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Biomedical subjects

G Peluso

Publications and source records attributed to G Peluso.

At least 55 records · Page 3Linked to original sources
PubMed1994

In vivo induction of macrophage Ia antigen (MHC class II) expression by biomedical polymers in the cage implant system.

Examination of the cellular components in the inflammatory exudate, which infiltrates subcutaneous cages, can be used to monitor the progress of an inflammatory response to an implanted material. Of particular interest is the study of monocyte/macrophage infiltration into the implanted cages containing biomaterials, as macrophages may initiate a wide spectrum of responses upon interaction with a foreign material. In this study, the authors propose a technique using subcutaneous tissue cages in conjunction with cytofluorimetric analysis of exudate leukocytes to evaluate the monocyte/macrophage cell activation in response to different materials. The studies reported here used several materials (thermoplastic and elastomeric polymers) as the challenging agent, to demonstrate whether polymers, chemically different from each other, could differentially activate macrophages to carry out their proinflammatory role more effectively. The materials tested included: poly(etherurethane ureas) (PEUU A'), poly(etherurethane ureas) with a surface active additive, Methacrol, (PEUU C'), polymethylsiloxane (PDMS), polyetherimide, (PEI), and polyetheretherketone, (PEEK). For all tested materials, the maximum numbers of exudate cells and of Ia-positive macrophages were found on day 7, although the entity of the cell increase was associated with the material used for the implant. Similarly, the percentage of Ia-positive macrophages varied according to the specific polymer present in the cages after 7 days. By day 14, the percentage of Ia-positive macrophages decreased with individual exudates showing 19-32% Ia-positive cells depending on the different type of material. Only in the case of PDMS did the percentage of Ia-positive macrophages remain the same as compared with control empty cage macrophages.

Animals↗
PubMed1994

Chitosan-mediated stimulation of macrophage function.

According to the modern definition of biocompatibility, a biocompatible material need not be inert but be bioactive. A benign reactivity implies that the reactivity has to be appropriate for the intended use. Chitosan, a non-acetylated or partially deacetylated chitin (a linear homopolymer of beta (1-4)-linked N-acetylglucosamine) has been proposed as a biomaterial because of its apparent satisfactory biocompatibility. The present investigation demonstrates that chitosan has an in vitro stimulatory effect on both macrophage nitric oxide (NO) production and chemotaxis. The macrophage NO secretion is attributed to the N-acetylglucosamine unit of the chitosan molecule rather than to the glucosamine residue (28 and 15 microM NO respectively). Moreover, the immune stimulatory effect of chitosan was very specific since other glycosaminoglycans, such as N-acetyl-D-mannosamine and N-acetyl-D-galactosamine, had no effects on NO production (5 and 8 respectively). In vivo experiments strengthen this hypothesis. Transmission electron microscopy analysis identifies the presence of many leucocytes in the specimens after 14 d post-implantation, showing poor healing processes (i.e. fibroblast proliferation and collagen deposition) that characterize the tissue repair at this time in our animal model.

Acetylglucosamine↗
PubMed1994

Suppression of rat epididymal sperm immunogenicity by a seminal vesicle secretory protein and transglutaminase both in vivo and in vitro.

The pretreatment of epididymal spermatozoa with SV-IV, one of the major secretory protein produced by the epithelium of adult rat seminal vesicles, was found to markedly decrease their ability to induce in vivo peritoneal macrophage activation, measured as class II major histocompatibility complex surface antigen expression, superoxide anion production, phagocytic activity, and antigen presentation. In addition, the treatment of spermatozoa with SV-IV produced a significant decrease of their immunogenicity evaluated in vitro by [3H]thymidine incorporation in splenocyte/spermatozoon co-culture. The concurrent presence of SV-IV and transglutaminase, an enzyme secreted in large amounts from the rat anterior prostate, amplified these phenomena. The suppression of the epididymal sperm immunogenicity is suggested to be of crucial importance for the prevention of the immune response to the sperm introduced in the immunocompetent female genital tract during coitus.

Animals↗
PubMed1994

Biological activities of CNBr fragments of a major protein secreted from the rat seminal vesicle epithelium.

Two fragments of SV-IV, one of the major proteins secreted from the rat seminal vesicle epithelium, were produced in vitro by protein cleavage with CNBr at level of the single methionine residue (Met-70) occurring in its polypeptide chain. After their purification by reversed-phase chromatography, SV-IV/A (1-70 fragment) and SV-IV/B (71-90 fragment) were assayed as transglutaminase substrates, and their anti-inflammatory, anti-thrombotic and immunosuppressive properties were evaluated in comparison with native SV-IV. Both fragments retained the SV-IV ability to act as transglutaminase substrates in vitro; fast atom bombardment mass spectrometry analyses of the reaction products pointed to Gln-9 and Gln-86 as acyl donor sites, and to Lys-59, -79 and -80 as acyl acceptor sites. In contrast, only SV-IV/A was shown to possess, like SV-IV, the property of inhibiting both the intensity of the carrageenin-induced rat foot edema and the platelet aggregation induced in vivo by different agents. Finally, the two protein fragments were found to be completely unable to inhibit both the mitogen-induced proliferation of human T cells and the mixed lymphocyte reaction.

Amino Acid Sequence↗
PubMed1993

Inhibition of interleukin-1 release and activity by the rat seminal vesicle protein SV-IV.

SV-IV, a 9.8-kd protein isolated from rat seminal vesicle secretion, has been shown to have strong non-species-specific immunosuppressive, anti-inflammatory, antithrombotic, and antiphospholipase A2 properties. The present investigation was undertaken to determine the mechanism of action of its immunosuppressive effects. It was found that SV-IV is a potent inhibitor of interleukin-1 (IL-1) release from lipopolysaccharide (LPS)-activated human adherent monocytes and an effective inhibitor of IL-1-induced thymocyte proliferation. The ability of SV-IV to form a noncovalent dimeric association with IL-1 alpha but not with IL-1 beta, its ability to induce a marked decrease of IL-1 binding to its own receptors on the thymocyte surface, and its capacity to bind specifically to the macrophage plasma membrane might play an important role in the molecular mechanism of these inhibitory effects.

Animals↗
PubMed1991

Macrophage activation induced by different carbon fiber-epoxy resin composites.

The activation of cells by interaction with solid surfaces is important in many settings, including the response of tissue to implanted materials. However, few comprehensive studies of both cell migration and activation have been performed so that the connection between these events and immunological activation against foreign material is not well understood. In the present study, synthesis and expression of Ia antigens by peritoneal exudate macrophages after implantation of different carbon fiber composites in the rat peritoneal cavity have been investigated in order to determine whether the type of material implanted affected the composition of Ia-bearing cells of the exudate. The results have confirmed the low level of expression of Ia on resident peritoneal macrophages; while we have found that macrophages, harvested after implantation, express a different amount of Ia related to the different cure cycles of the composite material used.

Animals↗
PubMed1991

Rat peritoneal immune response to carbon fibre reinforced epoxy composite implants.

The aim of this paper was to evaluate the histocompatibility of differently cured carbon fibre reinforced epoxy composites, studying their potential to induce an intolerance reaction in neighbouring tissues after peritoneal implantation in the rat. According to the microscopic and scanning electron microscope findings, the inductive capacity to generate connective tissue and cellular reaction was greatest in the partially cured material compared to the fully cured material. In addition, only the partially cured material implants appeared totally coated by macrophages at various stages of activation. The differences in the cellular reactions and scar tissue deposition in the interstices of these two composites are probably related to the chemical surface properties rather than to the structural characteristics of the materials.

Adsorption↗
PubMed1991

31P and 1H NMR studies of ethanolamine-linked phosphoglycerides metabolism in human T lymphocytes.

Aqueous and organic extracts of peripheral human T lymphocytes and of T lymphoblastoid cell lines have been examinated by 31P and 1H NMR spectroscopy in order to study the metabolism of ethanolamine (Etn) linked phosphoglycerides. The results show that the Etn concentration in the culture medium determines the composition of Etn-containing metabolites and phospholipids. The effect of phorbol esters, stimulating the synthesis and the breakdown of choline-containing phospholipids has been also studied. A phorbol 12-myristate 13-acetate (PMA) dependent membrane phosphatidylethanolamine hydrolysis, presumably mediated by protein kinase C activity, has been demonstrated.

Cells, Cultured↗
PubMed1990

An anti-inflammatory protein secreted from the rat seminal vesicle epithelium inhibits the synthesis of platelet-activating factor and the release of arachidonic acid and prostacyclin.

Platelet-activating factor (PAF), a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine, is a mediator of inflammation and endotoxic shock produced by a variety of stimulated cells. Since the main biosynthetic pathway of PAF involves acetylation of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) generated from 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine by phospholipase A2, we suggest a general physiological role played by steroid-induced anti-(phospholipase A2) proteins in the modulation of PAF synthesis. The results of the present study support this hypothesis since an androgen-induced anti-inflammatory protein, SV-IV, secreted from rat seminal vesicles, inhibits PAF synthesis in stimulated polymorphonuclear neutrophils, macrophages and endothelial cells. SV-IV impairs PAF synthesis by inhibiting the activation of phospholipase A2, that also results in the inhibition of arachidonic acid and prostacyclin release, and of acetyl-CoA:lyso-PAF acetyltransferase.

Acetyltransferases↗
PubMed1990

In vivo and in vitro inhibition of platelet aggregation by SV-IV, a major protein secreted from the rat seminal vesicle epithelium.

In summary, the present study documents that platelet aggregation triggered by thrombin, ADP, collagen and PAF both in vivo and in vitro, was prevented by SV-IV in a dose-dependent manner. Only platelet aggregation by AA was not affected by the protein, thus suggesting a possible involvement of PLA2 inhibition in the molecular mechanism at the basis of SV-IV anti-thrombotic effect.

Animals↗
PubMed1990

Transglutaminase-catalyzed modifications of SV-IV, a major protein secreted from the rat seminal vesicle epithelium.

One of the major proteins secreted from the rat seminal vesicle epithelium, namely SV-IV, was shown to act in vitro as acyl donor and acceptor substrate for transglutaminase from both guinea pig liver and rat anterior prostate secretory fluid. Electrophoretic and chromatographic experiments indicated that the enzyme catalyzed the formation of multiple modified forms of SV-IV. In the absence of small Mr amines, transglutaminase was able to produce at least six different molecular forms of the protein, half of which possessed an Mr higher than that of native SV-IV. These findings suggested that a variable number of intermolecular, and perhaps intramolecular, crosslinks were formed between one or both glutamine residues and one or more lysine residues occurring in the SV-IV polypeptide chain. In addition, at least three modified forms of the protein were produced by transglutaminase in the presence of high concentrations of spermidine, thus indicating the formation of different (gamma-glutamyl)polyamine derivatives of SV-IV. Rabbit uteroglobin and rat anterior prostate secretory protein(s) were also shown to be able to covalently bind spermidine in the presence of the enzyme. The possible biological significance of transglutaminase-mediated modifications of SV-IV, as well as of other proteins occurring in the mammal seminal fluid, are discussed.

Animals↗
PubMed1989

Immunosuppressive and anti-inflammatory properties of a major protein secreted from the epithelium of the rat seminal vesicles.

The nonspecies specific immunosuppressive and anti-inflammatory properties of a major protein (SV-IV) secreted from the epithelium of rat seminal vesicles (SV) are described. To detect the immunosuppressive effect, peripheral blood lymphocytes (PBL) were pretreated for 2 hr at 37 degrees with SV-IV, and the protein was maintained in the incubation medium during the whole culture time. We obtained evidence that, during preincubation of PBL and SV-IV the protein was transformed by a transglutaminase (TGase) released from PBL into modified low and high molecular weight forms able to bind to PBL surfaces. It is suggested that T lymphocytes are the possible targets of the immunosuppressive effect. SV-IV seems to inhibit only the early phase of the proliferative response of T lymphocytes to mitogens without having any direct effect on the enzymatic system involved in DNA synthesis. Moreover, the protein SV-IV was also shown to possess an anti-inflammatory property due to a block of the arachidonic acid cascade at the level of the enzyme phospholipase A2 (PLA2). The physiological significance of the immunosuppressive and anti-inflammatory properties of SV-IV are discussed in relation to different aspects of the mammalian reproduction.

Animals↗
PubMed1989

Inhibitory effect of SV-IV, a major protein secreted from the rat seminal vesicle epithelium, on phagocytosis and chemotaxis of human polymorphonuclear leukocytes.

The effect of SV-IV, one of the major proteins secreted from the rat seminal vesicle epithelium, on phagocytosis and chemotaxis of human polymorphonuclear leukocytes (PMNs) has been studied. Various cytological, biochemical, metabolic, and physical correlates of both biological activities have been found to be markedly reduced by the presence in the medium of micromolar concentrations of protein SV-IV. Moreover, the Scatchard analysis of the labeled SV-IV binding to PMN cell surface has demonstrated that such binding is specific. The binding sites contain only saturable components, completely displaceable by unlabeled SV-IV. The number of the specific sites has been calculated to be 87,000/cell, with a Kd of 1.72 X 10(-7) M. The molecular mechanism of the inhibitory effect is discussed along with the possible biological and clinical implications of the experimental findings.

Animals↗
PubMed1989

Inhibition of macrophage phagocytic activity by SV-IV, a major protein secreted from the rat seminal vesicle epithelium.

The protein SV-IV, one of the major secretory proteins produced by the rat seminal vesicle epithelium, has been found to possess a marked ability to inhibit in vitro the phagocytic properties of activated peritoneal rat macrophages, by a mechanism that apparently involves phagocytes and target cells. Although SV-IV is a substrate for transglutaminase (TGase), an enzyme secreted by activated macrophages, TGase does not seem to play any significant role either in the binding of the protein to the cells participating in the phagocytic process or in the inhibition of macrophage phagocytosis by SV-IV. The significance of the findings in relation to the reproductive process and their possible clinical implications are discussed.

Animals↗
PubMed1988

Cancer antigen 125, tissue polypeptide antigen, carcinoembryonic antigen, and beta-chain human chorionic gonadotropin as serum markers of epithelial ovarian carcinoma.

Cancer antigen 125 (CA 125) is common to most epithelial ovarian tumors. Therefore, it is potentially a good marker of this disease. This hypothesis was evaluated by measuring the serum levels of CA 125 in 81 patients with ovarian cancer (25 with nonactive and 56 with active disease), in 105 patients of both sexes with nonovarian tumors, and in 171 healthy controls of both sexes. The serum levels of three other markers, tissue polypeptide antigen (TPA), carcinoembryonic antigen (CEA), and human chorionic gonadotropin, beta subunit (beta-hCG), were also measured in the same 357 subjects. The results of this study clearly indicate the clinical irrelevance of both CEA and beta-hCG as tumor markers in ovarian carcinomas. Conversely, the clinical usefulness of CA 125 and TPA was confirmed. In particular, CA 125 and TPA showed comparable sensitivity, while CA 125 showed a higher specificity for ovarian cancer than TPA. The association of CA 125 with TPA was very useful in continuous observation of patients with active disease in order to evaluate the clinical effectiveness of the therapy. Moreover, for patients in clinical remission, the markers allowed early detection of a recurrence of the disease.

Adult↗