Integrin Expression in Tumor Progression — Role of Signaling Mechanisms
Róza Ádány in Tumor Matrix Biology, 2017
The integrin αIIbβ3, the principal matrix receptor of platelets, is a predominant matrix receptor in some rodent and human tumor cells.34,35,70,71 In these cells, αIIbβ3 was localized to focal adhesion sites36,37,70 and was found to be associated with vinculin.37 In B16a melanoma cells an intracellular pool of αIIbβ3 exists from which integrin molecules translocate to the cell surface.36 It was demonstrated that the intracellular translocation of this integrin to the plasma membrane and its upregulation at the cell surface is modulated by a 12-LOX metabolite of arachidonic acid, i.e., 12-(S)-HETE.30,36 The 12-(S)-HETE-action on integrin upregulation appears to be dependent upon both microfilament and intermediate filament integrity.36
Phosphoinositide Metabolism
Enrique Pimentel in Handbook of Growth Factors, 2017
Some cytoskeletal proteins may be substrates for protein kinase C-induced phosphorylation. One of these substrates is vinculin,257 a cytoskeletal protein that is phosphorylated in response to Ca2+ and phorbol esters in intact cells.258 The microtubule-associated protein 2 (MAP-2) is a substrate for protein kinase C.259 Protein kinase C phosphorylates MAP-2 exclusively on serine residues which inhibits its ability to cross-link actin filaments. Other cytoskeletal proteins, including tubulin, are poor substrates for protein kinase C. Neomycin, a drug that has a high affinity for phosphoinositides and interferes in vivo with phosphatidylinositol turnover, inhibits the polymerization of actin induced by thrombin or ADP in platelets.260 Phosphatidylinositol turnover may have a role in the control of microfilament-based cell motility.
The Rous Sarcoma Virus Oncogene and its Proto-Oncogene Counterpart
Pimentel Enrique in Oncogenes, 2020
In addition to 34K, two other cytoplasmic proteins, with mol wt of 50,000-dalton (50K) and 90,000-daltons (90K), also interact with pp60src but their respective functions are also not understood.112,113 Other protein substrates for pp60Art kinase activity may have higher molecular weights and about 30% of phosphotyrosine-containing protein molecules present in RSV-transformed cells have sizes greater than 100,000 daltons.114 A well identifed target, phosphorylated on tyrosine residues by the action of pp60src, is vinculin,115,116 a 130,000-daltons (130K) cytoskeletal protein which is apparently involved in the anchorage of microfilaments to the plasma membrane. However, additional phosphorylation of tyrosine residues in vinculin does not occur upon transformation by some ASV.117 The functional significance of this type of vinculin modification remains undetermined.
In vitro stimulation with radiofrequency currents promotes proliferation and migration in human keratinocytes and fibroblasts
Published in Electromagnetic Biology and Medicine, 2021
María Luisa Hernández-Bule, Elena Toledano-Macías, Aida Naranjo, Marina de Andrés-Zamora, Alejandro Úbeda
Vinculin is a protein involved in cell-to-substrate adhesion and cell migration at the three-dimensional level. This anchorage to the substrate is the supporting point for the elongation, orientation and traction of the cytoskeleton during migration (Thievessen et al. 2015). Vinculin is mainly located in: 1) focal complexes present in the lamellipodia emitted by the cells situated on the migration front, and 2) focal adhesions present in the region of the plasma membrane that contacts with the substrate, connecting integrins with the cytoskeleton and attaching the cell to the substrate. In order to be functionally active, vinculin must be located in cytoplasm regions close to the plasma membrane, although prior to migration, unfastening and degradation of this protein are also necessary for disruption of the cell-to-substrate junction (Goldmann 2016). In keratinocytes, the CRET-induced increase in the expression and translocation of vinculin to the membrane of cells placed on the migration front (Figures 7 and Figures 8) could be expected to promote cell migration. However, the wound assay did not detect increased migration rates in electrically treated keratinocytes.
Serum claudin-5, claudin-11, occludin, vinculin, paxillin, and beta-catenin levels in preschool children with autism spectrum disorder
Published in Nordic Journal of Psychiatry, 2023
Ayhan Bilgiç, Hurşit Ferahkaya, Hülya Karagöz, İbrahim Kılınç, Vesile Meltem Energin
Vinculin and paxillin may be other important molecules for BBB and intestinal barrier functions. Vinculin is a cytoplasmic protein that functions in cell-matrix and cell-cell adhesions and regulation of apoptosis. This molecule also plays a role in the regulation of tight junctions in the intestinal barrier. Like occludin, the research by Vojdani and colleagues found an elevation in antibody production against vinculin in patients with celiac disease and supported its role in intestinal permeability [24]. Paxillin is first defined as a cytoplasmic scaffold/adaptor protein that plays a crucial role in focal adhesion. However, further studies demonstrate that it could also have functions in cell migration, proliferation, and as a regulator of mRNA trafficking and subsequent translation [28]. Therefore, as well as their potential effects on barrier structures, these two molecules contribute to the development of ASD by affecting many developmental and physiological processes.
HER2 signaling regulates the tumor immune microenvironment and trastuzumab efficacy
Published in OncoImmunology, 2019
Tiziana Triulzi, Luca Forte, Viola Regondi, Martina Di Modica, Cristina Ghirelli, Maria Luisa Carcangiu, Lucia Sfondrini, Andrea Balsari, Elda Tagliabue
Protein fractions were extracted from BC cell lines with TNTG lysis buffer as described.37 The following primary antibodies were used: rabbit polyclonal antibodies against phospho-HER2 (Tyr1248, SC12352), HER3 (SC285), ERα (SC543) (Santa Cruz Biotechnology), Akt (#9272) and phospho-Akt (Ser473, #4060), NF-kB (#4764) and phospho-NF-kB (Ser536, #3033), EGFR (#1005), p44/42 MAPK (#9102) and phospho-p44/42 (Thr202/Tyr204, #9101) (Cell Signaling Technology); mouse monoclonal antibodies anti-HER2, clone Ab3 (Calbiochem, OP15); anti-vinculin, clone hVIN-1 (Sigma Aldrich, V9131). Polyclonal anti-rabbit (NA9340V) or anti–mouse (NA931V) IgG horseradish peroxidase (HRP) (Amersham GE Healthcare) was used as a secondary antibody. Protein expression was normalized to that of vinculin.