Idioma:

Identification of a non-mitogenic paracrine factor involved in mesenchymal-epithelial cell interactions between testicular peritubular cells and Sertoli cells

Skinner, Michael K. ; Fritz, Irving B.

Molecular and cellular endocrinology, 1986, Vol.44 (1), p.85-97 [Periódico revisado por pares]

Shannon: Elsevier Ireland Ltd

Texto completo disponível

Citações Citado por

Enviar para

Título:
Identification of a non-mitogenic paracrine factor involved in mesenchymal-epithelial cell interactions between testicular peritubular cells and Sertoli cells
Autor: Skinner, Michael K. ; Fritz, Irving B.
Assuntos: Androgen-Binding Protein - biosynthesis ; Animals ; Biological and medical sciences ; Cell Communication ; Cells, Cultured ; DNA - biosynthesis ; Follicle Stimulating Hormone - pharmacology ; Fundamental and applied biological sciences. Psychology ; Growth Substances - biosynthesis ; Hormone metabolism and regulation ; Insulin - pharmacology ; Male ; Mammalian male genital system ; Molecular Weight ; peritubular cell-produced modulatory protein (P-Mod-S) ; peritubular cell-Sertoli cell interactions ; Plasminogen Activators - biosynthesis ; Rats ; Rats, Inbred Strains ; Seminiferous Epithelium - metabolism ; Sertoli cell secretion of a lactalbumin-like protein ; Sertoli Cells - metabolism ; Testicular Hormones - isolation & purification ; Testicular Hormones - physiology ; Testis - metabolism ; Testis - physiology ; Testosterone - pharmacology ; Transferrin - biosynthesis ; Vertebrates: reproduction ; Vitamin A - pharmacology
É parte de: Molecular and cellular endocrinology, 1986, Vol.44 (1), p.85-97
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Seminiferous peritubular cells have previously been shown to secrete a protein termed P-Mod-S which modulates the functions of Sertoli cells. The present study provides an initial characterization of P-Mod-S and examines the actions of P-Mod-S on Sertoli cells. Gel filtration chromatography demonstrates that P-Mod-S has an apparent molecular weight of 70 000 that could not be dissociated to a lower molecular weight form. A 40- to 90-fold purification of P-Mod-S was obtained with a predicted half maximal effective concentration for Sertoli cells of less than 10 −9 M. Through an analysis of the actions of P-Mod-S on Sertoli cells it is demonstrated that P-Mod-S stimulates the Sertoli cell to a greater extent than any single hormone or vitamin known to influence the cell. P-Mod-S maximally stimulates testicular transferrin and androgen-binding protein production by Sertoli cells, but does not stimulate levels of plasminogen activator activity. P-Mod-S also appears to induce the synthesis of several proteins that are not detected in control non-treated Sertoli cell cultures. One such protein whose synthesis was stimulated by P-Mod-S treatment of Sertoli cells was a component having a molecular mass of 20 kDa. This 20 kDa Sertoli cell-secreted protein was specifically immunoprecipitated with an antibody against an epididymal lactalbumin-like protein. This implies that P-Mod-S can induce Sertoli cells to synthesize and secrete a lactalbumin-like protein. P-Mod-S was found not to contain mitogenic activity. Data presented indicate that testicular peritubular cells synthesize and secrete a 70 kDa non-mitogenic paracrine factor termed P-Mod-S which has a dramatic influence on Sertoli cell functions. Results are discussed with respect to modulation of epithelial (Sertoli) cell functions by components produced by mesenchymal (peritubular) cells.
Editor: Shannon: Elsevier Ireland Ltd
Idioma: Inglês

Links

Voltar para lista de resultados

Anterior Resultado 2 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

Identification of a non-mitogenic paracrine factor involved in mesenchymal-epithelial cell interactions between testicular peritubular cells and Sertoli cells

Skinner, Michael K. ; Fritz, Irving B.

Shannon: Elsevier Ireland Ltd

Buscando em bases de dados remotas. Favor aguardar.