haematopoetic cells independently of transcriptional regulation by receptor activator of NF-κB and c-Fms

Granholm

Lundberg²,

Lerner

2007

Journal of Endocrinology

View full text Add to dashboard Cite

The effects of calcitonin (CT) on osteoclast formation and gene expression have been studied in cultured mouse spleen cells and mouse bone marrow macrophages (BMMs). CT inhibited the formation of multinucleated osteoclasts and resorption pits in spleen cell cultures and BMM as well as in CD115 C CD3 K CD45RK sorted BMM cultures, incubated in the presence of macrophage colony-stimulating factor and receptor activator of NF-kB ligand (RANKL). No effect on apoptosis by CT was observed. CT did not affect the mRNA expressions of RANK and c-Fms, or the mRNA expressions of a wide variety of transcription factors and genes important for osteoclast differentiation and activity. CT induced inhibition of tartrateresistant acid phosphatase (TRAP), positive multinucleated osteoclast formation was not associated with any decrease of total TRAP activity, resulting in a large number of TRAP C mononucleated cells in CT-treated cultures. CT did not affect the mRNA expression of dendritic cell-specific transmembrane protein, d2 isoform of vacuolar (H C ) ATPase v o domain, a disintegrin and metalloproteinase domain 8 (ADAM8), ADAM12, DNAX-activating protein or Fc receptor common g chain suggested to be involved in fusion of mononucleated osteoclast progenitor cells. The inhibitory effect by CT was mimicked not only by compounds activating cAMP and protein kinase A (PKA) but also by a cAMP analogue activating the exchange protein directly activated by cAMP (Epac) pathway. It is concluded that CT, through cAMP/PKA/Epac cascades, inhibits osteoclast formation and that this effect is not associated with decreased transcription of genes known to be important for osteoclast progenitor cell differentiation, fusion or function.

show abstract

Section: Introductionmentioning

confidence: 99%

Calcitonin inhibits osteoclast formation in mouse haematopoetic cells independently of transcriptional regulation by receptor activator of NF-κB and c-Fms

Granholm

Lundberg²,

Lerner

2007

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Thus, CRSP1 is suggested to be an endogenous ligand for the central CT receptor. CRSP2 and CRSP3 were identified by screening a swine hypothalamus cDNA library using CRSP1 cDNA as a probe (Katafuchi et al, 2003b). Despite their high amino acid sequence similarity with CRSP1 and CGRP, CRSP2 and CRSP3 only faintly, if at all, stimulate recombinant CT, CGRP or AM receptor.…”

mentioning

confidence: 99%

“…Despite their high amino acid sequence similarity with CRSP1 and CGRP, CRSP2 and CRSP3 only faintly, if at all, stimulate recombinant CT, CGRP or AM receptor. RT-PCR analysis has revealed that mRNAs of CRSP2 and CRSP3 are expressed mainly in the central nervous system and thyroid, and that the expression profiles are principally similar to those of porcine CRSP1 and CGRP (Katafuchi et al, 2003b).…”

mentioning

confidence: 99%

Genomic organization, expression and evolution of porcine <i>CRSP1, 2, </i>and<i>3</i>

Rezaeian

Katafuchi

Yoshizawa

et al. 2008

Cytogenet Genome Res

View full text Add to dashboard Cite

Recently we identified and characterized porcine calcitonin receptor-stimulating peptide (CRSP) 1, CRSP2 and CRSP3 as members of the calcitonin/calcitonin gene-related peptide (CT/CGRP) family. In the present study, the genomic sequences and organization of CRSP1, 2, and 3 were determined, and the expression of the genes in the porcine brain was investigated using in situ hybridization. Analysis of 5′-upstream regions of the three CRSPs demonstrated that CRSP1 and CRSP2 have almost identical sequences (>98% similarity) and high sequence similarities including functional transcription binding sites with the corresponding region of human CALCA (CT/αCGRP), whereas CRSP3 retains less similarity with the above genes. RH mapping of CRSPs demonstrated that they resided in a region of swine chromosome 2 (SSC2). The arrangement of the genes in the region was found to be conserved in corresponding human and mouse regions. In situ hybridization demonstrated sense transcripts of the three genes in cerebrum, hippocampus, hypothalamus, pons/midbrain, and thalamus of 3-month-old pigs, and CRSP2 sense transcripts additionally in tractus opticus. The sense transcripts of αCGRP and CALCB (βCGRP) were detected in cerebrum, hippocampus, and pons/midbrain of newborn mice, and to a lesser extent in pons/midbrain of 8-week-old mice. These results taken together with the chromosomal conservation and phylogenetic clustering of CT/CGRP family indicate that CRSP1, 2, and 3 may be functionally different from αCGRP and βCGRP, though they are indicated to have a common progenitor gene.

show abstract

“…Unlike precursors for porcine and canine CRSP-2 peptides that have no typical prohormone convertase processing site on either end of the deduced mature peptides, the precursor of caprine CRSP-2 has a typical prohormone convertase processing site between the N-terminal flanking peptide and the deduced mature CRSP-2. Nevertheless, the synthetic CRSP-2 peptides used for this and previous studies might not be endogenous forms of CRSP-2 peptides (Katafuchi et al 2003b). Purification and structural determination of native CRSP-2 peptides is a prerequisite for evaluating the function and biological activity of CRSP-2 peptides.…”

Section: Discussionmentioning

confidence: 99%

“…We have since identified two additional closely related peptides CRSP-2 and CRSP-3 also from porcine brain (Katafuchi et al 2003b) and have also identified homologous peptides from cattle, dogs, and horse (Katafuchi et al 2004). Each of these peptides shows sequence homology to CT and CT gene-related peptide (CGRP) and thus they make up a part of the CGRP family.…”

Section: Introductionmentioning

confidence: 99%

Identification and biological activity of ovine and caprine calcitonin receptor-stimulating peptides 1 and 2

Charles

Katafuchi²,

Yandle

et al. 2008

Journal of Endocrinology

Self Cite

View full text Add to dashboard Cite

We have recently reported the isolation of three new members of the calcitonin (CT) gene-related peptide family of peptides, the CT receptor (CT-R)-stimulating peptides (CRSPs). We now report the sequencing and characterization of ovine/caprine CRSP-1 and caprine CRSP-2. Mature ovine and caprine CRSP-1 are identical and have strong structural homology to CRSP-1s identified to date from other species. As with other CRSP-1s, ovine/caprine CRSP-1 binds to and activates the CT-R but not the CT-like receptor (CL-R) in combination with the receptor activity-modifying proteins (RAMPs). By contrast, caprine CRSP-2 does not activate any of these receptor-RAMP complexes. Intravenous infusions of ovine CRSP-1 to normal conscious sheep induced dose-dependent reduction in plasma total Ca levels (PZ0 . 02) and corrected Ca levels (PZ0 . 017) associated with increases in plasma cAMP (PZ0 . 002). CRSP-1 reduced both plasma amino-terminal pro-C-type natriuretic peptide levels (PZ0 . 006) and plasma renin activity (PZ0 . 028). There were no significant effects observed on hemodynamic or renal indices measured. In conclusion, we have sequenced ovine/caprine CRSP-1 and caprine CRSP-2 precursors. This newly identified CRSP-1 has been shown to share the structural and biological features of CRSP-1s known to date. In vivo studies confirm that ovine CRSP-1 reduces plasma Ca levels in sheep, presumably via a cAMP-mediated mechanism. By contrast, caprine CRSP-2 did not stimulate any combination of CT-R, CL-R, and RAMPs. Accession numbers of cDNA determined in this study are caprine CRSP-1, AB364646; caprine CRSP-2, AB364647; and ovine CRSP-1, AB364648.

show abstract

Identification of second and third calcitonin receptor-stimulating peptides in porcine brain

Cited by 26 publications

References 28 publications

Calcitonin inhibits osteoclast formation in mouse haematopoetic cells independently of transcriptional regulation by receptor activator of NF-κB and c-Fms

Calcitonin inhibits osteoclast formation in mouse haematopoetic cells independently of transcriptional regulation by receptor activator of NF-κB and c-Fms

Genomic organization, expression and evolution of porcine <i>CRSP1, 2, </i>and<i>3</i>

Identification and biological activity of ovine and caprine calcitonin receptor-stimulating peptides 1 and 2

Contact Info

Product

Resources

About