Lysophosphatidic acid modulates the association of PTP1B with N-cadherin/catenin complex in SKOV3 ovarian cancer cells

Cell Biology International
Ruby Yun-Ju HuangJiahn-Chun Wu

Abstract

LPA (lysophosphatidic acid) is a natural phospholipid that plays important roles in promoting cancer cell proliferation, invasion and metastases. We previously reported that LPA induces ovarian cancer cell dispersal and disruption of AJ (adherens junction) through the activation of SFK (Src family kinases). In this study, we have investigated the regulatory mechanisms during the early phase of LPA-induced cell dispersal. An in vitro model of the ovarian cancer cell line SKOV3 for cell dispersal was used. LPA induces rapid AJ disruption by increasing the internalization of N-cadherin-β-catenin. By using immunoprecipitations, LPA was shown to induce increased tyrosine phosphorylation of β-catenin and alter the balance of β-catenin-bound SFK and PTP1B (phosphotyrosine phosphatase 1B). The altered balance of tyrosine kinase/phosphatase correlated with a concomitant disintegration of the β-catenin-α-catenin, but not the β-catenin-N-cadherin complex. This disintegration of β-catenin from α-catenin and the cell dispersal caused by LPA can be rescued by blocking SFK activity with the chemical inhibitor, PP2. More importantly, PP2 also restores the level of PTP1B bound to β-catenin. We propose that LPA signalling alters AJ stability by ...Continue Reading

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Citations

Jan 1, 2013·American Journal of Physiology. Lung Cellular and Molecular Physiology·Sergejs BerdnikovsJoan M Cook-Mills
Jul 9, 2014·The Journal of Cell Biology·Sei KuriyamaRoberto Mayor
Apr 12, 2017·Current Rheumatology Reports·Cristiano Sacchetti, Nunzio Bottini
Oct 8, 2020·Cytopathology : Official Journal of the British Society for Clinical Cytology·Ben DavidsonDag Andre Nymoen

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