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Steroid Sulfatase activates the integrin signaling pathway in human cervical cancer cells
Author(s) -
Ye DongJin,
Kwon YeoJung,
Baek HyoungSeok,
Chun YoungJin
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.533.34
Subject(s) - integrin , fibronectin , mapk/erk pathway , phosphorylation , cancer research , signal transduction , microbiology and biotechnology , kinase , chemistry , biology , receptor , biochemistry , extracellular matrix
Steroid sulfatase (STS) is an enzyme responsible for the hydrolysis of aryl and alkyl sulfates. STS plays a crucial function in the production of estrogens and androgens that induce the growth of hormone‐dependent tumors, such as those of breast or prostate cancer. However, the molecular function of STS in tumor growth is still not elucidated clearly. To investigate the function of STS in cancer cell growth, we examined whether STS is able to enhance the integrin signaling pathway. We observed that overexpression of STS in HeLa cells increases the protein and mRNA levels of integrin β1 and fibronectin, a ligand of integrin α5β1. Dehydroepiandrosterone (DHEA), the major metabolites of STS, also increases mRNA and protein expression of integrin β1 and fibronectin. STS overexpression and DHEA treatment induced phosphorylation of focal adhesion kinase (FAK) at the Tyr 925 residue. Furthermore, increased phosphorylation of ERK at Thr 202 and Tyr 204 residues by STS indicates that STS enhances the MAPK/ERK pathway. In conclusion, these results suggest that STS expression and DHEA treatment may enhance MAPK/ERK signaling through up‐regulation of integrin β1 expression and activation of FAK. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .