Laminin-5 β3A expression in LNCaP human prostate carcinoma cells increases cell migration and tumorigenicity

被引:31
作者
Calaluce, R
Bearss, DJ
Barrera, J
Zhao, Y
Han, HY
Beck, SK
McDaniel, K
Nagle, RB
机构
[1] Univ Arizona, Arizona Canc Ctr, Ctr Hlth Sci, Dept Pathol, Tucson, AZ USA
[2] Univ Arizona, Hlth Sci Ctr, Dept Pathol, Tucson, AZ USA
[3] Univ Arizona, Hlth Sci Ctr, Dept Mol & Cell Biol, Tucson, AZ USA
[4] Univ Arizona, Hlth Sci Ctr, Dept Cell Biol & Anat, Tucson, AZ USA
来源
NEOPLASIA | 2004年 / 6卷 / 05期
关键词
laminin-5; beta; 3A; prostate carcinoma cells; LNCaP; cell migration; tumorgenicity;
D O I
10.1593/neo.03499
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Interactions between extracellular matrix proteins and prostate carcinoma cells change dramatically during prostate tumor progression. We have concentrated on two key modifications that occur in the hemidesmosome in prostate carcinoma: loss of laminin-5 protein expression and altered basal cell polarity of the alpha6beta4 integrin. We previously demonstrated two cell line-specific isoforms (beta3A and beta3B) of the LAMB3 message. Cells expressing only the beta3B isoform did not translate the beta3 protein and were unable to assemble the laminin-5 trimer. One such cell line, LNCaP, was selected to determine whether restoration of the laminin-5 beta3A isoform would cause expression of a functional laminin-5 beta3 chain, assembly and secretion of the laminin-5 trimer, and reversion to a non-neoplastic phenotype. Laminin-5 beta3A cDNA was cloned and stably transfected into LNCaP cells. We observed the restoration of the beta3 protein, but a laminin-5 trimer was not secreted. Moreover, increased cell migration was demonstrated, and tumorigenicity was increased in SCID mice. A microarray analysis, performed between transfected and nontransfected LNCaP cells, showed most changing genes to be associated with signal transduction. The beta3 chain of laminin-5 may thus play an important role in signal transduction, which may enhance cell motility and tumorigenesis.
引用
收藏
页码:468 / 479
页数:12
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