Biochemical and Biophysical Research Communications
Regular ArticleInduction of Tyrosine Phosphorylation and Translocation of Ezrin by Hepatocyte Growth Factor/Scatter Factor (HGF/SF)
References (0)
Cited by (54)
Ezrin immunoexpression in gastric cells of domestic cats infected with Helicobacter spp
2023, Research in Veterinary ScienceCitation Excerpt :Ezrin, a member of the ezrin-radixin-moesin (ERM) protein family is a membrane cytoskeletal crosslinker protein, which plays a key role to regulate several cytoskeletal-related functions, including cell adhesion, cell survival and cell motility (Fan et al., 2011). It is known to be involved in stimulation-dependent processes of membrane remodelling in epithelial cells (Hanzel et al., 1991; Jiang et al., 1995). In stomach it is highly concentrated on the apical surfaces of parietal cells and predominantly expressed on the apical and basolateral canalicular membranes, where it contributes to acid secretion (Yao et al., 1996; Yoshida et al., 2016).
Apigenin 7-O-glucoside promotes cell apoptosis through the PTEN/PI3K/AKT pathway and inhibits cell migration in cervical cancer HeLa cells
2020, Food and Chemical ToxicologyCitation Excerpt :The ability of cancer cells to invade and metastasize is the most difficult stage in the treatment of cervical cancer. Metastatic cells must first detach from neighboring cells, then use matrix metalloproteinases (MMPs) to enter the blood or lymphatic vessels through the extracellular matrix and capsule, and finally migrate through the blood to distant places (Brooks, 1996; Folkman, 1996; Jiang et al., 1995; Zhang et al., 2007). Migration is a key process for cancer cell invasion and metastasis (Kim et al., 2011).
Effect of matrine on HeLa cell adhesion and migration
2007, European Journal of PharmacologyHepatocyte growth factor, its receptor, and their potential value in cancer therapies
2005, Critical Reviews in Oncology/HematologyModulation of ezrin and E-cadherin expression by IL-1β and TGF-β1 in human trophoblasts
2004, Journal of Reproductive ImmunologyIdentification and Relevance of the CD95-binding Domain in the N-terminal Region of Ezrin
2004, Journal of Biological ChemistryCitation Excerpt :By analogy with other ERM-binding membrane proteins, the two-hybrid system was performed using either the ezrin or the radixin FERM domain and the whole CD95 cytoplasmic domain. Particularly, the ezrin N-terminal 392 aa, including the FERM domain and both tyrosine phosphorylation sites (i.e. Tyr145 and Tyr353) (39) or the whole radixin FERM domain (known to lack Tyr353), were fused to the GAL4 transcriptional activation domain of the pVP16-AD, and the CD95 cytoplasmic domain (aa 185–335) was fused to the GAL4 DNA binding domain of the pM GAL4-BD cloning vector (Fig. 1, B and C). pG5CAT containing the CAT gene was used as reporter plasmid.