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PubMed2003

Isolation and characterization of gelatin-binding bison seminal vesicle secretory proteins.

Bovine seminal plasma (BSP) contains a family of major proteins designated BSP-A1/A2, BSP-A3, and BSP-30kDa (collectively called BSP proteins) that bind to sperm at ejaculation and potentiate sperm capacitation. Homologous proteins have been identified in stallion, boar, goat, and ram seminal plasma. We report here the isolation and characterization of homologous proteins from bison seminal vesicle secretions. Seminal vesicle secretory proteins were precipitated by adding cold ethanol and recovered by centrifugation. The precipitates were resuspended in ammonium bicarbonate, dialyzed, and lyophilized. Lyophilized proteins were dissolved in 0.05 M phosphate buffer (PB) and loaded onto a gelatin-agarose column. The unadsorbed proteins and adsorbed proteins were eluted with PB and 5 M urea in PB, respectively. The gelatin-adsorbed fraction was analyzed by SDS-PAGE and revealed the presence of four major proteins designated BiSV-16kDa, BiSV-17kDa, BiSV-18kDa, and BiSV-28kDa (BiSV: bison seminal vesicle proteins). Heparin-Sepharose chromatography allowed the separation of BiSV-16kDa, which did not bind heparin from other BiSV proteins, which bound heparin. Immunoblotting revealed that BiSV-16kDa cross-reacted with BSP-A3 antibodies, BiSV-17kDa and BiSV-18kDa cross-reacted with BSP-A1/-A2 antibodies, and BiSV-28kDa cross-reacted with BSP-30kDa antibodies. Radioimmunoassays indicated that approximately 25% of bison seminal vesicle total proteins are related to BSP proteins. The amino-terminal sequencing indicated that BiSV proteins share almost 100% sequence identity with BSP proteins. In addition, BiSV proteins bind to low-density lipoproteins isolated from hen's egg yolk. These results confirm that BSP protein homologs are present in mammalian seminal plasma and they may share the same biological role.

Amino Acid Sequence↗

PubMed1995

Structure and sequence of a mouse gene encoding an androgen-regulated protein: a new member of the seminal vesicle secretory protein family.

The gene encoding MSVSP99 (mouse seminal vesicle secretory protein of 99 amino acids), an androgen-dependent protein specifically expressed in the mouse seminal vesicle, was isolated and sequenced. A mouse genomic library constructed in the lambda EMBL12 vector was screened using a full length cDNA probe. One genomic clone was selected, 7.4 kb of which were shown to contain the whole MSVSP99 gene. The complete sequence of the MSVSP99 gene (1.7 kb), plus 0.8 and 0.3 kb of the 5' and 3' flanking regions respectively, has been determined. The gene is composed of four exons interrupted by three introns. The size range for the four exons is 47-217 bp, while that of introns is 87-615 bp. The transcription start site was identified as an adenine residue located 21 nucleotides upstream from the ATG start codon. Putative TATA and CAAT boxes were identified, along with a number of regions that shared homologies with known regulatory sequences. These included androgen-responsive elements located in the promoter as well as in the gene sequence. Sequence comparisons with other androgen-responsive genes showed strong homologies between the MSVSP99 gene and the seminal vesicle secretory protein (SVS) family genes (rat SVS II, IV, V and VI). Moreover, some regions were found to be conserved between the MSVSP99 gene and the human semenogelin I and II genes.

Amino Acid Sequence↗

PubMed1987

The androgen-dependent mouse seminal vesicle secretory protein IV: characterization and complementary deoxyribonucleic acid cloning.

Seminal vesicle secretory protein IV of a mouse has been isolated, and the cDNA coding for its mRNA has been cloned and sequenced. The 556-nucleotides encode 16 amino acid signal peptides and 92 residues of mature protein. Considerable homology between mouse and rat SVS IV cDNA was found. In the leader peptide and 3'-noncoding region there is 92% and 85% homology, respectively. The other regional homologies are 86% for the first 12, 68.5% for the last 35, and 40% for the middle 44 amino acids. The expression of mouse SVS IV mRNA is under the control of androgen. Administration of testosterone to castrated mice resulted in induction of the mRNA level to 50% of the mature male in 96 h of hormone treatment. Secretion of the protein after testosterone injection follows a similar pattern.

Amino Acid Sequence↗

PubMed1983

Characterization of a genomic clone for rat seminal vesicle secretory protein IV.

The entire coding region for rat seminal vesicle secretory protein IV was obtained on a 3.5 kb Eco RI fragment isolated from a genomic library in lambda Charon 4A. The coding sequence for SVS IV message is interrupted twice by introns. The first lies just downstream from the juncture of the 21 amino acid secretory signal peptide with the start of the mature protein, and the second lies in the 3'-nontranslated region. The major transcriptional start site was mapped by primer extention and is 22 nucleotides upstream from the translational initiation codon. S1 protection experiments indicated additional minor transcriptional starts about 27 and 50 nucleotides further upstream from the major cap site. The entire transcriptional unit comprises about 1740 nucleotides. The SVS IV gene does not belong to an obvious gene family, and it is conserved in mice and guinea pigs.

Amino Acid Sequence↗

PubMed1988

Processing of two protein precursors yields four mature guinea pig seminal vesicle secretory proteins.

The translation of the two most abundant guinea pig seminal vesicle epithelium mRNAs (1800 nucleotides and 950 nucleotides) and the subsequent processing of their protein products were studied in an effort to elucidate the mechanism by which the four mature guinea pig seminal vesicle epithelium (GPSVE) secretory proteins are produced. The primary translation products of the 1800 nt and 950 nt mRNAs are two secretory protein precursors of 45 kDa and 20 kDa, respectively. Removal of signal peptides from these two precursors produces proteins of 43 kDa and 18.5 kDa, which are recognized by polyclonal antisera directed against the four mature secretory proteins. The existence of further processing intermediates in the production of the secretory proteins is suggested by the appearance of other immunoreactive polypeptides following incubation of GPSVE in nutrient medium containing [3H] leucine. Immunological and pulse-chase analysis strongly suggests that the 43-kDa protein gives rise to SVP-1, -3, and -4 and that SVP-2 is derived from the 18.5-kDa protein.

Animals↗

PubMedDate not supplied

Mouse seminal vesicle secretory protein of 99 amino acids (MSVSP99): characterization and hormonal and developmental regulation.

Polyclonal antibodies have been generated to investigate the localization, tissue and species distribution, androgen regulation, and ontogeny of a protein secreted by mouse seminal vesicle, designated as MSVSP99 (ie, mouse seminal vesicle secretory protein of 99 amino acids). MSVSP99 is a polymorphic compound with a molecular weight of around 14 kilodaltons and a positive immunoreactivity range of 5.23 to 5.70. Positive immunoreactivity was restricted to the epithelial cells of the seminal vesicle. Western blot analysis showed organ specificity for MSVSP99, which could not be detected in several organs in the mouse. Time course decrease of MSVSP99 after castration closely followed that of its mRNA. In contrast, the length of time required to restore control levels after testosterone treatment was higher for the protein than it was for its mRNA. Whereas the MSVSP99 gene is already active in 10-day-old males, MSVSP99 is first detected at 27 days. Then, we conclude that factors other than the accumulation of the mRNA regulate MSVSP99 expression.

Amino Acid Sequence↗

PubMed1985

Methylation of the rat seminal vesicle secretory protein IV gene. Extensive demethylation occurs in several male sex accessory glands.

Seminal vesicle secretory protein IV (SVS IV) is perhaps the most abundant protein made by the epithelial cells of the rat seminal vesicle. In this report, we have asked whether the methylation of its gene correlates with its tissue-specific pattern of expression. Using methylation-sensitive restriction endonucleases HpaII and AvaI, we could examine seven potential methylation sites in or near the gene. All seven sites were largely unmethylated in the seminal vesicle, while in most nonexpressing organs, all sites were heavily modified. The correlation of demethylation with expression was broken by finding that both ventral prostate and coagulating gland (anterior prostate) DNA showed the same demethylation pattern seen for the seminal vesicle. SVS IV protein has not been reported in either of these two organs, and we could not detect mature SVS IV message in prostate RNA or SVS IV transcription by in vitro incubation of prostate nuclei. We conclude that demethylation of the SVS IV gene accompanies the differentiation of several androgen-dependent sex accessory glands but confirm that demethylation per se is not a sufficient signal to bring about gene transcription.

Animals↗

PubMed1997

The androgen-dependent mouse seminal vesicle secretory protein of 99 amino acids (MSVSP99): regulation of the mRNA and preliminary characterization of the promoter.

MSVSP99 (mouse seminal vesicle secretory protein of 99 amino acids) is a member of the rat and mouse seminal vesicle secretory protein (SVS) family. In order to characterize its androgenic regulation, the cloned cDNA and gene encoding MSVSP99 have been used. At adulthood, the MSVSP99 mRNA represents from 3 to 7% of the total mRNA population. This mRNA accumulation is under androgenic control because it is abolished by castration and restored in castrated mice by heptylate testosterone injection. During ontogenesis, MSVSP99 mRNA is just detectable in 10-day-old mice, and reaches adult levels at 30 days. Neonatal castration abolishes MSVSP99 mRNA accumulation in 20-day-old mice. Transcription elongation assays show that androgens act mainly on the MSVSP99 gene transcription. In an attempt to obtain information about the mechanism of androgen action on transcription, preliminary transient transfection experiments in CV-1 cells permitted us to define a promoter region (-387/ + 16), the activity of which is enhanced by dihydrotestosterone.

Androgens↗

PubMed1999

Identification of low density lipoprotein receptor-related protein-2/megalin as an endocytic receptor for seminal vesicle secretory protein II.

The low density lipoprotein receptor-related protein-2/megalin (LRP-2) is an endocytic receptor that is expressed on the apical surfaces of epithelial cells lining specific regions of the male and female reproductive tracts. In the present study, immunohistochemical staining revealed that LRP-2 is also expressed by epithelial cells lining the ductal region and the ampulla of the rat seminal vesicle. To identify LRP-2 ligands in the seminal vesicle, we probed seminal vesicle fluid with 125I-labeled LRP-2 in a gel-blot overlay assay. A 100-kDa protein (under non-reducing conditions) was found to bind the radiolabeled receptor. The protein was isolated and subjected to protease digestion, and the proteolytic fragments were subjected to mass spectroscopic sequence analysis. As a result, the 100-kDa protein was identified as the seminal vesicle secretory protein II (SVS-II), a major constituent of the seminal coagulum. Using purified preparations of SVS-II and LRP-2, solid-phase binding assays were used to show that the SVS-II bound to the receptor with high affinity (Kd = 5.6 nM). The binding of SVS-II to LRP-2 was inhibited using a known antagonist of LRP-2 function, the 39-kDa receptor-associated protein RAP. Using a series of recombinant subfragments of SVS-II, the LRP-2 binding site was mapped to a stretch of repeated 13-residue modules located in the central portion of the SVS-II polypeptide. To evaluate the ability of LRP-2 to mediate 125I-SVS-II endocytosis and lysosomal degradation, ligand clearance assays were performed using differentiated mouse F9 cells, which express high levels of LRP-2. Radiolabeled SVS-II was internalized and degraded by the cells, and both processes were inhibited by antibodies to LRP-2 or by RAP. The results indicate that LRP-2 binds SVS-II and can mediate its endocytosis leading to lysosomal degradation.

Amino Acid Sequence↗

PubMedDate not supplied

Rat seminal-vesicle secretory protein SVS II binds DNA with a preference for the 5' regulatory region of secretory protein SVS IV gene: co-isolation with components of the nuclear matrix.

In rats, the ventral prostate and seminal vesicles produce distinct sets of proteins whose functions and tissue-specific regulation by androgens remain unclear. We have utilized the genes encoding the major secretory protein of seminal vesicles, SVS IV, and the C3 subunit of prostatein of the ventral prostate to study how the nuclear matrix might determine their tissue-specific gene expression. Nuclear matrix proteins were prepared from purified nuclei with DNase and 2 M NaCl, separated in SDS gels, and transferred onto membranes for DNA-binding (southwestern) and immunological (western) analyses. The 5' region of the SVS IV gene (SVS IV-7S) bound to a 45,000-kDa molecular-weight protein band in the nuclear matrix of seminal vesicles but not to that of ventral prostate, kidney, or liver. Sequencing revealed that this band was a seminal-vesicle secretory protein, SVS II, whose identity was confirmed with an anti-SVS II antiserum in western blots. Actin-like protein, similar in mobility to SVS II, was detected in seminal-vesicle and ventral prostate nuclear matrix, but not in seminal-vesicle fluid. Reducing agent (10 mM dithiothreitol) and acidic (pH 6.5) buffer did not eliminate SVS II, but isolation of nuclear matrices with ammonium sulfate, nucleases, and urea decreased SVS II immunoreactivity and removed actin-like protein. SVS II binding to SVS IV-7S DNA was greater than its binding to either a comparable fragment of the C3 gene or linearized pUC-19 plasmid, and it was not eliminated by a 100-fold competition. When seminal-vesicle fluid was mixed with rat liver, some SVS II co-isolated with the nuclear-matrix proteins, indicating that nonspecific interactions contribute to its association with the nucleoskeleton. However, these interactions may not represent the intracellular behavior of SVS II in seminal-vesicle epithelium. Sequence comparisons indicate significant homologies between SVS II and some other seminal proteins, including bovine caltrin, which, under the name seminalplasmin, is known to possess antimicrobial activity. Collectively, these data suggest that in addition to its known functions, SVS II may also bind extraneous DNA in seminal fluid. Additionally, SVS II may participate as a structural component in the organization of a tissue-specific seminal-vesicle nuclear matrix.

Animals↗

PubMed1993

Cloning and sequence analysis of a cDNA encoding an androgen-dependent mouse seminal vesicle secretory protein.

We report the cloning and sequencing of a new cDNA sequence encoding a protein from the mouse seminal vesicle. An open reading frame of 297 nucleotides encoded a protein of 99 amino acids with a calculated molecular mass of 11.454 kDa. The first 21 amino acids constituted a signal peptide followed by 78 amino acids encoding the secreted protein. The cDNA sequence comprised a 3' untranslated region of 226 bp and the polyadenylation signal AATAAA, 19 bp upstream from the poly(A)+ tail. A high degree of homology was found between this protein and members of the family of seminal vesicle secretory (SVS) proteins, especially rat SVS VI. Northern blot analysis indicated the presence of a 0.7 kb mRNA species in the mRNAs of seminal vesicle tissue. Castration resulted in a marked decrease in the level of the 0.7 kb mRNA encoding the protein, whereas administration of testosterone to castrated males restored the 0.7 kb mRNA.

Amino Acid Sequence↗

PubMed1991

Characterization of the gene for the bovine seminal vesicle secretory protein SVSP109.

As part of an attempt to understand androgen-regulation of SVSP109, a bovine seminal vesicle secretory protein of 109 amino acids, we have characterized the bovine SVSP109 gene. The 6.1 kb gene is organized in five exons and four introns. Regulatory sequences involved in regulation of transcription could not be identified by simple sequence homologies. The SVSP109 gene may provide an excellent example for functional properties of exons: exon 1 encodes the entire signal peptide and exon 4 the complete fibronectin type II-domain, responsible for protein-protein interactions.

Amino Acid Sequence↗

PubMed1982

Effect of castration on the synthesis of seminal vesicle secretory protein IV in the rat.

The effects of castration on the synthesis (accumulation) of a major seminal vesicle secretory protein (SVS IV) were examined in young adult rats. In vitro incorporation of labeled amino acids into SVS IV by minced tissue was monitored by immunological methods. Castration resulted in a large decrease in the differential synthesis of SVS IV. A significant decrease in the relative incorporation of isotope into SVS IV was evident within 3 days of castration, and by 4 weeks relative incorporation dropped some 30-fold. These changes took place in the presence of a large generalized decline in protein synthesis so that incorporation into SVS IV on an organ basis decreased by over 200-fold. SVS IV messenger RNA levels were estimated by RNA excess solution hybridization using a cloned cDNA probe. Relative message levels declined after castration in harmony with the declines in SVS IV synthesis. SVS IV mRNA was decreased by a relative factor of approximately 20 and an absolute factor of approximately 200 in long-term (40-day) castrates. Accordingly, the seminal vesicle conforms to the general pattern of steroid regulated systems in which hormone withdrawal leads to differential decreases in the steady-state pool size for specific mRNAs. The seminal vesicle is unusual, however, in that a prolonged period is required for maximum differential effects to occur.

Animals↗

PubMed1987

Comparison of seminal vesicle secretory proteins of rodents using antibody and nucleotide probes.

The copulatory vaginal plug is a conspicuous feature of rodent reproduction. The five major seminal vesicle secretory proteins of Rattus norvegicus (proteins I-V), which form the copulatory plug, constitute a closely related androgen-regulated family that appears to share a common evolutionary origin. The relationships between these rat proteins and the major seminal vesicle proteins of other rodents were explored using antibodies specific for the individual rat proteins. Immunoblotting of proteins separated by SDS-PAGE showed that the vesicular proteins of R. rattus are identical to those of R. norvegicus except for an additional protein related to protein III. No differences were seen in inbred and outbred strains of R. norvegicus. Of the major proteins of Mus musculus, one showed strong homology with rat protein II and three others were weakly homologous to proteins I, IV (or S) and V (or F); none showed homology to rat protein III. The only homology between the vesicular proteins of Mesocricetus auratus (Syrian hamster) and Meriones ungulatus (Mongolian gerbil) was with rat protein II while those of Cavia porcellus (guinea pig) showed no homology at all with the rat proteins. In addition, cDNA probes for rat genes IV and V both detected weak homologues in seminal vesicle RNA from mice but not guinea pigs.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed2006

Cytokeratin-20 and seminal vesicle secretory protein VI as possible marker proteins in urinary bladder preneoplastic lesions induced by N-butyl-N-(4-hydroxybutyl) nitrosamine.

BACKGROUND: A simple and non-invasive methods for the diagnosis of transitional cell carcinoma of the bladder are needed for the prevention of invasive tumor. A proteomic technology has recently been developed to facilitate protein profiling of biological mixtures. We tried to detect the marker proteins by proteomic approach during the initiation stages on N-butyl-N-(4-hydroxybutyl) nitrosamine (BBN)-induced bladder carcinogenesis in rats. METHODS: Ten rats in group A were given 0.05% BBN in drinking water for 12 weeks. Other 10 rats in group B with 10 rats were designated as a control group and were not given BBN. Whole urinary bladders of all rats were excised at 12 weeks from the beginning of the experiment. Conventional proteomics was performed with high resolution 2-dimension gel electrophoresis followed by computational image analysis and protein identification using mass spectrometry. RESULTS: A comparison of urinary bladder hyperplasia tissue with control tissue showed that five proteins; actin gamma2 propeptide, cytokeratin-20 (CK-20), proapolipoprotein, alpha2 actin (alpha-cardiac actin) and heat shock 27 kDa protein-1 were over-expressed in hyperplastic tissues. Three proteins; transcription factor myocardin, seminal vesicle secretory protein VI (SVS-VI) precursor and hypothetical protein RMT-7 were under-expressed in hyperplastic tissues. CONCLUSION: In our animal mode, BBN-induced urinary bladder mucosal hyperplasia resulted in an increase in the expression of five proteins and a decrease in the expression of three proteins. Of these, CK-20 and SVS-VI seem to be of particular interest. However other method such as Western blotting seems to be needed for confirmation of these proteins and more information on human bladder tissue is needed for clinical application.

Animals↗

PubMed1991

Inability of Tfm (testicular feminization) epithelial cells to express androgen-dependent seminal vesicle secretory proteins in chimeric tissue recombinants.

To assess the role of androgen receptors (ARs) in the expression of androgen-dependent seminal vesicle (SV) secretory proteins, tissue recombinants were prepared with rat seminal vesicle mesenchyme plus ureter epithelium of wild-type or Tfm mice (rat SVM plus wild-type mouse URE and rat SVM plus Tfm mouse URE, respectively). After growth in male hosts, both the wild-type and Tfm ureter epithelia were induced by SVM to differentiate into a simple columnar epithelium exhibiting the complex folded morphology characteristic of the SV. In SVM plus wild-type mouse URE recombinants, epithelial ARs were induced, and the epithelium expressed the full spectrum of SV secretory proteins. By contrast, in SVM plus Tfm mouse URE recombinants, the Tfm epithelium was genetically incapable of producing functional ARs and failed to produce SV secretory proteins. These data demonstrate in vivo that the induction of SV secretory proteins by androgens is an event requiring intraepithelial ARs. In contrast, androgen-dependent epithelial morphogenesis, columnar cytodifferentiation, and probably also proliferation can be expressed in Tfm epithelium grown in association with wild-type mesenchyme, strongly suggesting that these events are indirect effects on the epithelium mediated by mesenchymal ARs.

Androgens↗

PubMed1994

Suppression of rat epididymal sperm immunogenicity by a seminal vesicle secretory protein and transglutaminase both in vivo and in vitro.

The pretreatment of epididymal spermatozoa with SV-IV, one of the major secretory protein produced by the epithelium of adult rat seminal vesicles, was found to markedly decrease their ability to induce in vivo peritoneal macrophage activation, measured as class II major histocompatibility complex surface antigen expression, superoxide anion production, phagocytic activity, and antigen presentation. In addition, the treatment of spermatozoa with SV-IV produced a significant decrease of their immunogenicity evaluated in vitro by [3H]thymidine incorporation in splenocyte/spermatozoon co-culture. The concurrent presence of SV-IV and transglutaminase, an enzyme secreted in large amounts from the rat anterior prostate, amplified these phenomena. The suppression of the epididymal sperm immunogenicity is suggested to be of crucial importance for the prevention of the immune response to the sperm introduced in the immunocompetent female genital tract during coitus.

Animals↗

PubMed1984

Polymorphism of rat seminal vesicle secretory proteins: characterization of svp-1 and svp-2 and their identification with the major secretory proteins IV and V.

The proteins secreted by the rat seminal vesicle can be separated into five denaturing conditions. Two polymorphic proteins, svp-1 and svp-2, also present in the mouse, are produced by the seminal vesicle as well, but the procedure used for their identification makes it impossible to ascertain whether they correspond to any of the major fractions mentioned above. We show here that, on the basis of molecular weight measurements and of amino acid composition determinations, svp-1 and RSV-V are indeed the same protein. We also show that svp-2 is strictly related to another major secretory protein, RSV-IV, whose amino acid composition is almost identical, but for a few amino acid residues, to that of svp-2. We thus conclude that the latter protein is a variant of RSV-IV that can be expressed only in rats homozygous for a given allele at the svp-2 locus. This paper thus brings together published information on the genetics of the loci coding for svp-1 and for svp-2 and on the molecular biology of RSV-IV and RSV-V and of their corresponding gene.

Amino Acids↗