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Calcitonin Receptor-Stimulating Peptide -1, -2 & -3 (CRSP -1, -2 &-3)

Central effects of calcitonin receptor-stimulating peptide-1 on energy homeostasis in rats
The CT-R [calcitonin (CT) receptor] is expressed in the central nervous system and is involved in the regulation of food intake, thermogenesis, and behaviors. CT-R-stimulating peptide-1 (CRSP-1), a potent ligand for the CT-R, was recently isolated from the porcine brain. In this study, we first confirmed that porcine CRSP-1 (pCRSP-1) enhanced the cAMP production in COS-7 cells expressing recombinant rat CT-R, and then we examined the central effects of pCRSP-1 on feeding and energy homeostasis in rats. Intracerebroventricular (icv) administration of pCRSP-1 to free-feeding rats suppressed food intake in a dose-dependent manner. Chronic icv infusion of pCRSP-1 suppressed body weight gain over the infusion period. Furthermore, icv administration of pCRSP-1 increased body temperature and decreased locomotor activity. The central effects of pCRSP-1 were more potent than those of porcine CT in rats. In contrast, ip administration of pCRSP-1 did not elicit any anorectic or catabolic effects. Administration icv of pCRSP-1 also induced mild dyskinesia of the lower extremities and decreased gastric acid output. Fos expression induced by icv administration of pCRSP-1 was detected in the neurons of the paraventricular nucleus, dorsomedial hypothalamic nucleus, arcuate nucleus, locus coeruleus, and nucleus of solitary tract, areas that are known to regulate feeding and energy homeostasis. Administration icv of pCRSP-1 increased plasma concentrations of ACTH and corticosterone, implying that the hypothalamic-pituitary-adrenocortical axis might be involved in catabolic effects of pCRSP-1. These results suggest that CRSP-1 can function as a ligand for the CT-R and may act as a catabolic signaling molecule in the central nervous system.
Sawada H, et al. Endocrinology. 2006 Apr;147(4):2043-50. Epub 2006 Jan 12.
 
Structure and biological properties of three calcitonin receptor-stimulating peptides, novel members of the calcitonin gene-related peptide family
In this review, we describe the structure and biological properties of calcitonin receptor-stimulating peptide-1 (CRSP-1), CRSP-2 and CRSP-3, the novel members of the CGRP family. CRSP-1, which has been identified in the pig, cow, dog, and horse, is a specific ligand for the calcitonin (CT) receptor, and porcine CRSP-1 elicits a 100-fold greater effect on a recombinant porcine CT receptor than porcine CT, although this peptide has high structural similarity with CGRP. CRSP-1 is expressed and synthesized mainly in the central nervous system (CNS), pituitary and thyroid gland. In an in vivo experiment, bolus administration of CRSP-1 into rats reduced the plasma calcium concentration, but did not alter blood pressure, indicating its action as a CT receptor agonist in the peripheral circulation. In the CNS, CRSP-1 is also deduced to be an endogenous agonist for the CT receptor. CRSP-2 has been identified in the pig and dog, and CRSP-3 has been identified only in the pig. They are expressed and synthesized mainly in the CNS and thyroid gland. However, their endogenous molecular forms, receptors, and biological activity remain unidentified.
Katafuchi T, Minamino N. Peptides. 2004 Nov;25(11):2039-45

Identification of second and third calcitonin receptor-stimulating peptides in porcine brain
We identified two cDNAs encoding new calcitonin receptor-stimulating peptides (CRSPs) in porcine hypothalamus cDNA library by cross-hybridization with the CRSP cDNA, and designated the second and third peptides as CRSP-2 and CRSP-3. The putative amino acid sequences of prepro-CRSP-2 and prepro-CRSP-3 showed higher identity with that of prepro-CRSP-1 than that of prepro-calcitonin gene-related peptide (CGRP), respectively, and these three CRSPs are considered to form a new family in the CGRP superfamily. RT-PCR analysis demonstrated that both CRSP-2 and CRSP-3 gene transcripts were expressed mainly in the central nervous system and thyroid gland. Synthetic CRSP-2 and CRSP-3 stimulated cAMP production very weakly in LLC-PK(1) cells compared with CRSP and calcitonin (CT). Furthermore, CRSP-2 and CRSP-3 did not elicit a cAMP elevation at all in the COS-7 cells expressing CT receptor or CT-like receptor with or without one of receptor activity-modifying proteins. These results suggest the presence of still unidentified action mechanisms and functions of the peptides in the CGRP superfamily.
Katafuchi T, Hamano K, Kikumoto K, Minamino N. Biochem Biophys Res Commun. 2003 Aug 29;308(3):445-51.

Calcitonin Receptor-Stimulating Peptide (CRSP), a new member of the calcitonin gene-related peptide family: Its isolation from porcine brain, structure, tissue distribution and biological activity

We isolated a novel biologically active peptide, designated Calcitonin Receptor-Stimulating Peptide (CRSP), from the acid extract of the porcine brain by monitoring cAMP production in the porcine kidney cell line LLC-PK1. Determination of the amino acid sequence and cDNA analysis encoding a CRSP precursor showed that this peptide has approximately 60% identity in the amino acid sequence with human calcitonin gene-related peptide type-a (aCGRP ), type-b (bCGRP ), and porcine CGRP. Northern blot analysis and radioimmunoassay demonstrated that CRSP is expressed mainly in the thyroid gland and the central nervous system, in which the calcitonin receptor was abundantly expressed. Synthetic CRSP elicited a potent stimulatory effect on the cAMP production in LLC-PK1 cells. Although it shows significant sequence similarity with CGRPs, this peptide did not elicit cAMP elevation in cells that were endogenously expressing a CGRP receptor or an adrenomedullin receptor, or were transfected with either of these recombinant receptors. Administration of CRSP into anesthetized rats did not alter the blood pressure, but induced a transient decrease in the plasma calcium concentration. In fact, this peptide potently increased the intracellular cAMP concentration in COS-7 cells that expressed the recombinant calcitonin receptor. These unique properties indicate that CRSP is not a porcine counterpart of bCGRP and probably elicits its biological effects via the calcitonin receptor.
Katafuchi T, et al. J. Biol. Chem., 278,12046-12054 ( 2003)

Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co-expression of calcitonin receptor with receptor activity-modifying proteins
We tested whether heterodimers comprised of calcitonin (CT) receptor lacking the 16-amino acid insert in intracellular domain 1 (CTR(I1-)) and receptor activity-modifying protein (RAMP) can function not only as calcitonin gene-related peptide (CGRP) receptors but also as adrenomedullin (AM) receptors. Whether transfected alone or together with RAMP, human (h)CTR(I1-) appeared mainly at the surface of HEK-293 cells. Expression of CTR(I1-) alone led to significant increases in cAMP in response to hCGRP or hAM, though both peptides remained about 100-fold less potent than hCT. However, the apparent potency of AM, like that of CGRP, approached that of CT when CTR(I1-) was co-expressed with RAMP. CGRP- or AM-evoked cAMP production was strongly inhibited by salmon CT-(8-32), a selective amylin receptor antagonist, but not by hCGRP-(8-37) or hAM-(22-52), antagonists of CGRP and AM receptors, respectively. Moreover, the inhibitory effects of CT-(8-32) were much stronger in cells co-expressing CTR(I1-) and RAMP than in cells expressing CTR(I1-) alone. Co-expression of CTR(I1-) with RAMP thus appears to produce functional CT-(8-32)-sensitive AM receptors.
Kuwasako K, et al. Biochem Biophys Res Commun., 301(2):460-4 (2003)

Identification, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides
We have recently identified in porcine brain a series of new peptides, designated calcitonin receptor-stimulating peptide-1 (CRSP-1), CRSP-2, and CRSP-3, but failed to find their counterparts in humans and rodents by either database searching or experimental cross-hybridization. In this study, we isolated cDNAs encoding precursors of bovine CRSP-1, canine CRSP-1, and canine CRSP-2 from their thyroid cDNA libraries. Although the deduced mature amino acid sequences of bovine and canine CRSP-1s and canine CRSP-2 showed identity with their respective porcine CRSP counterparts, none of them had a C-terminal amide structure. In LLC-PK(1) cells endogenously expressing the calcitonin (CT) receptor, bovine and canine CRSP-1s enhanced the cAMP production, while canine CRSP-2 did not stimulate it at all. Equine CGRP-I had a high identity in its amino acid sequence with porcine CRSP-1 and stimulated LLC-PK(1) cells at a potency comparable to that of porcine CT. None of these CRSPs or equine CGRP-I stimulated the CT-like receptor, even in the presence of receptor activity-modifying proteins. These results demonstrate that CRSP-1, a new class of biologically active peptide, is present in animals evolutionarily close to pigs and induces its activity through the calcitonin receptor, suggesting a wide existence and common properties of this peptide in mammals.
Katafuchi T, Hamano K, Minamino N. Biochem Biophys Res Commun. 2004 Jan 2;313(1):74-9

Antibody for Calcitonin Receptor-Stimulating Peptide-3 (CRSP-3) Immunohistochemistry in rat brain
CRSP-1
Effects of icv administration of pCRSP-1 on food intake. A, Cumulative food intake in
free-feeding rats in the dark phase (n = 12 per group) was measured following icv
administration of saline, pCRSP-1 (0.3, 0.5, 1.0 nmol) or pCT (1.0 nmol). B, Cumulative food intake in 14 h-fasted rats in the light phase (n = 8 per group) was measured following icv administration of saline, pCRSP-1 (0.3, 0.5, 1.0 nmol) or pCT (1.0 nmol) at the light phase. Control rats were given 0.9% saline. *, P < 0.05; **, P < 0.001 (vs. saline controls). a, P < 0.05; b, P < 0.001 (vs. pCT). C, Effect of ip administration of pCRSP-1 (10 nmol) in the dark phase to rats (n = 6 per group). Control rats were given 0.9% saline by ip injection. D, Conditioned taste aversion test. Conditioned rats (n = 10 per group) received icv administration of pCRSP-1 (0.5, 1.0 nmol) or saline and ip administration of LiCl or saline. *, P < 0.05 (vs. ip saline controls). E, Cumulative food intake in free-feeding rats in the dark phase (n = 9 per group) was measured following icv administration of saline or pCRSP-2 (1.0 nmol). F, Cumulative food intake in free-feeding rats in the dark phase (n = 8 per group) was measured following icv administration of saline or pCRSP-3 (1.0 nmol). Sawada H, et al. Endocrinology. 2006 Apr;147(4):2043-50. Epub 2006 Jan 12.
Effects of chronic icv administration of pCRSP-1 on rats. One-day food intake (A) and
cumulative body weight gain (B) were measured during icv injection (2.0 nmol/day) for 7 days (n = 7 per group). Each pair-fed rat was given the same amount of food as the paired pCRSP-1-administered rat consumed on the previous day. Control rats were given 0.9% saline. *, P < 0.05; **, P < 0.001 (vs. saline controls). a, P < 0.05 (vs. pair-fed). Sawada H, et al. Endocrinology. 2006 Apr;147(4):2043-50. Epub 2006 Jan 12.
Effects of icv administration of pCRSP-1 on body temperature and locomotor activity.
A, Body temperature was measured from -30 min to 240 min after administration of pCRSP-1 (0.1, 1.0 nmol) or pCT (0.1 nmol) (n = 6 per group). Control rats were given 0.9% saline. *, P < 0.05; **, P < 0.001 (vs. saline controls). a, P < 0.05 (vs. pCT). B, Body temperature was measured up to 240 min after administration of pCRSP-1 (1.0 nmol), pCRSP-2 (5.0 nmol), or pCRSP-3 (5.0 nmol). Control rats were given 0.9% saline. **, P < 0.001 (vs. saline controls). C, Locomotor activity was measured for 12 h after administration of pCRSP-1 (0.3, 0.5, 1.0 nmol) or pCT (1.0 nmol) (n = 5 per group). Control rats were given 0.9% saline. *, P < 0.05; **, P < 0.001 (vs. saline controls). a, P < 0.05 (vs. pCT). Sawada H, et al. Endocrinology. 2006 Apr;147(4):2043-50. Epub 2006 Jan 12.
Plasma levels of ACTH 15 min after the administration of pCRSP-1 (1.0 nmol) or
saline (n = 5 per group). B, Plasma levels of corticosterone 30 min after the administration of pCRSP-1 (1.0 nmol) or saline (n = 5 per group). *, P < 0.05 (vs. saline controls). Sawada H, et al. Endocrinology. 2006 Apr;147(4):2043-50. Epub 2006 Jan 12.
Fig. 1. Nucleotide and deduced amino acid sequences of bovine (A) and canine (B) CRSP-1, and alignment of deduced mature peptides of bovine and canine CRSP-1 with equine CGRP-I, porcine CRSP-1, and porcine CGRP (C). (A,B) Nucleotide and amino acid numbers are shown on the right. Putative signal peptides are shown in italics. The mature amino acid sequence of each CRSP-1 is boxed. (C) The deduced mature amino acid sequences of bovine (bCRSP-1) and canine CRSP-1 (cCRSP-1) are aligned with those of equine CGRP-I (eCGRP-I), porcine CRSP-1 (pCRSP-1), and porcine CGRP (pCGRP). The amino acids identical to porcine CRSP-1 are shaded.
T. Katafuchi et al. Biochemical and Biophysical Research Communications 313 (2004) 74–79 75
Fig. 2. Nucleotide and deduced amino acid sequences of canine CRSP-2 (A), and alignment of deduced mature peptide of canine CRSP-2 with canine CRSP-1 and CGRP, and porcine CRSP-2, CRSP-3, and CRSP-1 (B). (A) Nucleotide and amino acid numbers are shown on the right. Putative signal peptide is shown in italics. The mature amino acid sequence of canine CRSP-2 is boxed. (B) The deduced amino acid sequences of mature canine CRSP-2 (cCRSP-2) are aligned with those of canine CRSP-1 (cCRSP-1), canine CGRP (cCGRP), porcine CRSP-2 (pCRSP-2), porcine CRSP-3 (pCRSP-3), and porcine CRSP-1 (pCRSP-1). The amino acids identical to canine CRSP-2 are shaded.
Fig. 3. Dose–response elevation of cAMP production in the culture medium of LLC-PK1 cells. LLC-PK1 cells were stimulated with the indicated concentrations of bovine CRSP-1 (closed circle), canine CRSP-1 (closed triangle), equine CGRP-I (open circle), porcine CRSP- 1 (open square), porcine CT (closed square), and canine CRSP-2 (open triangle). Each point represents the meanSEM of three separate determinations.
T. Katafuchi et al. / Biochemical and Biophysical Research Communications 313 (2004) 74–79
 
 
 

Nucleotide sequences and deduced amino acid sequences of CRSP-2 (A) and CRSP-3 (B) cDNA, and alignments of amino-acid sequences of porcine prepro-CRSPs and prepro-CGRP (C). (A, B) Nucleotide and amino acid numbers are shown on the right. Putative mature amino acid sequences of CRSP-2 and CRSP-3 are boxed. The donor glycine of the C-terminal amide is shaded and the termination codon is marked with an asterisk. The signal sequences are shown in italics. (C) The amino acid sequences of prepro-CRSP-2 and CRSP-3 are compared with those of prepro-CRSP-1 and prepro-CGRP. The deduced amino acid sequences for mature peptides are shown by upper cases and prepro peptides are indicated by lower cases. The putative prohormone convertase cleavage sites are boxed. The residues that are in common with and distinct from CRSP-2 are shown by bold and gray characters, respectively.
Katafuchi T, Hamano K, Kikumoto K, Minamino N. Biochem Biophys Res Commun. 2003 Aug 29;308(3):445-51

Measurement of mRNA levels of CRSP-1, CRSP-2, CRSP-3, CGRP, CT, and GAPDH by RT-PCR. RT-PCR analyses were performed as described in "Materials and methods" with total RNA from each of the 19 organs listed at the top. The PCR products of CRSP-1 (306 bp), CRSP-2 (305 bp), CRSP-3 (329 bp), CGRP (640 bp), CT (570 bp), and GAPDH (378 bp) were resolved by electrophoresis in agarose gels, stained with ethidium bromide, and visualized using an FLA-2000 fluorescent image analyzer. The bottom panel shows the RT-PCR amplification of GAPDH mRNA as proof of the integrity of each RNA preparation.
Katafuchi T, Hamano K, Kikumoto K, Minamino N. Biochem Biophys Res Commun. 2003 Aug 29;308(3):445-51

Effects of CRSPs and its related peptides on the cAMP production in the LLC-PK1 cells. LLC-PK1 cells were stimulated with the indicated concentrations (0, 10-11–r10-6 M) of porcine CRSP-1 (closed square), CRSP-2 (open circle), CRSP-3 (closed circle), CT (open square), CGRP (open triangle), and human AM (closed triangle). LLC-PK1 cells were harvested on a 48-well plate, cultured for 24 h, and then used for the measurement of cAMP production. Each point represents the means r SEM of three separate determinations.
Katafuchi T, Hamano K, Kikumoto K, Minamino N. Biochem Biophys Res Commun. 2003 Aug 29;308(3):445-51

Effects of CRSPs and its related peptides on CT receptor or CL receptor in the absence or presence of RAMPs. CT receptor (CTR) or CL receptor (CLR) cDNA inserted into pcDNA was transfected into COS-7 cells with one of RAMP1, RAMP2, and RAMP3 cDNA inserted into pcDNA or insert-free pcDNA, which is indicated at the top-right of each figure, using Lipofectamine Plus reagent. The cells were then cultured for 24 h and used for the experiments. The cells were stimulated with 10-7 M of the indicated peptides. Each point represents the means r SEM of three separate determinations.
Katafuchi T, Hamano K, Kikumoto K, Minamino N. Biochem Biophys Res Commun. 2003 Aug 29;308(3):445-51




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