Artículos de revistas
Imatinib Restores Vasp Activity And Its Interaction With Zyxin In Bcr-abl Leukemic Cells
Registro en:
Biochimica Et Biophysica Acta - Molecular Cell Research. Elsevier, v. 1853, n. 2, p. 388 - 395, 2015.
1674889
10.1016/j.bbamcr.2014.11.008
2-s2.0-84914133165
Autor
Bernusso V.A.
Machado-Neto J.A.
Pericole F.V.
Vieira K.P.
Duarte A.S.S.
Traina F.
Hansen M.D.
Olalla Saad S.T.
Barcellos K.S.A.
Institución
Resumen
Vasodilator-stimulated phosphoprotein (VASP) and Zyxin are interacting proteins involved in cellular adhesion and motility. PKA phosphorylates VASP at serine 157, regulating VASP cellular functions. VASP interacts with ABL and is a substrate of the BCR-ABL oncoprotein. The presence of BCR-ABL protein drives oncogenesis in patients with chronic myeloid leukemia (CML) due to a constitutive activation of tyrosine kinase activity. However, the function of VASP and Zyxin in BCR-ABL pathway and the role of VASP in CML cells remain unknown. In vitro experiments using K562 cells showed the involvement of VASP in BCR-ABL signaling. VASP and Zyxin inhibition decreased the expression of anti-apoptotic proteins, BCL2 and BCL-XL. Imatinib induced an increase in phosphorylation at Ser157 of VASP and decreased VASP and BCR-ABL interaction. VASP did not interact with Zyxin in K562 cells; however, after Imatinib treatment, this interaction was restored. 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