Use of a cloned double stranded cDNA coding for a major androgen dependent protein in rat seminal vesicle secretion: the effect of testosterone in gene expression

Mansson, Per-Erik; Akio, Sugino; Harris, S. E.

doi:10.1093/nar/9.4.935

Cited by 89 publications

(72 citation statements)

References 24 publications

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“…Seminal vesicle (SV) protein 4 (SV-IV; according to its mobility by sodium dodecyl sulfate [SDS]-polyacrylamide gel electrophoresis [PAGE]) is a small (M r , 9,758), basic (pI 8.9), thermostable, secretory protein produced in large amounts by the SV epithelium of the adult rat under the strict transcriptional control of androgen (1,15,24). Proteins immunologically related to SV-IV have also been identified in several rat tissues (uterus, lung, liver, brain, etc.)…”

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confidence: 99%

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Effect of Protein SV-IV on ExperimentalSalmonella entericaSerovar Typhimurium Infection in Mice

Romano-Carratelli

Bentivoglio

Nuzzo

et al. 2002

Clin Vaccine Immunol

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Seminal vesicle protein IV (SV-IV) is a secretory anti-inflammatory, procoagulant, and immunomodulatory protein produced in large amounts by the seminal vesicle epithelium of the rat under the strict transcriptional control of androgen. In particular, this protein was shown to possess the ability to markedly inhibit in vivo the humoral and cell-mediated immune responses of mice to nonbacterial cellular antigens (sheep erythrocytes and spermatozoa). We report data that demonstrate that in mice treated with SV-IV and infected with Salmonella enterica serovar Typhimurium, SV-IV is able to downregulate some important immunological and biochemical parameters that serovar Typhimurium normally upregulates in these animals. This event did not correlate with a lower bacterial burden but was associated with a markedly increased one (300%). Furthermore, the treatment of mice with SV-IV alone also produced a significant increase in the rate of mortality among serovar Typhimurium-infected animals. The mechanism underlying these phenomena was investigated, and the strong immunosuppression produced by SV-IV in serovar Typhimurium-infected mice was suggested to be the basis for the increased rate of mortality. The SV-IV-mediated immunosuppression was characterized by a decrease in the humoral and cell-mediated immune responses, altered lymphocyte-macrophage interaction, downregulation of cytokine and inducible nitric oxide synthase gene expression, inhibition of macrophage phagocytosis and intracellular killing activities, and absence of apoptosis in the splenocyte population of SV-IV-and serovar Typhimurium-treated mice. The immunosuppressive activity of SV-IV was specific and was not due to aspecific cytotoxic effects. SV-IV-specific receptors (K d ‫؍‬ 10 ؊8 M) occurring on the macrophage and lymphocyte plasma membranes may be involved in the molecular mechanism underlying the SV-IV-mediated immunosuppression. Some results obtained by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay also revealed a functional impairment of mitochondria (a decrease in mitochondrial dehydrogenase activity), thus indicating the possible implication of these organelles in the immunosuppressive process.

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“…as well as in human seminal fluid and SV secretions (2,17,18). The SV-IV protein has been purified to homogeneity and extensively characterized (1,2,15,17,18,24,25,35). Its 90-amino-acid sequence is known, and the gene coding for it has been isolated, sequenced, and expressed in Escherichia coli (6,12,13,16).…”

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confidence: 99%

Effect of Protein SV-IV on ExperimentalSalmonella entericaSerovar Typhimurium Infection in Mice

Romano-Carratelli

Bentivoglio

Nuzzo

et al. 2002

Clin Vaccine Immunol

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“…tures of the SVS 11, IV, and V components are known (Pan et al, 1980: Mansson et al, 1981Harris et al, 1983Harris et al, , 1990McDonald et al, 1984;Williams et al, 1985). Molecular analysis has shown that SVS I1 is the major component of the copulatory plug (Manyai, 1964: Hart, 1970), but SVS I and SVS I11 are probably plug constituents as well as they form high-molecularmass complexes with SVS I1 by cystine bridges (Wagner and Kistler, 1987).…”

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Chemical Characterization of the Predominant Proteins Secreted by Mouse Seminal Vesicles

Lundwall¹,

Peter²,

Lövgren³

et al. 1997

European Journal of Biochemistry

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Mouse seminal vesicles secrete four major protein components with estimated molecular masses of 95, 38, 17, and 16 kDa. Amino acid sequencing revealed that the 95-kDa component represents a protein with an unknown structure, while the 38-kDa component was identified as semenoclotin, the 17-kDa component as seminal-vesicle-secreted protein IV, and the 16-kDa component as seminal-vesicle-secreted protein V. Semenoclotin and the 95-kDa component were readily cross-linked by transglutaminase, suggesting that the two proteins are involved in the formation of the mouse copulatory plug. Treatment of mouse seminal vesicle fluid with human prostate-specific antigen rapidly degraded semenoclotin, indicating a structural resemblance of this protein to human semenogelins, despite the vast difference in primary structure. As previously reported for other seminal-vesicle-secreted proteins, the semenoclotin transcripts are shown to be under androgen control.Keywords: seminal vesicle ; semen ; androgen; transglutaminase ; coagulation.Mammalian semen is formed by the mixing of spermatozoarich fluid from epididymis with secretions from the accessory sex glands during ejaculation, that mainly consists of fluids from the seminal vesicles and the prostate (Mann and Lutwark-Mann, 1981). In most species, the major contribution is provided by the seminal vesicles, amounting to more than half of the semen volume. The newly ejaculated sperm is highly viscous or gellike, but within a short time it will either liquefy, as in man, or transform into a firm coagulum, yielding a copulatory plug through the action of a prostate-secreted transglutaminase, as seen in rodents.The proteins responsible for gel and clot formation are present at very high concentrations in the seminal vesicle fluid. Somewhat unexpectedly, the primary structure of these proteins are highly dissimilar between species (Lundwall and Lazure, 1995; Lundwall and Ulvsback, 1996). This is caused by a relatively recent evolution of an ancestral gene, involving duplications, exon expansion, and varying selection of splice sites. The genes constitute the REST gene family (abbreviation for rapidly evolving substrates for transglutaminase) as most members seem to encode substrates for transglutaminase (Lundwall, 1996 : Lundwall and Ulvsback, 1996).The rat seminal vesicle secretion consists of five predominant protein components, designated seminal-vesicle-secreted proteins I-V (SVS I-V) in order of size (Ostrowski et al., 1979). The SVS IV and V components are also referred to as S and F proteins by some authors (Higgins et al., 1976). The strucCorrespondence to A. Lundwall,

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“…4, according to its mobility in SDS/PAGE), a basic, thermostable, secretory protein of low MW (9758) synthesized by the rat seminal vesicle (SV) epithelium under strict androgen transcriptional control (Ostrowski, 1979;Mansson, 1981;Lwaleed, 2004). SV-IV has been purified to homogeneity and characterized extensively (Ostrowski, 1979;Mansson, 1981;Pan, 1982;Harris, 1983;Kandala, 1983;McDonald, 1983;Abrescia, 1985Abrescia, ,1986Metafora, 1987a;D'Ambrosio, 1993;Stiuso, 1999;Lwaleed, 2004). Proteins immunorelated by SV-IV have been found in several rat tissues (uterus, lung, liver, brain, etc.…”

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confidence: 99%

The N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates α-thrombin activity: potential clinical implications

et al. 2008

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We have previously shown that seminal vesicle protein IV (SV-IV) and its 1-70 N-terminal fragment have anti-inflammatory activity and modulate anti-thrombin III (AT) activity. Moreover, mass spectrometry analysis of purified SV-IV has shown that the protein was found to be highly heterogeneous and 14% of the total SV-IV molecules are truncated forms, of particular interest the 1-16, 1-17, and 1-18 peptides. In this work we report experimental data which demonstrate that the 1-16 peptide (P1-16) possesses a marked effect on the AT activity by preventing the formation of the thrombin-AT complex. We found that the formation of thrombin-AT complex is markedly decreased in the presence of P1-16 used at equimolar concentration with thrombin as evaluated with SDS-PAGE. We also monitored the conformational changes of thrombin in the presence of different P1-16 concentrations, and calculated the K d of thrombin/P1-16 system by circular dichroism technique. The probable interaction sites of P1-16 with thrombin have been also evaluated by molecular graphics and computational analyses. These results have potential implications in the treatment of sterility and thrombotic diseases.

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Use of a cloned double stranded cDNA coding for a major androgen dependent protein in rat seminal vesicle secretion: the effect of testosterone in gene expression

Abstract: The abundant class of poly(A+)RNA [poly(A+)RNA ] from rat seminal vesicle was used to synthesize ds-cDNA1 . The ds-ckAA

Cited by 89 publications

References 24 publications

Effect of Protein SV-IV on ExperimentalSalmonella entericaSerovar Typhimurium Infection in Mice

Effect of Protein SV-IV on ExperimentalSalmonella entericaSerovar Typhimurium Infection in Mice

Chemical Characterization of the Predominant Proteins Secreted by Mouse Seminal Vesicles

The N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates α-thrombin activity: potential clinical implications

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