Prolonged ethanol ingestion decreases alpha-mannosidase activity and induces its redistribution to the fluid phase in rat cauda epididymis

The role of glycosidases in mammalian epididymal fluid is still a controvertial subject. There exists a body of evidence in favour of a function in remodeling the sperm surface as one step in gamete maturation, whilst others argue in favor of an extraepididymal role for these enzymes. In this study...

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Detalles Bibliográficos
Autores: Arco, M., Sartor, Tirso, Cabrera Kreiker, Ricardo Jorge, Sosa Escudero, Miguel Angel
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2003
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/128668
Acceso en línea:http://hdl.handle.net/11336/128668
Access Level:acceso abierto
Palabra clave:Glycosidases
alpha-mannosidase
epididymis
alcoholism
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Descripción
Sumario:The role of glycosidases in mammalian epididymal fluid is still a controvertial subject. There exists a body of evidence in favour of a function in remodeling the sperm surface as one step in gamete maturation, whilst others argue in favor of an extraepididymal role for these enzymes. In this study we measured the activity and distribution of four glycosidases in rat cauda epididymis after prolonged ethanol ingestion, a condition associated with fertility disturbances. We found that alpha-mannosidase is the most sensitive enzyme to the stress caused by alcohol, since its activity in epididymis significantly decreased and partly redistributed from the spermatozoa to the fluid phase. From these results we suggested that alcohol treatment affects the expression of the enzyme and possibly induces a loss of interaction with the affinity sites on the sperm surface. Although other enzymes also underwent changes due to the alcohol treatment, we focussed on the importance of alpha-mannosidase in the fertilizing capability of spermatozoa.