The self‐association of protein SV‐IV and its possible functional implications

Stiuso, Paola; Metafora, Salvatore; Facchiano, Angelo; Colonna, Giovanni; Ragone, Raffaele

doi:10.1046/j.1432-1327.1999.00944.x

Cited by 17 publications

(64 citation statements)

References 34 publications

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“…2).These data are consistent with similar binding observations already published (Metafora et al, 1989;Morelli et al, 2007). (Stiuso et al, 1999;Romano-Carratelli et al, 2002). The binding at 37°C was found about 25% lower, probably as consequence of a slight release of counts from cell surface caused by the relatively high Kd.…”

Section: Sv-iv Fitc and [ 125 I]sv-iv Binding To The Surface Of Humansupporting

confidence: 91%

“…The protein was purified to homogeneity from adult rat (Fisher-Wistar strain) seminal vesicle secretion according to a published procedure (Stiuso et al, 1999). A peculiar feature of SV-IV is the high thermoresistance: incubation in boiling water for 30-60 min neither precipitates the protein nor changes its biological properties.…”

Section: Purification Of Protein Sv-ivmentioning

confidence: 99%

“…A peculiar feature of SV-IV is the high thermoresistance: incubation in boiling water for 30-60 min neither precipitates the protein nor changes its biological properties. The concentration of purified SV-IV was evaluated by its molar absorption at 276 nm (4100 M -1 cm -1 ) (Stiuso et al, 1999;Caporale et al, 2004).…”

Section: Purification Of Protein Sv-ivmentioning

confidence: 99%

“…The protein is biologically active between 2 and 30 M. Below the latter value the monomeric active population exceeds the inactive trimeric one with a maximum at about 10 M, while the opposite is true above this concentration (Stiuso et al, 1999;Caporale et al, 2004). …”

Section: Introductionmentioning

confidence: 96%

“…SV-IV gene has been isolated, sequenced, cloned, and expressed in E. coli (D'Ambrosio et al, 1993). The mature protein, purified to homogeneity, has been extensively characterized (Ostrowski et al, 1979;Pan and Li, 1982;Kandala et al, 1983;Stiuso et al, 1999;Caporale et al, 2004). SV-IV is a highly flexible molecule whose biologically active configuration is monomeric, whereas its inactive one is trimeric (Stiuso et al, 1999;Caporale et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Anti-apoptotic seminal vesicle protein IV inhibits cell-mediated immunity

Fuggetta

Lanzilli

Cottarelli

et al. 2008

Journal of Reproductive Immunology

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Section: Sv-iv Fitc and [ 125 I]sv-iv Binding To The Surface Of Humansupporting

confidence: 91%

Section: Purification Of Protein Sv-ivmentioning

confidence: 99%

Section: Purification Of Protein Sv-ivmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Anti-apoptotic seminal vesicle protein IV inhibits cell-mediated immunity

Fuggetta

Lanzilli

Cottarelli

et al. 2008

Journal of Reproductive Immunology

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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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The immunomodulatory protein SV‐IV protects serum‐deprived cells against apoptosis but not against G0/G1 arrest: Possible implications for the survival of implanting embryo

Morelli

Peluso

Petillo

et al. 2007

Journal Cellular Physiology

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Serum deprivation induced in human lymphoblastoid Raji cells oxidative stress-associated apoptotic death and G0/G1 cell cycle arrest. Addition into culture medium of the immunomodulatory protein Seminal vesicle protein 4 (SV-IV) protected these cells against apoptosis but not against cycle arrest. The antiapoptotic activity was related to: (1) decrease of endocellular reactive Oxygen species (ROS) (2) increase of mRNAs encoding anti-oxidant enzymes (catalase, G6PD) and antiapoptotic proteins (survivin, cox-1, Hsp70, c-Fos); (3) decrease of mRNAs encoding proapoptotic proteins (c-myc, Bax, caspase-3, Apaf-1). The biochemical changes underlaying these effects were probably induced by a protein tyrosine kinase (PTK) activity triggered by the binding of SV-IV to its putative plasma membrane receptors. The ineffectiveness of SV-IV to abrogate the cycle arrest was accounted for by its downregulating effects on D1,3/E G1-cyclins and CdK2/4 gene expression, ppRb/pRb ratio, and intracellular ROS concentration. In conclusion, these experiments: (1) prove that SV-IV acts as a cell survival factor; (2) suggest the involvement of a PTK in SV-IV signaling; (3) point to cell cycle-linked enzyme inhibition as responsible for cycle arrest; (4) provide a model to dissect the cycle arrest and apoptosis induced by serum withdrawal; (5) imply a possible role of SV-IV in the survival of hemiallogenic implanting embryos.

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The self‐association of protein SV‐IV and its possible functional implications

Cited by 17 publications

References 34 publications

Anti-apoptotic seminal vesicle protein IV inhibits cell-mediated immunity

Anti-apoptotic seminal vesicle protein IV inhibits cell-mediated immunity

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

The immunomodulatory protein SV‐IV protects serum‐deprived cells against apoptosis but not against G0/G1 arrest: Possible implications for the survival of implanting embryo

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