Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1983410 | The International Journal of Biochemistry & Cell Biology | 2016 | 14 Pages |
Abstract
Lysyl oxidase-like 2 (LOXL2) is a member of the lysyl oxidase family, which plays an important role in extracellular matrix protein biosynthesis and tumor progression. In the present study, we identified a novel splice variant, LOXL2Î72, which encodes a peptide having the same N- and C-termini as wild-type LOXL2 (LOXL2WT), but lacks 72 nucleotides encoding 24 amino acids. LOXL2Î72 had dramatically reduced enzymatic activity, and was no longer secreted. However, LOXL2Î72 promoted greater cell migration and invasion than LOXL2WT. Furthermore, a dual luciferase reporter assay indicated that LOXL2Î72 activates distinct signal transduction pathways compared to LOXL2WT, consistent with cDNA microarray data showing different expression levels of cell migration- and invasion-related genes induced following over-expression of each LOXL2 isoform. In particular, LOXL2Î72 distinctly promoted esophageal squamous cell carcinoma (ESCC) cell migration via up-regulating the C-C motif chemokine ligand 28 (CCL28). Our results suggest that the new LOXL2 splice variant contributes to tumor progression by novel molecular mechanisms different from LOXL2WT.
Keywords
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Authors
Hai-Ying Zou, Guo-Qing Lv, Li-Hua Dai, Xiu-Hui Zhan, Ji-Wei Jiao, Lian-Di Liao, Tai-Mei Zhou, Chun-Quan Li, Bing-Li Wu, Li-Yan Xu, En-Min Li,