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Caveolin‐1 up‐regulates integrin α2,6‐sialylation to promote integrin α5β1‐dependent hepatocarcinoma cell adhesion
Author(s) -
Yu Shengjin,
Fan Jianhui,
Liu Linhua,
Zhang Lijun,
Wang Shujing,
Zhang Jianing
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.002
Subject(s) - integrin , fibronectin , cell adhesion , neural cell adhesion molecule , microbiology and biotechnology , chemistry , focal adhesion , cell adhesion molecule , sialic acid , integrin linked kinase , adhesion , cell , biology , biochemistry , cell cycle , cyclin dependent kinase 2 , organic chemistry
The alterations of integrin glycosylation play a crucial role in tumor metastasis. Our previous studies indicated that caveolin‐1 promoted the expression of the key α2,6‐sialytransferase ST6Gal‐I and fibronectin‐mediated adhesion of mouse hepatocarcinoma cell. Herein, we investigated the role of α2,6‐sialylated α5‐integrin in the adhesion of mouse hepatocarcinoma H22 cell. We demonstrated that caveolin‐1 up‐regulated cell surface α2,6‐linked sialic acid via stimulating ST6Gal‐I transcription. Cell surface α2,6‐sialylation was required for integrin α5β1‐dependent cell adhesion to fibronectin, and an increase in α2,6‐linked sialic acid on α5‐subunit facilitated fibronectin‐mediated focal adhesion kinase phosphorylations, suggesting that α2,6‐sialylated α5‐subunit promoted integrin α5β1‐dependent cell adhesion.