Tissue distribution and nucleotide sequence of bovine mRNA for salivary proline-rich protein P-B

Isemura, Satoko; Watanabe, Sachiyo; Fujiwara, Shigeki; Sanada, Kazuo

doi:10.1016/j.archoralbio.2004.06.001

Cited by 4 publications

(7 citation statements)

References 15 publications

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“…12 We recently reported its presence in rat corpus cavernosum tissue. Therefore, we determined if hSMR3A is similarly present in human corporeal tissue.…”

Section: Detection Of Smr3a In Human Corporamentioning

confidence: 96%

hSMR3A as a Marker for Patients With Erectile Dysfunction

et al. 2007

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Purpose-We recently reported that Vcsa1 is one of the most down-regulated genes in the corpora of rats in 3 distinct models of erectile dysfunction. Since gene transfer of plasmids expressing Vcsa1 or intracorporeal injection of its mature peptide product sialorphin into the corpora of aging rats was shown to restore erectile function, we proposed that the Vcsa1 gene has a direct role in erectile function. To determine if similar changes in gene expression occur in the corpora of human subjects with erectile dysfunction we identified a human homologue of Vcsa1 (hSMR3A) and determined the level of expression of hSMR3A in patients.Materials and Methods-hSMR3A was identified as a homologue of Vcsa1 by searching protein databases for proteins with similarity. hSMR3A cDNA was generated and subcloned into the plasmid pVAX to generate pVAX-hSMR3A. pVAX-hSMR3A (25 or 100 μg) was intracorporeally injected into aging rats. The effect on erectile physiology was compared histologically and by measuring intracorporeal pressure/blood pressure with controls treated with the empty plasmid pVAX. Total RNA was extracted from human corporeal tissue obtained from patients undergoing previously scheduled penile surgery. Patients were grouped according to normal erectile function (3), erectile dysfunction and diabetes (5) and patients without diabetes but with erectile dysfunction (5). Quantitative reverse-transcriptase polymerase chain reaction was used to determine the hSMR3A expression level.Results-Intracorporeal injection of 25 μg pVAX-hSMR3A was able to significantly increase the intracorporeal pressure-to-blood pressure ratio in aging rats compared to age matched controls. Higher amounts (100 μg) of gene transfer of the plasmid caused less of an improvement in the intracorporeal pressure-to-blood pressure ratio compared to controls, although there was histological and visual evidence that the animals were post-priapitic. These physiological effects were similar to previously reported effects of intracorporeal injection of pVAX-Vcsa1 into the corpora of aging rats, establishing hSMR3A as a functional homologue of Vcsa1. More than 10-fold down-regulation in hSMR3A transcript expression was observed in the corpora of patients with vs without erectile dysfunction. In patients with diabetes associated and nondiabetes associated erectile dysfunction hSMR3A expression was found to be down-regulated.Conclusions-These results suggest that hSMR3A can act as a marker for erectile dysfunction associated with diabetic and nondiabetic etiologies. Given that our previous studies demonstrated that gene transfer of the Vcsa1 gene and intracorporeal injection of its protein product in rats can restore erectile function, these results suggest that therapies that increase the hSMR3A gene and product expression could potentially have a positive impact on erectile function. Penile erection is a neurovascular process that relies on a concerted action of the nervous system, the vascular system and cavernous smooth muscle tissues. ED is attrib...

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“…12 We recently reported its presence in rat corpus cavernosum tissue. Therefore, we determined if hSMR3A is similarly present in human corporeal tissue.…”

Section: Detection Of Smr3a In Human Corporamentioning

confidence: 96%

hSMR3A as a Marker for Patients With Erectile Dysfunction

et al. 2007

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“…1). The sequence of the polynucleotide of 356 bp cloned previously (AB192573) was reported to be identical with the corresponding part of human P-B cDNA (7). When the sets PB1+/PB2− and PB1+/PB3− were used as primers, a band of 662 bp was occasionally detected in addition to the expected 124 bp and 167 bp bands (Fig.…”

Section: Methodsmentioning

confidence: 98%

“…In 1990, Strawich and Glimcher (16) demonstrated the presence of a protein corresponding to human salivary P-B in bovine tooth germ. We demonstrated that bovine tooth germ is the site where P-B is produced by PCR cloning of P-B cDNA from bovine tooth germ cDNA and that the coding region for the mature protein and the subsequent 185 bp of bovine P-B tooth germ cDNA are identical to the corresponding region in human P-B cDNA (7,9). During the course of cloning, we have obtained a PCR product of 662 bp in which the nucleotide sequence of 5' 1-393 bp is essentially identical to that of human P-B cDNA, whereas the following 269 bp sequence has no homology at all.…”

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confidence: 99%

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Evidence for inclusion of a segment of Escherichia coli genomic DNA in bovine tooth germ mRNA encoding salivary proline-rich protein P-B

et al. 2005

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In the course of cloning of bovine cDNA for proline-rich protein (PRP) P-B from bovine tooth germ cDNA, we found that one clone with 662 bp contained a 5'-terminal 393 bp (1-393 bp) sequence essentially identical to that of human P-B cDNA (154-546 in D29833) and bovine P-B cDNA (1-356 bp in AB192573) and a sequence of 233 bp (394-626 bp) highly homologous to the segment of E. coli K12 genomic DNA (365511-365744 in NC000913). Although the latter sequence is contained in the vector pT7Blue, which we used, our results show that this chimeric structure in bovine tooth germ P-B cDNA is not an artifact formed during the cloning process, but intrinsic to the bovine genome since the chimeric structure was detected in bovine tooth germ and bovine genomic DNA.

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“…It is a 57-amino acid peptide containing 30 proline and 9 glycine residues, pQRGPRGPYPPG-PLAPPQPFGPGFVPPPPPPPYGPGRIPPPPPAPYGPGIFPPPPPQP. The P-B is a mature peptide by itself [12][13][14][15], but its biological role remains still unclear [16,17]. Previous circular dichroism (CD) studies of P-B, based on the coincidence of the positions of trough and peak in the CD spectrum of the aqueous solution of poly-L-proline with that of P-B, indicated that the consecutive prolyl residues in the peptide adopt a poly-L-proline form II structure [18].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and conformational analysis of salivary proline‐rich peptide P‐B

Kamysz

Sikorska

2010

Journal of Peptide Science

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The 57-amino acid human salivary polypeptide P-B has been synthesized by the solid-phase method using 9-fluorenylmethoxycarbonyl (Fmoc) strategy. The circular dichroism (CD) spectroscopy, Fourier-transform infrared spectroscopy (FTIR) and molecular modeling methods have been used for conformational studies of P-B. Examination of the CD spectra of P-B showed the content of the secondary structure to be independent of temperature over the range 0-60 °C at pH = 7 as well as over the pH range of 2-12 at 37 °C. P-B adopts predominantly unordered structure with locally appearing β-turns. The cumulative results obtained using the CD and FTIR spectroscopic techniques indicate the percentage of the polyproline type-II (PPII) helix being as low as about 10%. Similarly, the molecular dynamics (MD) simulations reveal only a short PPII helix in the C-terminal fragment of the peptide (Pro(51)-Pro(54)), which constitutes 7%.

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Tissue distribution and nucleotide sequence of bovine mRNA for salivary proline-rich protein P-B

Cited by 4 publications

References 15 publications

hSMR3A as a Marker for Patients With Erectile Dysfunction

hSMR3A as a Marker for Patients With Erectile Dysfunction

Evidence for inclusion of a segment of Escherichia coli genomic DNA in bovine tooth germ mRNA encoding salivary proline-rich protein P-B

Synthesis and conformational analysis of salivary proline‐rich peptide P‐B

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