Does phosphorylation of cofilin affect the progression of human bladder cancer?

<p>Abstract</p> <p>Background</p> <p>We determined the differently expressed protein profiles and their functions in bladder cancer tissues with the aim of identifying possible target proteins and underlying molecular mechanisms for taking part in their progression.<...

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Main Authors: Chung Hong, Kim Bokyung, Jung Seung-Hyo, Won Kyung-Jong, Jiang Xiaowen, Lee Chang-Kwon, Lim So, Yang Sang-Kuk, Song Ki, Kim Hong
Format: Article
Language:English
Published: BMC 2013-02-01
Series:BMC Cancer
Subjects:
Online Access:http://www.biomedcentral.com/1471-2407/13/45
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spelling doaj-28f89b52e7564b9582263b18ed9ac3542020-11-24T21:45:12ZengBMCBMC Cancer1471-24072013-02-011314510.1186/1471-2407-13-45Does phosphorylation of cofilin affect the progression of human bladder cancer?Chung HongKim BokyungJung Seung-HyoWon Kyung-JongJiang XiaowenLee Chang-KwonLim SoYang Sang-KukSong KiKim Hong<p>Abstract</p> <p>Background</p> <p>We determined the differently expressed protein profiles and their functions in bladder cancer tissues with the aim of identifying possible target proteins and underlying molecular mechanisms for taking part in their progression.</p> <p>Methods</p> <p>We examined the expression of proteins by proteomic analysis and western blot in normal urothelium, non-muscle-invasive bladder cancers (NMIBCs), and muscle-invasive bladder cancers (MIBCs). The function of cofilin was analyzed using T24 human bladder cancer cells.</p> <p>Results</p> <p>The expression levels of 12 proteins were altered between bladder cancers and normal bladder tissues. Of these proteins, 14-3-3σ was upregulated in both NMIBCs and MIBCs compared with controls. On the other hand, myosin regulatory light chain 2, galectin<b>-</b>1<b>,</b> lipid-binding AI, annexin V, transthyretin, CARD-inhibitor of NF-κB-activating ligand, and actin prepeptide were downregulated in cancer samples. Cofilin, an actin-depolymerizing factor, was prominent in both NMIBCs and MIBCs compared with normal bladder tissues. Furthermore, we confirmed that cofilin phosphorylation was more prominent in MIBCs than in NMIBCs using immunoblotting and immunohistochemcal analyses. Epidermal growth factor (EGF) increased the phosphorylation of cofilin and elevated the migration in T24 cells. Knockdown of cofilin expression with small interfering RNA attenuated the T24 cell migration in response to EGF.</p> <p>Conclusions</p> <p>These results demonstrate that the increased expression and phosphorylation of cofilin might play a role in the occurrence and invasiveness of bladder cancer. We suspected that changes in cofilin expression may participate in the progression of the bladder cancer.</p> http://www.biomedcentral.com/1471-2407/13/45CofilinPhosphorylationInvasionUrothelial cell carcinoma
collection DOAJ
language English
format Article
sources DOAJ
author Chung Hong
Kim Bokyung
Jung Seung-Hyo
Won Kyung-Jong
Jiang Xiaowen
Lee Chang-Kwon
Lim So
Yang Sang-Kuk
Song Ki
Kim Hong
spellingShingle Chung Hong
Kim Bokyung
Jung Seung-Hyo
Won Kyung-Jong
Jiang Xiaowen
Lee Chang-Kwon
Lim So
Yang Sang-Kuk
Song Ki
Kim Hong
Does phosphorylation of cofilin affect the progression of human bladder cancer?
BMC Cancer
Cofilin
Phosphorylation
Invasion
Urothelial cell carcinoma
author_facet Chung Hong
Kim Bokyung
Jung Seung-Hyo
Won Kyung-Jong
Jiang Xiaowen
Lee Chang-Kwon
Lim So
Yang Sang-Kuk
Song Ki
Kim Hong
author_sort Chung Hong
title Does phosphorylation of cofilin affect the progression of human bladder cancer?
title_short Does phosphorylation of cofilin affect the progression of human bladder cancer?
title_full Does phosphorylation of cofilin affect the progression of human bladder cancer?
title_fullStr Does phosphorylation of cofilin affect the progression of human bladder cancer?
title_full_unstemmed Does phosphorylation of cofilin affect the progression of human bladder cancer?
title_sort does phosphorylation of cofilin affect the progression of human bladder cancer?
publisher BMC
series BMC Cancer
issn 1471-2407
publishDate 2013-02-01
description <p>Abstract</p> <p>Background</p> <p>We determined the differently expressed protein profiles and their functions in bladder cancer tissues with the aim of identifying possible target proteins and underlying molecular mechanisms for taking part in their progression.</p> <p>Methods</p> <p>We examined the expression of proteins by proteomic analysis and western blot in normal urothelium, non-muscle-invasive bladder cancers (NMIBCs), and muscle-invasive bladder cancers (MIBCs). The function of cofilin was analyzed using T24 human bladder cancer cells.</p> <p>Results</p> <p>The expression levels of 12 proteins were altered between bladder cancers and normal bladder tissues. Of these proteins, 14-3-3σ was upregulated in both NMIBCs and MIBCs compared with controls. On the other hand, myosin regulatory light chain 2, galectin<b>-</b>1<b>,</b> lipid-binding AI, annexin V, transthyretin, CARD-inhibitor of NF-κB-activating ligand, and actin prepeptide were downregulated in cancer samples. Cofilin, an actin-depolymerizing factor, was prominent in both NMIBCs and MIBCs compared with normal bladder tissues. Furthermore, we confirmed that cofilin phosphorylation was more prominent in MIBCs than in NMIBCs using immunoblotting and immunohistochemcal analyses. Epidermal growth factor (EGF) increased the phosphorylation of cofilin and elevated the migration in T24 cells. Knockdown of cofilin expression with small interfering RNA attenuated the T24 cell migration in response to EGF.</p> <p>Conclusions</p> <p>These results demonstrate that the increased expression and phosphorylation of cofilin might play a role in the occurrence and invasiveness of bladder cancer. We suspected that changes in cofilin expression may participate in the progression of the bladder cancer.</p>
topic Cofilin
Phosphorylation
Invasion
Urothelial cell carcinoma
url http://www.biomedcentral.com/1471-2407/13/45
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