Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid

SUMMARY: Tyrosine phosphorylated proteins have been localized and identified in male reproductive tissues such as testis and capacitated/ acrosome reacted sperm except epididymis. The changes of such proteins are associated with decreased sperm quality of valproic acid treatment. This study aimed to...

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Autores principales: Sawatpanich,Tarinee, Arun,Supatcharee, Tongpan,Saranya, Chaichun,Amnart, Sampannang,Apichakarn, Sukhorum,Wannisa, Maneenin,Chanwit, Burawat,Jaturon, Iamsaard,Sitthichai
Lenguaje:English
Publicado: Sociedad Chilena de Anatomía 2018
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Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022018000300835
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spelling oai:scielo:S0717-950220180003008352019-09-16Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic AcidSawatpanich,TarineeArun,SupatchareeTongpan,SaranyaChaichun,AmnartSampannang,ApichakarnSukhorum,WannisaManeenin,ChanwitBurawat,JaturonIamsaard,Sitthichai Localization Beta actin Tyrosine phosphorylated proteins Epididymal fluid Rats SUMMARY: Tyrosine phosphorylated proteins have been localized and identified in male reproductive tissues such as testis and capacitated/ acrosome reacted sperm except epididymis. The changes of such proteins are associated with decreased sperm quality of valproic acid treatment. This study aimed to investigate the presence and alterations of protein phosphorylation in epididymal epithelium and fluid of rats treated VPA. Sixteen adult male rats were divided into control and VPA-treated groups (n=8/ each). Treated rats were injected with VPA (500 mg/ kgBW, intraperitoneally) for 10 consecutive days. At the end of experiment, the monoclonal antiphosphotyrosine (clone 4G10) was used for immunohistochemistry to probe tyrosine phosphorylated proteins and also to examine the expression of such proteins using immuno-Western blotting in epididymal tissue and fluid. The result showed that positive reactivity of phosphorylated proteins was clearly observed in cytoplasmic principle cells, nuclei of apical & basal cells and sperm mass surrounded with epididymal fluids. The profiles of phosphorylated proteins in epididymal fluid were 182, 127, 80, 70, 57, 45, 34, and 31 kDas, respectively. Interestingly, VPA affected the changes of phosphorylated proteins and β actin in head, body, and tail epididymal fluids. We conclude that tyrosine phosphorylated proteins were detected in epididymal epithelium and fluid. The expressions of those proteins and actin were altered under VPA treating.info:eu-repo/semantics/openAccessSociedad Chilena de AnatomíaInternational Journal of Morphology v.36 n.3 20182018-09-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022018000300835en10.4067/S0717-95022018000300835
institution Scielo Chile
collection Scielo Chile
language English
topic Localization
Beta actin
Tyrosine phosphorylated proteins
Epididymal fluid
Rats
spellingShingle Localization
Beta actin
Tyrosine phosphorylated proteins
Epididymal fluid
Rats
Sawatpanich,Tarinee
Arun,Supatcharee
Tongpan,Saranya
Chaichun,Amnart
Sampannang,Apichakarn
Sukhorum,Wannisa
Maneenin,Chanwit
Burawat,Jaturon
Iamsaard,Sitthichai
Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
description SUMMARY: Tyrosine phosphorylated proteins have been localized and identified in male reproductive tissues such as testis and capacitated/ acrosome reacted sperm except epididymis. The changes of such proteins are associated with decreased sperm quality of valproic acid treatment. This study aimed to investigate the presence and alterations of protein phosphorylation in epididymal epithelium and fluid of rats treated VPA. Sixteen adult male rats were divided into control and VPA-treated groups (n=8/ each). Treated rats were injected with VPA (500 mg/ kgBW, intraperitoneally) for 10 consecutive days. At the end of experiment, the monoclonal antiphosphotyrosine (clone 4G10) was used for immunohistochemistry to probe tyrosine phosphorylated proteins and also to examine the expression of such proteins using immuno-Western blotting in epididymal tissue and fluid. The result showed that positive reactivity of phosphorylated proteins was clearly observed in cytoplasmic principle cells, nuclei of apical & basal cells and sperm mass surrounded with epididymal fluids. The profiles of phosphorylated proteins in epididymal fluid were 182, 127, 80, 70, 57, 45, 34, and 31 kDas, respectively. Interestingly, VPA affected the changes of phosphorylated proteins and β actin in head, body, and tail epididymal fluids. We conclude that tyrosine phosphorylated proteins were detected in epididymal epithelium and fluid. The expressions of those proteins and actin were altered under VPA treating.
author Sawatpanich,Tarinee
Arun,Supatcharee
Tongpan,Saranya
Chaichun,Amnart
Sampannang,Apichakarn
Sukhorum,Wannisa
Maneenin,Chanwit
Burawat,Jaturon
Iamsaard,Sitthichai
author_facet Sawatpanich,Tarinee
Arun,Supatcharee
Tongpan,Saranya
Chaichun,Amnart
Sampannang,Apichakarn
Sukhorum,Wannisa
Maneenin,Chanwit
Burawat,Jaturon
Iamsaard,Sitthichai
author_sort Sawatpanich,Tarinee
title Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
title_short Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
title_full Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
title_fullStr Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
title_full_unstemmed Localization and Changes of Tyrosine Phosphorylated Proteins and ß Actin in Epididymis of Rats Treated with Valproic Acid
title_sort localization and changes of tyrosine phosphorylated proteins and ß actin in epididymis of rats treated with valproic acid
publisher Sociedad Chilena de Anatomía
publishDate 2018
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022018000300835
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