By Ivar Giaever, Charles R. Keese (auth.), Wen G. Jiang (eds.)
Cell dependent impedance sensing is turning into a brand new biophysical and mobile expertise in phone dependent analyses. The expertise has been utilized in research of mobile development and demise, cellphone adhesion and migration, mobilephone invasion and cell-cell interactions, telephone toxicity, angiogenesis, telephone permeability, sign transduction and mobile behaviour below circulation stipulations. it's a probe unfastened, hugely delicate, and flexible expertise platform. fresh improvement within the know-how has additionally allowed excessive throughput, automatic analyses. it's been extensively explored in chemistry, toxicity, mobile biology, melanoma biology, and different parts of chemistry, medicinal chemistry, existence and clinical technology. Written by way of specialists within the sector of telephone impedance sensing, together with the Nobel Laureate Dr Ivar Giaever, this books covers the historical past of electrical cell-substrate impedance sensing, their purposes in phone dependent investigations, rather within the sector of melanoma biology. This e-book is the 1st in this know-how platform and may be a hugely beneficial reference for molecular and cellphone biologists, melanoma biologists, chemists and biochemists, scientific researchers who paintings within the components of mobile biology, molecular biology, toxicology, pharmaceutical undefined, lifestyles technology and scientific research.
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Extra info for Electric Cell-Substrate Impedance Sensing and Cancer Metastasis
Modification of the cytoplasmic domain of the integrin pair by intracellular signaling proteins, such as phosphorylation, lipid binding, or protein-protein interactions, can lead to altered integrin affinity with the extracellular ligand resulting in modulated cellular functions, including adhesion, migration, proliferation, aggregation, apoptosis, and cell cycle progression. As described above, the integrin-mediated cell-ECM interactions are established via the aggregation of a number of proteins.
Other investigators have demonstrated a role for paxillin in regulating focal adhesion turnover. Paxillin phosphorylated on residues Y31 and Y118 can compete with the p190RhoGAP/ p120RasGAP complex for p120RasGAP, resulting in the release of p190RhoGAP to act on and inhibit RhoA (Tsubouchi et al. 2002). Also, paxillin binding with Crk results in Rac1 activation (Lamorte et al. 2003; Valles et al. 2004). Furthermore, phorbol ester activation of PKC has been shown to block paxillin Y31 and Y118 phosphorylation (Schmidt and Hall 2002).
J Cereb Blood Flow Metab 27:123–134 Klinger JR et al (2007) Rottlerin causes pulmonary edema in vivo: a possible role for PKCd. J Appl Physiol 103:2084–2094 Kosaka Y, Ogita K, Ase K, Nomura H, Kikkawa U, Nishizuka Y (1988) The heterogeneity of protein kinase C in various rat tissues. Biochem Biophys Res Commun 151:973–981 Lamark T et al (2003) Interaction codes within the family of mammalian phox and Bem1p domaincontaining proteins. J Biol Chem 278:34568–34581 Lamorte L, Rodrigues S, Sangwan V, Turner CE, Park M (2003) Crk associates with a multimolecular paxillin/GIT2/b-PIX complex and promotes Rac-dependent relocalization of paxillin to focal contacts.