Activation of extracellular signal-related kinases 1 and 2 in Sertoli cells in experimentally cryptorchid rhesus monkeys / 亚洲男科学杂志(英文版)
Asian Journal of Andrology
;
(6): 265-272, 2006.
Artigo
em Inglês
| WPRIM
| ID: wpr-253848
ABSTRACT
<p><b>AIM</b>To assess the spatiotemporal changes in the expression of extracellular signal-regulated kinases 1 and 2 (ERK1/2), c-Jun N-terminal kinases (JNK) and p38 mitogen-activated protein kinases (MAPK) in response to heat stress in the cryptorchid testis, and to investigate a possible relation to Sertoli cell dedifferentiation.</p><p><b>METHODS</b>Immunohistochemistry and western blot were used to examine the expression and activation of ERK1/2, p38 and JNK in the cryptorchid testis at various stages after experimental cryptorchidism.</p><p><b>RESULTS</b>The abdominal temperature did not obviously change the total ERK1/2 expression but significantly activated phospho-ERK1/2 in the Sertoli cells of the cryptorchid testis. Heat stress increased total JNK expression in the Sertoli cells of the cryptorchid testis but did not activate phospho-JNK. Neither total p38 nor phospho-p38 was induced by heat stress in the Sertoli cells of the cryptorchid testis. Changes in the spatiotemporal expression of cytokeratin 18 (CK18), a marker of immature or undifferentiated Sertoli cells, were induced in the cryptorchid testis in a pattern similar to the activation of ERK1/2.</p><p><b>CONCLUSION</b>The activation of ERK1/2 in the testis may be related to dedifferentiation of Sertoli cells under heat stress induced by experimental cryptorchidism.</p>
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Patologia
/
Escroto
/
Imuno-Histoquímica
/
Proteína Quinase 1 Ativada por Mitógeno
/
Criptorquidismo
/
MAP Quinase Quinase 4
/
Proteína Quinase 3 Ativada por Mitógeno
/
Proteínas Quinases p38 Ativadas por Mitógeno
/
Modelos Animais de Doenças
/
Ativação Enzimática
Limite:
Animais
Idioma:
Inglês
Revista:
Asian Journal of Andrology
Ano de publicação:
2006
Tipo de documento:
Artigo
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