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1.
J Reprod Immunol ; 78(2): 85-93, 2008 Jul.
Article in English | MEDLINE | ID: mdl-18243331

ABSTRACT

The in vitro effect of seminal vesicle protein IV (SV-IV) on the cytotoxic activity of human natural or acquired cellular immunity has been investigated by standard immunological procedures, a (51)Cr-release cytotoxicity assay, and labeled-ligand binding experiments. The data obtained demonstrate that: (1) fluoresceinated or [(125)I]-labeled SV-IV binds specifically to the surface of human purified non-adherent mononuclear cells (NA-MNC); (2) SV-IV suppresses the cytotoxicity of natural killer (NK) cells against K562 target cells, that of IL-2-stimulated NK (LAK) cells against DAUDI target cells, and that of VEL antigen-sensitized cytotoxic T lymphocytes (CTLs) against VEL target cells; (3) treatment of K562 target cells alone with SV-IV decreases their susceptibility to NK-induced lysis. These findings indicate that the protein SV-IV has a marked in vitro inhibitory effect on NK, LAK and CTL cytotoxicity, providing a better understanding of its immune regulatory functions.


Subject(s)
Killer Cells, Lymphokine-Activated/immunology , Killer Cells, Natural/immunology , Leukocytes, Mononuclear/immunology , Seminal Vesicle Secretory Proteins/metabolism , T-Lymphocytes, Cytotoxic/immunology , Cell Line, Tumor , Cytotoxicity, Immunologic , Humans , Immunity, Cellular , K562 Cells , Killer Cells, Lymphokine-Activated/metabolism , Killer Cells, Natural/metabolism , Leukocytes, Mononuclear/metabolism , Seminal Vesicle Secretory Proteins/immunology , Seminal Vesicle Secretory Proteins/isolation & purification , T-Lymphocytes, Cytotoxic/metabolism
2.
Eur J Biochem ; 268(13): 3858-69, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11432754

ABSTRACT

In this study we show that SV-IV, a major immunomodulatory, anti-inflammatory, and sperm immunoprotective protein secreted from the rat seminal vesicle epithelium, acts in vitro as a substrate of protein kinase C (PKC) competing efficiently with H1 histone, a very well known PKC substrate. Electrospray mass spectrometry (ES-MS) analysis demonstrated that approximately 10% of the native SV-IV molecules were phosphorylated by PKC and that such a modification involved only a single serine residue (Ser58) out of the 22 occurring in the protein. Interestingly, this modification produced a substantial enhancement (approximately 50%) of the native SV-IV's ability to stimulate the activity of both horseradish peroxidase (POD) and selenium-dependent glutathione peroxidase (GPX), an enzyme that is known to protect the mammalian spermatozoa from oxidative stress and loss of motility in the female genital tract following ejaculation. In contrast, the phosphorylation of SV-IV on Ser58 did not produce any effect on the anti-inflammatory properties of SV-IV, as measured by its ability to inhibit the phospholipase A2.


Subject(s)
Cyclic AMP-Dependent Protein Kinases/metabolism , Glutathione Peroxidase/metabolism , Horseradish Peroxidase/metabolism , Protein Kinase C/metabolism , Proteins/chemistry , Proteins/metabolism , Seminal Vesicles/metabolism , Serine , Amino Acid Sequence , Animals , Chromatography, High Pressure Liquid , Kinetics , Male , Molecular Sequence Data , Peptide Fragments/chemistry , Phosphorylation , Proteins/isolation & purification , Rats , Rats, Inbred F344 , Rats, Wistar , Seminal Plasma Proteins , Spectrometry, Mass, Electrospray Ionization , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Tetradecanoylphorbol Acetate/pharmacology
3.
Eur J Biochem ; 268(12): 3399-406, 2001 Jun.
Article in English | MEDLINE | ID: mdl-11422369

ABSTRACT

SV-IV is a basic, thermostable, secretory protein of low Mr (9758) that is synthesized by rat seminal vesicle (SV) epithelium under strict androgen transcriptional control. This protein is of obvious pharmacological interest because it has potent nonspecies-specific immunomodulatory, anti-inflammatory, and pro-coagulant activities. In evaluating the clinical relevance and the possible use in medicine of SV-IV, we became interested in the study of its structure-function relationships and aimed to identify in its polypeptide chain specific peptide fragments possessing the marked anti-inflammatory properties of the protein not associated with other biological activities (pro-coagulation and immunomodulation) typical of this molecule. By using two different experimental approaches (the fragmentation of the protein into peptide derivatives by chemical methods and the organic synthesis on solid phase of selected peptide fragments), data were obtained showing that in this protein: (a) the immunomodulatory activity is related to the structural integrity of the whole molecule; (b) the anti-inflammatory activity is located in the N-terminal region of the molecule, the 8-16 peptide fragment being the most active; (c) the identified anti-inflammatory peptide derivatives do not seem to possess pro-coagulant activity, even though this particular function has been located in the 1-70 segment of the molecule.


Subject(s)
Anti-Inflammatory Agents/chemical synthesis , Peptide Fragments/chemical synthesis , Proteins/chemistry , Seminal Vesicle Secretory Proteins , Amino Acid Sequence , Animals , Anti-Inflammatory Agents/chemistry , Coagulants/chemical synthesis , Coagulants/chemistry , Cyanogen Bromide/chemistry , Immunosuppressive Agents/chemical synthesis , Immunosuppressive Agents/chemistry , Male , Molecular Sequence Data , Peptide Fragments/chemistry , Rats , Rats, Wistar
4.
Int J Cancer ; 72(2): 321-8, 1997 Jul 17.
Article in English | MEDLINE | ID: mdl-9219840

ABSTRACT

The treatment of human peripheral blood mononuclear cells (PBMC) with micromolar concentrations of SV-IV, a major protein secreted from the rat seminal vesicle epithelium, promotes in this cell population a marked cytotoxic activity against the Raji lymphoblastoid cell line. This activity is apparently due to cell-to-cell contact interactions. The expression of HLA DR on Raji cells has a modulatory effect on the SV-IV-induced cytotoxic activity. The experimental evidence strongly suggests that the cytotoxic effector cells are functionally activated NK cells.


Subject(s)
Cytotoxicity, Immunologic , Lymphocytes/immunology , Proteins/immunology , Seminal Vesicle Secretory Proteins , Seminal Vesicles/metabolism , Animals , Epithelium/metabolism , Humans , Male , Proteins/metabolism , Rats , Tumor Cells, Cultured
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