Isolation and characterisation of genes for androgen-responsive secretory proteins of rat seminal vesicles

McDonald, Charles J.; Williams, Lindsay; McTurk, P; Fuller, Frances M.; Mclntosh, Elizabeth; Higgins, Stephen J.

doi:10.1093/nar/11.4.917

Cited by 65 publications

(49 citation statements)

References 40 publications

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“…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). SV-IV is a very flexible molecule that in aqueous solution behaves as a concentration-dependent self-associating system in which the degree of association (monomer N dimer N trimer equilibrium) appears to control the biological properties of the protein (35).…”

mentioning

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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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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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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“…4,5 The protein SV-IV has a sequence of 90 amino acids 6 and its gene has been isolated, sequenced, and expressed in E.coli. [7][8][9][10][11] The SV-IV gene exists in two forms, which differ by the number of 20-base pair (bp) tandem repeats in an intron (B intron); this intron size variability has been shown to identify an allelic variant by appropriate genetic crosses. 10 The protein SV-IV possesses immunomodulatory, [12][13][14][15] anti-inflammatory 12,16 antiphagocytic, antichemotactic, 17,18 and procoagulant properties [19][20][21] which are not species specific.…”

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confidence: 99%

Structural heterogeneity, post-translational modifications, and biological activities of SV-IV, a major protein secreted from the rat seminal vesicle epithelium

Ferranti¹,

Mamone²,

Malorni³

et al. 1997

Rapid Commun. Mass Spectrom.

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The primary structure of purified SV-IV, a major secretory protein synthesized by the rat seminal vesicle (SV) epithelium, was analysed by electrospray mass spectrometry (ES-MS). The protein was found to be highly heterogeneous. The various components were separated and identified by reversed phase high-performance liquid chromatography (HPLC) on line with ES-MS. Structural characterization of the SV-IV cyanogen bromide digests revealed the occurrence of a Val/Met substitution in about 50% of the purified protein molecules. We suggest that this mutation is the expression of a genetic polymorphism. Other minor components, corresponding to structural changes (fragmentation, deletion, and phosphorylation) of SV-IV and probably due to post-translational modifications of the native protein, were also detected. In particular, by using protein tyrosine phosphatase hydrolysis combined with ES-MS, we demonstrated that, in the phosphorylated species of SV-IV, a single phosphate group was covalently bound to the Tyr-36 residue. The significance of these findings in relation to the regulation of important biological processes, such as immune response, blood coagulation, inflammatory reaction, and mammalian reproduction, are discussed.

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“…P02783) is a purified and extensively characterized (M r = 9,758; pI = 8.9) multifunctional secretory protein. It is synthesized by the rat seminal vesicle epithelium under androgen transcriptional control [1,2,3,4,5] and is encoded by a gene sequenced, cloned, and expressed in Escherichia coli [6,7,8,9]. Its polypeptide chain is a thermostable, intrinsically disordered [10,11,12] and highly flexible molecule.…”

Section: Introductionmentioning

confidence: 99%

Antiapoptotic Seminal Vesicle Protein IV Induces Histamine Release from Human FcεRI+ Cells

Prevete

Rossi

Triggiani

et al. 2009

Int Arch Allergy Immunol

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Background: Seminal vesicle protein number 4 (SV-IV) is a small, basic, multifunctional, intrinsically disordered secretory protein synthesized in large amounts by rat seminal vesicle epithelium under androgen transcriptional control. SV-IV-immunorelated proteins occur in other rat tissues and in humans. Methods: The in vitro effect of SV-IV on human FcΕRI+ cells was investigated by standard immunologic, biochemical and molecular biology procedures. Results: SV-IV-induced histamine release from human basophils and lung mast cells without any influence on leukotriene C₄ release and cell migration. The histamine release rate was slower compared with that induced by anti-IgE, the temperature dependence of the event being similar. SV-IV-induced histamine release was Ca²⁺-dependent, suggesting a physiological interaction of the protein with FcΕRI+ cells. SV-IV and anti-IgE acted synergistically on the histamine release. SV-IV did not induce de novo synthesis of cytokines and growth factors (transforming growth factor-β₁, interleukin-10, interleukin-13, tumor necrosis factor-α, vascular endothelial growth factor A) in FcΕRI+ cells. Conclusions: SV-IV protein induces in human FcΕRI+ cells the release of histamine, a proinflammatory, antiapoptotic and immunosuppressive biogenic amine. These data: (1) are consistent with the antiapoptotic and immunosuppressive properties of SV-IV; (2) confirm a regulatory feature of SV-IV on mammal inflammatory reactivity by either inhibiting the arachidonate cascade pathway or stimulating proinflammatory cytokine release from lymphocyte/monocytes and histamine from FcΕRI+ cells; (3) raise the possibility of a protective role of SV-IV on implanting hemiallogenic blastocysts against maternal reactive oxygen species and immunological attacks at the uterine implantation site.

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Isolation and characterisation of genes for androgen-responsive secretory proteins of rat seminal vesicles

Cited by 65 publications

References 40 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

Structural heterogeneity, post-translational modifications, and biological activities of SV-IV, a major protein secreted from the rat seminal vesicle epithelium

Antiapoptotic Seminal Vesicle Protein IV Induces Histamine Release from Human FcεRI+ Cells

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