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Differential Distribution and Activity Profile of Acylpeptide Hydrolase in the Rat Seminiferous Epithelium.
Covarrubias, Alejandra A; De la Fuente-Ortega, Erwin; Rossi, Gabriela; Cocca, Ennio; Rossi, Mosè; Palmieri, Gianna; Pancetti, Floria C.
Afiliação
  • Covarrubias AA; Laboratorio de Neurotoxicología Ambiental, Departamento de Ciencias Biomédicas, Facultad de Medicina, Universidad Católica del Norte, Coquimbo 1781421, Chile.
  • De la Fuente-Ortega E; Departamento de Ciencias Biomédicas, Facultad de Medicina, Universidad Católica del Norte, Coquimbo 1781421, Chile.
  • Rossi G; Laboratorio de Neurotoxicología Ambiental, Departamento de Ciencias Biomédicas, Facultad de Medicina, Universidad Católica del Norte, Coquimbo 1781421, Chile.
  • Cocca E; Institute of Biosciences and Bioresources, National Research Council (CNR-IBBR), 80131 Naples, Italy.
  • Rossi M; Institute of Biosciences and Bioresources, National Research Council (CNR-IBBR), 80131 Naples, Italy.
  • Palmieri G; Institute of Biosciences and Bioresources, National Research Council (CNR-IBBR), 80131 Naples, Italy.
  • Pancetti FC; Laboratorio de Neurotoxicología Ambiental, Departamento de Ciencias Biomédicas, Facultad de Medicina, Universidad Católica del Norte, Coquimbo 1781421, Chile.
Biomedicines ; 10(7)2022 Jul 04.
Article em En | MEDLINE | ID: mdl-35884896
Acylpeptide hydrolase (APEH) is a serine protease involved in amino acid recycling from acylated peptides (exopeptidase activity) and degradation of oxidized proteins (endoproteinase activity). This enzyme is inhibited by dichlorvos (DDVP), an organophosphate compound used as an insecticide. The role of APEH in spermatogenesis has not been established; therefore, the aim of this study was to characterize the distribution and activity profile of APEH during this process. For this purpose, cryosections of male reproductive tissues (testis and epididymis) and isolated cells (Sertoli cells, germ cells, and spermatozoa) were obtained from adult rats in order to analyze the intracellular localization of APEH by indirect immunofluorescence. In addition, the catalytic activity profiles of APEH in the different male reproductive tissues and isolated cells were quantified. Our results show that APEH is homogeneously distributed in Sertoli cells and early germ cells (spermatocytes and round spermatids), but this pattern changes during spermiogenesis. Specifically, in elongated spermatids and spermatozoa, APEH was localized in the acrosome and the principal piece. The exopeptidase activity was higher in the germ cell pool, compared to sperm and Sertoli cells, while the endoproteinase activity in epididymal homogenates was higher compared to testis homogenates at 24 h of incubation. In isolated cells, this activity was increased in Sertoli and germ cell pools, compared to spermatozoa. Taken together, these results indicate that APEH is differentially distributed in the testicular epithelium and undergoes re-localization during spermiogenesis. A possible role of APEH as a component of a protection system against oxidative stress and during sperm capacitation is discussed.
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Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Biomedicines Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Chile

Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Biomedicines Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Chile