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Biomedical subjects

E Ziparo

Publications and source records attributed to E Ziparo.

35 records · Page 2Linked to original sources
PubMed1990

Ontogenesis of the nuclear 3,5,3'-triiodothyronine receptor in the rat testis.

The aim of this study was to investigate the ontogenesis of the nuclear T3 receptor among the different cell types in the rat testis from fetuses at the 19th day of gestation and animals 1, 5, 15, 20, and 60 days after birth. Whole testis, tubular fraction, nontubular fractions, and Sertoli cells cultured in vitro or enriched in vivo by irradiation were used. The results demonstrate that high affinity, low capacity T3-binding sites are localized only in Sertoli cells; the binding specificity and affinity (Kd ranges from 0.8 +/- 0.2 to 2.6 +/- 0.4 nM) do not change significantly with the age of the animals and are comparable to those observed for T3 receptors in other mammalian tissues. In the whole testis, the concentration of receptors changes during gonadal development, being maximally expressed in the fetus (154.3 +/- 8.1 fg T3 bound/10(6) nuclei) and from 1 (203.4 +/- 10.9 fg T3 bound/10(6) nuclei) to 5 (185.3 +/- 15.1 fg T3 bound/10(6) nuclei) days of postnatal life, decreasing significantly at 15 and 20 days (65.4 +/- 2.0 and 57.9 +/- 1.9 fg T3 bound/10(6) nuclei, respectively) and being virtually absent in the adult. The same change in receptor concentration was found in Sertoli cells obtained by different techniques. This ontogenetic profile coincides with the pattern of Sertoli cell proliferation and differentiation, thus suggesting a role of thyroid hormones in the regulation of growth and maturation of the somatic cells of the seminiferous epithelium.

Animals↗
PubMed1989

Modulation of phagocytic activity in cultured Sertoli cells.

Phagocytic activity of rat Sertoli cells that were cultured in vitro has been evaluated as the ability to internalize polystyrene beads. Our data demonstrate that these cells are active phagocytes and that such phagocytic activity is under negative control by follicle-stimulating hormone (FSH). The hormonal control is mediated by increased intracellular levels of cAMP. Moreover Sertoli cell responds to tuftsin, an oligopeptide known to act only on macrophages and granulocytes, by increasing up to five times its phagocytic activity. Phagocytic uptake of polystyrene beads is associated with dramatic changes of the cellular shape. Such morphological modifications are significantly reduced under FSH stimulation. The physiological implications of the data are discussed.

Animals↗
PubMed1989

Spectrin, fodrin and protein 4.1-like proteins in differentiating rat germ cells.

The presence and the distribution of proteins of the membrane skeleton in differentiating germ cells of the rat has been investigated. Immunofluorescence and immunoblotting analysis, performed using monoclonal and polyclonal antibodies to human erythroid alpha-spectrin and protein 4.1 and to brain spectrin (fodrin), demonstrated the presence of analogues of spectrin and fodrin in spermatocytes and round spermatids and of protein 4.1-like molecules in spermatocytes, spermatids and spermatozoa. Spectrin and fodrin showed molecular weights comparable to those of their analogues in erythrocytes but a distinct intracellular distribution. Fodrin was localized along the plasma membrane while spectrin appeared associated with the regions of the Golgi apparatus and of the developing acrosome. Antibodies to protein 4.1 recognized molecules with a molecular weight not comparable with that in erythrocytes, and their presence in spermatozoa was confined to specific regions of the head and of the tail.

Animals↗
PubMed1987

Membrane molecules involved in adhesion properties of cultured Sertoli cells.

Membrane components involved in adhesion properties of cultured Sertoli cells have been studied by a combination of immunological and biochemical methods. An antiserum prepared against Sertoli cells induced reversible rounding and detachment of the cells from the culture dishes. The cell surface morphology during detachment was studied by scanning electron microscopy and indirect immunofluorescence. A Triton soluble fraction of crude membrane preparations inhibited the antibody-induced detachment. The antibodies recognized a restricted number of membrane glycoproteins [detectable as prominent bands on Sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE), Mr 170, 140, 80, and 48K] both in the Triton soluble fraction of crude membrane preparation and on intact Sertoli cells. The data suggest that the molecules involved in adhesion properties of cultured Sertoli cells are integral membrane glycoproteins exposing antigenic determinants at the cell surface.

Animals↗
PubMed1986

Proteins of the membrane skeleton in rat Sertoli cells.

Analogues of the alpha, beta and gamma subunits of human spectrin and erythroid protein 4.1 have been detected in rat Sertoli cell primary cultures. Immunofluorescence of permeabilized cells showed that erythroid type spectrin, protein 4.1 and actin co-distribute within the cells as filamentous structures. Fodrin-like molecules were distributed in a diffuse manner, mostly associated with the plasma membrane. Immunoprecipitation and immunoblotting experiments indicated that the polypeptides present in rat Sertoli cells are immunologically related and display molecular weights similar to their analogues in the human erythroid and non-erythroid membrane skeleton.

Actins↗
PubMed1983

Changes of Sertoli cell glycoproteins induced by removal of the associated germ cells.

Sertoli cell glycoproteins were studied in culture where these cells were in contact with germ cells (Sertoli cell enriched cultures, SCEC) and in pure Sertoli cell cultures. Sertoli cell only cultures (SCOC) were prepared by a short treatment of SCEC with hypotonic solution or by culturing seminiferous epithelium fragments from prenatally irradiated rats. After metabolic labeling with [3H]fucose. [14C]N-acetylglucosamine or [3H]leucine, SCEC and SCOC particulate fractions (105 000 g pellet) were analyzed by one-dimensional slab gel electrophoresis and fluorography. The comparison of the electrophoretic patterns obtained, demonstrated that a glycoprotein of MW 48 000, undetectable in SCEC, was present in SCOC after labelling with both sugar precursors. The MW 48 000 glycoprotein was also present in the electrophoretic profile of particulate fraction from [3H]fucos-labelled Sertoli cell cultures from prenatally irradiated rat. Such difference was not observed after labelling with [3H]leucine; in this experimental condition a MW 48 000 band was present in the electrophoretic profile of polypeptides from SCEC as well from SCOC. The synthesis of this glycoprotein represented a specific and stable cell response, since it occurred only a few hours after germ cell removal, and it was still detectable 3 days later. FSH stimulation did not influence the synthesis of the MW 48 000 glycoprotein, whereas it increased the synthesis of high MW glycoproteins. The hypothesis is discussed that the appearance of a new glycoprotein when Sertoli cells have lost their contact with germ cells could represent a product of glycosylation of preexisting molecules and their possible location in the Sertoli cell membrane. The results presented here provide additional evidence that Sertoli cell functions may be dependent on the association with the germ cell.

Animals↗
PubMed1983

Intercellular communication in rat seminiferous tubules.

Intercellular electrical coupling in seminiferous tubules from prepubescent and adult Wistar rats has been studied by using conventional techniques. It is found that cells in the seminiferous epithelium are electrically coupled. Experiments performed using "Sertoli cell-enriched" seminiferous tubules indicate the existence of intercellular ionic communication between Sertoli cells. Junctional conductance is independent of the direction of electrical field and it is affected by A23187 Ca ionophore (5 microM) but not by exposure to the neurotransmitter norepinephrine (1-5 X 10(-5) M). Intracellular resistivity (including junctional resistance) is higher in mature as compared to immature germinal epithelium. These findings suggest that cell metabolites or second messenger molecules could be transferred via the low-resistance pathways between epithelium cells to coordinate cellular activity.

Aging↗
PubMed1983

Murine Sertoli cells: major histocompatibility antigens and glycoconjugates.

Sertoli cells, cultured from testes of 2-3-week-old Balb/c mice, contain tripartite nucleoli, exhibit phagocytic function, and have the typical morphologic appearance of Sertoli cells by light microscopy, transmission and scanning electron microscopy. Fluorescence-activated cell sorter analysis indicated the presence on mouse. Sertoli cells of H-2 but not Ia antigens. Alpha-D-mannose and N-acetyl-D-glucosamine determinants are detected on Sertoli cell surface by inhibition of lectin binding using appropriate sugars. Interaction of Sertoli cells with concanavalin A (Con A) or wheatgerm agglutinin (WGA) results in rapid patching of the labeled lectin, which become internalized as perinuclear vesicles. These changes are accompanied by rounding of the Sertoli cell, mimicking cellular changes known to occur when fat Sertoli cells are stimulated in vitro by FSH or cyclic AMP. Thus, Sertoli cells have surface alloantigens that permit them to serve as target to cytotoxic T lymphocytes, but not as antigen presenting cells.

Animals↗
PubMed1980

Surface interaction in vitro between Sertoli cells and germ cells at different stages of spermatogenesis.

The presence of surface-recognition mechanisms between somatic and germ cells of the seminiferous epithelium has been studied in the rat by an assay in vitro based on the ability of homogeneous populations of spermatogenic cells, at specific differentiative stages, to adhere to monolayers of cultured Sertoli cells. The results show that germ cells adhere specifically to Sertoli cells and that the adhesion is dependent on the differentiative stage of the germ cells. Pachytene spermatocytes show the highest ability to adhere and form typical junctional specializations with the underlying Sertoli cells, while round spermatids adhere much less to the substrate. The possible regulative role of a somatic cell-germ interaction is discussed.

Animals↗
PubMed1979

Morphological characteristics of male germ cells of rats in contact with Sertoli cells in vitro.

Fragments of seminiferous epithelium were prepared from 3-week-old rats. Although the Sertoli cells formed a monolayer, germ cells (spermatogonia and early spermatocytes) remained in association with them and were of normal ultrastructural appearance. Germ cells became completely separated from Sertoli cells after 3 weeks of culture in a chemically defined medium. The contact areas between Sertoli and germ cells were characterized by desmosome-like junctions while those between germ cells appeared to be pentalaminar.

Animals↗
PubMed1978

The distribution of spectrin along the membranes of normal and echinocytic human erythrocytes.

Spectrin molecules are distributed uniformly throughout the submembranous regions of intact human erythrocytes. Spectrin does not appear to extend into the red blood cell cytoplasm to any significant extent. Thus, it does not form a recognizable internal scaffolding nor does it seem to connect distant segments of the cell membrane. Spectrin retains its submembranous location in the spiny processes of echinocytes produced by ATP depletion. Thus, these processes do not seem to form by a simple extrusion mechanism powered by contraction of the spectrin network. Spectrin seems to be important for the stability of the lipid bilayer of the red cell membrane, and it probably also plays a role in regulating red cell shape. How it performs either function is still unknown.

Antibodies↗
PubMedDate not supplied

Control and impairment of immune privilege in the testis and in semen.

It has long been known that the testis is an immunologically privileged site in the body, and that human seminal plasma possesses a generalized immunosuppressive activity. Multiple factors participate in the establishment of immunotolerance in the testis: the blood-tubular barrier; the local production of immunosuppressive molecules by Sertoli cells; and the Fas system as regulator of immunological homeostasis in both physiological and pathological conditions. Cytokine-induced up-regulation of Fas as well as of integrin ligands, which are known to be specific binding molecules for lymphocytes on the Sertoli cell surface, indicates that the 'nursing' cells of seminiferous epithelium might be important in the impairment of immune privilege, causing autoimmune orchitis. In addition, the soluble form of Fas-ligand protein present in the seminal plasma of infertile patients might suggest a role for this immunomodulatory protein in male infertility. Finally, an understanding of the mechanisms underlying immune privilege in the testis and in semen might help to clarify how cells expressing 'non-self' antigens (such as male gametes) can escape the immune system in both the male and female genital tracts.

Female↗