Endogenous testicular D-aspartic acid regulates gonadal aromatase activity in boar.
J Endocrinol Invest
; 29(2): 141-6, 2006 Feb.
Article
en En
| MEDLINE
| ID: mdl-16610240
ABSTRACT
D-aspartic acid (D-Asp), aromatase enzyme activity and the putative D-Asp involvement on aromatase induction have been studied in the testis of mature boars. The peroxidase-antiperoxidase and the indirect immunofluorescence methods, applied to cryostat and paraffin sections, were used to evaluate D-Asp and aromatase distributions. D-Asp level was dosed by an enzymatic method performed on boar testis extracts. Biochemical aromatase activity was determined by in vitro experiments carried out on testis extracts. D-Asp immunoreactivity was found in Leydig cells, and, to a lesser extent, in germ cells. Analogously, aromatase immunoreactivity was present in Leydig cells, but absent from seminiferous tubule elements. In vitro experiments showed that the addition of D-Asp to testicular tissue acetone powder induced a significant increase of aromatase activity, as assessed by testosterone conversion to 17beta-estradiol. Enzyme Km was not affected by D-Asp (about 25 nM in control and D-Asp added tests). These findings suggest that D-Asp could be involved in the local regulation of aromatase in boar Leydig cells and intervenes in this organ's production of estrogens.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Testículo
/
Aromatasa
/
Ácido D-Aspártico
Tipo de estudio:
Diagnostic_studies
Límite:
Animals
Idioma:
En
Revista:
J Endocrinol Invest
Año:
2006
Tipo del documento:
Article
País de afiliación:
Italia