Protein secretory patterns of rat Sertoli and peritubular cells are influenced by culture conditions (original) (raw)
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Culture patterns and sorting of rat Sertoli cell secretory proteins
Journal of cell science, 1988
A cocultivation chamber and two types of permeable substrates have been used to study: (1) the culture patterns of rat Sertoli and peritubular cells, and Sertoli cells cocultured with spermatogenic cells or peritubular cells; and (2) the polarized secretion of Sertoli cell-specific proteins transferrin, S70 and S45-S35 heterodimeric protein. Substrates included a nylon mesh (with openings of 100 micron) coated with extracellular matrix (ECM) material and an uncoated microporous filter (with pores of 0.45 micron). Sertoli cells cultured on ECM-coated nylon mesh organized a continuous sheet of multilayered epithelial cells essentially devoid of spermatogenic cells while peritubular cells formed a layer of squamous cells. Sertoli cells cultured on uncoated microporous substrate formed a continuous sheet of cuboidal epithelial cells with numerous basal cytoplasmic processes projecting into the substrate and abundant apically located spermatogenic cells, while peritubular cells organized...
Effects of serum components on the morphology of sertoli cells in culture
The Anatomical Record, 1980
Studies of Sertoli cell structure, maturation, and function have been aided by the use of in vitro systems. Although numerous papers have appeared that utilize the Sertoli cell culture model, few papers have dealt with the characterization of these cells under various culture environments. Recently, i t has been reported that the addition of serum to the culture medium prevents induction of long cytoplasmic appendages in cultured Sertoli cells that have been treated with FSH, TSH, or cAMP. The purpose of this investigation was to determine which serum components, obtained by gel filtration, are capable of inhibiting the morphological response induced by FSH, TSH, or cAMP. Sertoli cell-enriched cultures were prepared using collagenase and trypsin digestion, each followed by gravity sedimentation. Untreated cells grown on plastic or glass substrates assumed a n epithelioid appearance after several days. Cells treated with FSH, TSH, or cAMP formed long cytoplasmic appendages after 1-2 days. This response was prevented or reversed by the addition of fetal calf serum (lo%), crystallized bovine serum albumin (0.25%-2%), or purified albumin obtained by gel filtration of whole serum (0.25%). I t was also found that fractions t h a t elute between the void volume and the initial albumin fractions (molecular weights of approximately 50,000 and greater) mimic the hormone-induced response after only 1 G 1 2 hours. The results of this investigation indicate that albumin is the primary serum component responsible for inhibiting morphological alterations induced by FSH, TSH, and cAMP. Furthermore, i t is apparent t h a t the production of long filamentous cytoplasmic appendages in Sertoli cells can be induced by a wide variety of substances.
Annals of the New York Academy of Sciences, 1982
In the testis of the sexually mature animal, Sertoli cells maintain structural and functional relationships with germinal cells. Sertoli cells are nonproliferative in the mature animal and maintain a transient association with germinal cells. It is believed that biological signals generated by the functionally cycling Sertoli cells 1. ' ? enable the spermatogenic process to reach completion. However, the functional nature of the Sertoli cell-germinal cell relationship is poorly understood. Therefore, it seems relevant to increase our understanding of Sertoli cell physiology as a step towards the study of germinal cell differentiation into spermatozoa. A convenient approach for the assessment of Sertoli cell function is the use of a cell culture system in which physiological activities can be correlated with events occurring in the seminiferous epithelium. Using primary cultures of rat Sertoli cells, it was shown that F S H rcgulates the synthesis and secretion of androgen-binding protein (ABP) ; '
Proceedings of the National Academy of Sciences, 1982
The accumulation of two polypeptides, SCml and SCm2, in the medium of Sertoli cell cultures is enhanced by follicle-stimulating hormone (FSH) but is unaffected by either the cAMP analog, N6,0-dibutyryl cAMP or luteinizing hormone. The assigned molecular weights of SCm1 and SCm2 differ from those of androgen-binding protein subunits or any other previously identified Sertoli cell secretory product. Incubation of Sertoli cell cultures with either FSH or N6,02'-dibutyryl cAMP also stimulates the incorporation of [rS]methionine into two intracellular polypeptides, SCc1 and SCc2. In addition, the phosphorylation of three intracellular polypeptides, SCc3, SCc4, and SCc5, is intensified when Sertoli cell cultures are treated with either FSH or N6,02'-dibutyryl cAMP. Based on these results and on previous work, we conclude that (i) SCmI and SCm2 may, like androgen-binding protein, be secreted by Sertoli cells and function extracellularly while SCcI and SCc2 are involved in FSH-dependent intracellular activity; (ii) SCc3, SCc4, and SCc5 are possible substrates for FSH-stimulated, cAMP-dependent protein kdnase activity; and (iii) SCc5 is an isoelectric variant of vimentintype intermediate filament protein presumably involved in FSHand N6,02'-dibutyryl cAMP-induced Sertoli cell shape changes.
Proteins of the membrane skeleton in rat Sertoli cells
Journal of Cell Science
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.