Alpha-glucosidase in the human epididymis: topographic distribution and clinical application

Pena P; Risopatrón J.; Villegas, J; Miska W.; Schill, WB; Sanchez R.

Abstract

?-Glucosidase activity (EC.3.2.1.20) is present in human seminal plasma, and the neutral form of the enzyme originates almost exclusively from the epididymis. In this study, the specific immunocytochemical location of ?-glucosidase in the human epididymis was evaluated using a polyclonal antibody. Furthermore, a spectrophotometric assay was employed to assess epididymal obstruction in infertile patients. The enzymatic activity of ?-glucosidase free of prostate isoform (AGFPI) was determined spectrophotometrically at 405 nm. According to AGFPI activity, patients with leucocytospermia, oligozoospermia and azoospermia were recorded as having normal values or low values indicating epididymal obstruction. Specific immunochemistry staining was demonstrated in the cytoplasmic cells at the epithelial level, in the transition area and in the efferent ducts. The values of the three groups and the control were as follows (mean ± SEM): normozoospermia (control): 20.2 ± 1.4 mU ml-1; azoospermia: normal value: 17.6 ± 2.2 mU ml-1, low value: 7.4 ± 1.8 mU ml-1; oligozoospermia: normal value: 22.3 ± 2.5 mU ml -1, low value: 7.3 ± 0.7 mU ml-1; leucocytospermia: increase value: 38.9 ± 3.7 mU ml-1, low value: 11.1 ± 1.3 mU ml-1. This study suggests that determination of ?-glucosidase might be helpful to evaluate functions of the epididymis and particularly to exclude epididymal obstruction.

Más información

Título según WOS: Alpha-glucosidase in the human epididymis: topographic distribution and clinical application
Título según SCOPUS: Alpha-glucosidase in the human epididymis: Topographic distribution and clinical application
Título de la Revista: ANDROLOGIA
Volumen: 36
Número: 5
Editorial: Wiley
Fecha de publicación: 2004
Página de inicio: 315
Página final: 320
Idioma: English
URL: http://doi.wiley.com/10.1111/j.1439-0272.2004.00625.x
DOI:

10.1111/j.1439-0272.2004.00625.x

Notas: ISI, SCOPUS - ISI