Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/119158
Título: Does oligosaccharide-phosphatidylinositol (glycosyl-phosphatidylinositol) hydrolysis mediate prolactin signal transduction in granulosa cells?
Autores/as: Fanjul Rodríguez, Luisa Fernanda 
Marrero Arencibia, María Isabel 
González, Juan
Quintana, José
Santana Delgado, María Del Pino 
Estévez Rosas, Francisco Jesús 
Mato, José María
Ruiz De Galarreta Hernandez,C. Manuel 
Clasificación UNESCO: 32 Ciencias médicas
2302 Bioquímica
320502 Endocrinología
Palabras clave: Granulosa cell
Protein-kinase-a
Hormone
Fecha de publicación: 1993
Publicación seriada: European journal of biochemistry (Print) 
Resumen: Initial biosynthetic radiolabelling experiments with cultured granulosa cells revealed the presence of an oligosaccharide-phosphatidylinositol (glycoyl-phosphatidylinositol; (Ose)nPtdIns) structurally related to (Ose)nPtdIns-lipids isolated from other cell types. Prolactin (PRL) stimulated [3H]glucosamine-(Ose)nPtdIns turnover and the rapid generation of [3H]myristoyl-diacylglycerol in cultured follicle-stimulating hormone-(FSH)-primed granulosa cells endowed with PRL receptors. In parallel experiments performed with [3H]myo-inositol-labelled granulosa cells, treatment with PRL stimulated (Ose)nPtdIns hydrolysis in a similar manner, whereas no effect on phosphoinositide (PtdIns, PtdInsP and PtdInsP2) turnover could be observed. These results strongly suggest that the cleavage of (Ose)nPtdIns by phosphodiesterase followed by the subsequent generation of diacylglycerol and a soluble phosphoinositol-oligosaccharide (inositol-phosphoglycan; (Ose)nInsP) moiety could be part of the signal-transduction mechanism linking PRL receptors to their biological effects in granulosa cells. To test this hypothesis, we examined the effect of PRL and purified (Ose)nInsP moiety (from rat liver membranes) on granulos cell 3β-hydroxysteroid dehydrogenase/Δ5–4 isomerase (3β-HSD) enzyme activity. Results presented show that, in FSH-primed granulosa cells, PRL (40 nM) and (Ose)nInsP (5 μM) prevented gonadotropin-stimulated 3β-HSD activity. Further-more, in undifterentiated granulosa cells where PRL receptors are absent, no effect of the hormone on 3β-HSD activity could be observed, whereas, (Ose)nInsP (1–10 μM) inhibited enzyme activity in a dose-dependent manner.
URI: http://hdl.handle.net/10553/119158
ISSN: 0014-2956 (Print)
DOI: 10.1111/j.1432-1033.1993.tb18194.x
Fuente: European journal of biochemistry [ISSN 0014-2956], v. 216 (3), p. 747-755 (Septiembre 1993)
Colección:Artículos
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