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약학대학
약학과
Journal papers
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Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis
Title
Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis
Authors
Kim H.J.
;
Kim Y.M.
;
Lim S.
;
Nam Y.K.
;
Jeong J.
;
Kim H.-J.
;
Lee K.-J.
Ewha Authors
이공주
;
김희정
;
김현정
SCOPUS Author ID
이공주
; 김희정
Issue Date
2009
Journal Title
Oncogene
ISSN
0950-9232
Citation
Oncogene vol. 28, no. 1, pp. 117 - 127
Indexed
SCI; SCIE; SCOPUS
Document Type
Article
Abstract
Ubiquitin C-terminal hydrolase-L1 (UCH-L1) catalyses the hydrolysis of ubiquitin ester and amide mainly in neuronal cells. Recently it was proposed as a marker with a potential role in carcinogenesis. However, the molecular mechanism underlying the biological function of UCH-L1 in tumor cells is poorly understood. We found that UCH-L1 is highly expressed in non-small lung cancer cell line H157, having high invasive potential, and that the expression of UCH-L1 in tumor cells enhances their invasive potential in vitro and in vivo. UCH-L1 changes cell morphology by regulating cell adhesion through Akt-mediated pathway. Suppressing UCH-L1 expression by RNAi significantly suppressed the invasion in vitro and in vivo, and the activation of Akt and downstream mitogen activated protein kinases c-Jun N-terminal kinases and p38, but not ERK. In Akt-negative mutants, overexpression of UCH-L1 does not affect the invasion and migration capability of H157 cells. These results suggest that UCH-L1 is a key molecule to regulate tumor-cell invasion by upstream activation of Akt. © 2009 Macmillan Publishers Limited All rights reserved.
DOI
10.1038/onc.2008.364
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