IMBICE   05372
INSTITUTO MULTIDISCIPLINARIO DE BIOLOGIA CELULAR
Unidad Ejecutora - UE
artículos
Título:
Hormonal regulation of pituitary FSH sialylation in male rats.
Autor/es:
AMBAO V; RULLI S; CARINO MH; CONSOLE G; ULLOA-AGUIRRE A; CALANDRA RS; CAMPO S
Revista:
MOLECULAR AND CELLULAR ENDOCRINOLOGY.
Editorial:
Elsevier
Referencias:
Lugar: Holanda; Año: 2009 vol. 309 p. 39 - 47
ISSN:
0303-7207
Resumen:
Sialic acid content in FSH is modulated by GnRH and sexual steroids. Gal1,3GlcNAc2,3-sialyltransferase
(ST3Gal III) and Gal1,4GlcNAc2,6-sialyltransferase (ST6Gal I) incorporate sialic acid residues into FSH
oligosaccharides. The aim of the present studywas to assess pituitary FSH molecular microheterogeneity
and ST3Gal III/ST6Gal I expression during sexual development and after castration in male rats. Preparative
isoelectric focusing and lectin chromatography were used to isolate FSH glycosylation variants
according to charge and complexity of their oligosaccharides; RT-PCR and immunohistochemistry were
employed to analyse sialyltransferase expression. Sexual development was associated with a progressive
shift towardsmore acidic/sialylated FSH glycoforms concomitantly with an increment in ST6Gal I gene and
protein expression. After castration, a transient decrease followed by a marked increase in ST6Gal I expressionwere
observed. Less acidic/sialylated FSH glycoforms bearing incomplete oligosaccharides increased
after castration, despite high ST6Gal I expression. ST3Gal III expression remained unchanged in all the
experimental conditions examined. These results show that the synthesis of FSH isoforms possessing2,3-sialyltransferase
(ST3Gal III) and Gal1,4GlcNAc2,6-sialyltransferase (ST6Gal I) incorporate sialic acid residues into FSH
oligosaccharides. The aim of the present studywas to assess pituitary FSH molecular microheterogeneity
and ST3Gal III/ST6Gal I expression during sexual development and after castration in male rats. Preparative
isoelectric focusing and lectin chromatography were used to isolate FSH glycosylation variants
according to charge and complexity of their oligosaccharides; RT-PCR and immunohistochemistry were
employed to analyse sialyltransferase expression. Sexual development was associated with a progressive
shift towardsmore acidic/sialylated FSH glycoforms concomitantly with an increment in ST6Gal I gene and
protein expression. After castration, a transient decrease followed by a marked increase in ST6Gal I expressionwere
observed. Less acidic/sialylated FSH glycoforms bearing incomplete oligosaccharides increased
after castration, despite high ST6Gal I expression. ST3Gal III expression remained unchanged in all the
experimental conditions examined. These results show that the synthesis of FSH isoforms possessing2,6-sialyltransferase (ST6Gal I) incorporate sialic acid residues into FSH
oligosaccharides. The aim of the present studywas to assess pituitary FSH molecular microheterogeneity
and ST3Gal III/ST6Gal I expression during sexual development and after castration in male rats. Preparative
isoelectric focusing and lectin chromatography were used to isolate FSH glycosylation variants
according to charge and complexity of their oligosaccharides; RT-PCR and immunohistochemistry were
employed to analyse sialyltransferase expression. Sexual development was associated with a progressive
shift towardsmore acidic/sialylated FSH glycoforms concomitantly with an increment in ST6Gal I gene and
protein expression. After castration, a transient decrease followed by a marked increase in ST6Gal I expressionwere
observed. Less acidic/sialylated FSH glycoforms bearing incomplete oligosaccharides increased
after castration, despite high ST6Gal I expression. ST3Gal III expression remained unchanged in all the
experimental conditions examined. These results show that the synthesis of FSH isoforms possessing
2,6-linked sialic acid is hormonally regulated in male rats.
2,6-linked sialic acid is hormonally regulated in male rats.