Rat Seminal Vesicle Protein SV-IV and Its Transglutaminase-Synthesized Polyaminated Derivative SPD2-SV-IV Induce Cytokine Release from Human Resting Lymphocytes and Monocytesin Vitro

Tufano, Maria Antonietta; Porta, Raffaele; Farzati, Bartolomeo; Pierro, Próspero Di; Rossano, Fabio; Catalanotti, P; Baroni, Adone; Metafora, Salvatore

doi:10.1006/cimm.1996.0061

Cited by 31 publications

(62 citation statements)

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“…Similar results were obtained with resting or antigen-stimulated CTLs. In addition, the possibility that the immunosuppression was due to aspecific cytotoxic properties can be ruled out by the following observations: 1) immunosuppression was detectable on activated MNC (see Results) only at low concentrations (5 to 30 M), rich in biologically active SV-IV monomers; at similar low concentrations SV-IV did not inhibit but, in contrast, stimulated quiescent lymphocytes to synthesize and release specific cytokines (Tufano et al, 1996); 2) at concentrations higher than 30 M, rich in biologically inactive SV-IV trimers, no cytotoxic effects were observed (Stiuso et al, 1999); 3) the inhibitory effects of SV-IV on proliferation were found only for immunocompetent cells (Metafora et al, 1989); 4) in addition, SV-IV has been recently demonstrated to possess intrinsic antiapoptotic activity (Morelli et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…SV-IV possesses a nonspecies-specific ability to modulate inflammation and humoral and cellmediated immune response (Metafora et al, 1989;Peluso et al, 1994;Romano-Carratelli et al, 1995;Tufano et al, 1996;Santagada et al, 2002), to stimulate horseradish and Se-dependent peroxidases (Metafora et al, 2001 and unpublished data), to protect its target cells against oxidative stress-associated apoptosis and, in particular, to defend nonself epididymal spermatozoa from immunological or reactive oxygen species (ROS) attacks in the female genital tract (Paonessa et al, 1984;Morelli et al, 2007). The anti-inflammatory properties are related to phospholipase A 2 (PLA 2 ) inhibition (Metafora et al, 1989), whereas the pro-inflammatory features are based on SV-IV ability to stimulate mast-cell and basophil degranulation with concurrent release of histamine and other mediators (Metafora et al, manuscript in preparation).…”

Section: Introductionmentioning

confidence: 99%

“…The anti-inflammatory properties are related to phospholipase A 2 (PLA 2 ) inhibition (Metafora et al, 1989), whereas the pro-inflammatory features are based on SV-IV ability to stimulate mast-cell and basophil degranulation with concurrent release of histamine and other mediators (Metafora et al, manuscript in preparation). The modulation of immune response is caused by interference of the protein with macrophage-T cell cooperation (Metafora et al, 1989;Peluso et al, 1994;Romano-Carratelli et al, 1995;Tufano et al, 1996;Santagada et al, 2002). Natural killer cells (NKs) and antigen-specific cytotoxic T lymphocytes (CTLs) are involved in host resistance to infections, immune surveillance against tumors, and rejection of transplanted tissues.…”

Section: Introductionmentioning

confidence: 99%

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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: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Fuggetta

Lanzilli

Cottarelli

et al. 2008

Journal of Reproductive Immunology

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“…There are also reports claiming that all of the major components might be involved in plug formation as they may serve as substrates for transglutaminase (Fawell et al, 1986;. However, it is likely that the cmall components do not primarily exert their function as plug constituents: SVS IV has been shown to exhibit immune modulating activity (Romano-Carratelli et al, 1995: Tufano et al, 1996.…”

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confidence: 99%

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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“…), in human seminal fluid and SV secretion (Abrescia, 1985(Abrescia, , 1986Metafora, 1987a). SV-IV possesses potent non-species specific immunomodulatory and antiinflammatory activities, and modulates the coagulation process by affecting the thrombin-antithrombin III (AT) interaction (Galdiero, 1989;Metafora, 1989a, b;Camussi, 1990;Romano-Carratelli 1993;Vuotto, 1993;Di Micco 1994, 2000Peluso, 1994;Mancuso, 1996;Tufano, 1996). Moreover, it can bind the plasma membrane of epididymal spermatozoa, decreasing the immunogenicity of SV-IV (Pavonessa, 1984;Metafora, 1987b;Peluso, 1994).…”

Section: Introductionmentioning

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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Rat Seminal Vesicle Protein SV-IV and Its Transglutaminase-Synthesized Polyaminated Derivative SPD2-SV-IV Induce Cytokine Release from Human Resting Lymphocytes and Monocytesin Vitro

Cited by 31 publications

References 0 publications

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

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

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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