Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.

Malpighian tubules (MTs) are highly specific organs of arthropods (Insecta, Myriapoda and Arachnida) for excretion and osmoregulation. In order to highlight the important genes and pathways involved in multi-functions of MTs, we performed a systematic proteomic analysis of silkworm MTs in the presen...

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Autores principales: Xiao-wu Zhong, Yong Zou, Shi-ping Liu, Qi-ying Yi, Cui-mei Hu, Chen Wang, Qing-you Xia, Ping Zhao
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Publicado: Public Library of Science (PLoS) 2013
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Acceso en línea:https://doaj.org/article/198d4efd345a412c9e6fc67a15cf14a0
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spelling oai:doaj.org-article:198d4efd345a412c9e6fc67a15cf14a02021-11-18T08:53:12ZProteomic-based insight into Malpighian tubules of silkworm Bombyx mori.1932-620310.1371/journal.pone.0075731https://doaj.org/article/198d4efd345a412c9e6fc67a15cf14a02013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098719/?tool=EBIhttps://doaj.org/toc/1932-6203Malpighian tubules (MTs) are highly specific organs of arthropods (Insecta, Myriapoda and Arachnida) for excretion and osmoregulation. In order to highlight the important genes and pathways involved in multi-functions of MTs, we performed a systematic proteomic analysis of silkworm MTs in the present work. Totally, 1,367 proteins were identified by one-dimensional gel electrophoresis coupled with liquid chromatography-tandem mass spectrometry, and as well as by Trans Proteomic Pipeline (TPP) and Absolute protein expression (APEX) analyses. Forty-one proteins were further identified by two-dimensional gel electrophoresis. Some proteins were revealed to be significantly associated with various metabolic processes, organic solute transport, detoxification and innate immunity. Our results might lay a good foundation for future functional studies of MTs in silkworm and other lepidoptera.Xiao-wu ZhongYong ZouShi-ping LiuQi-ying YiCui-mei HuChen WangQing-you XiaPing ZhaoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e75731 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Xiao-wu Zhong
Yong Zou
Shi-ping Liu
Qi-ying Yi
Cui-mei Hu
Chen Wang
Qing-you Xia
Ping Zhao
Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
description Malpighian tubules (MTs) are highly specific organs of arthropods (Insecta, Myriapoda and Arachnida) for excretion and osmoregulation. In order to highlight the important genes and pathways involved in multi-functions of MTs, we performed a systematic proteomic analysis of silkworm MTs in the present work. Totally, 1,367 proteins were identified by one-dimensional gel electrophoresis coupled with liquid chromatography-tandem mass spectrometry, and as well as by Trans Proteomic Pipeline (TPP) and Absolute protein expression (APEX) analyses. Forty-one proteins were further identified by two-dimensional gel electrophoresis. Some proteins were revealed to be significantly associated with various metabolic processes, organic solute transport, detoxification and innate immunity. Our results might lay a good foundation for future functional studies of MTs in silkworm and other lepidoptera.
format article
author Xiao-wu Zhong
Yong Zou
Shi-ping Liu
Qi-ying Yi
Cui-mei Hu
Chen Wang
Qing-you Xia
Ping Zhao
author_facet Xiao-wu Zhong
Yong Zou
Shi-ping Liu
Qi-ying Yi
Cui-mei Hu
Chen Wang
Qing-you Xia
Ping Zhao
author_sort Xiao-wu Zhong
title Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
title_short Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
title_full Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
title_fullStr Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
title_full_unstemmed Proteomic-based insight into Malpighian tubules of silkworm Bombyx mori.
title_sort proteomic-based insight into malpighian tubules of silkworm bombyx mori.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/198d4efd345a412c9e6fc67a15cf14a0
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