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Cytoskeletal alterations

Delon J, Bercovici N, Liblau R, Trautmann A. Imaging antigen recognition by naive CD4+ T cells compulsory cytoskeletal alterations for the triggering of an intracellular calcium response. Eur J Immunol 1998 28(2) 716-729. [Pg.288]

Bellomo G, Mirabelli F, Salis A, Vairetti M, Richelmi P, Finardi G, Thor H. Orrenius S. Oxidative stress-induced plasma membrane blebbing and cytoskeletal alterations in normal and cancer cells. Ann NY Acad Sci 1988 551 128-130. [Pg.153]

Tau pathology corresponds to the intraneuronal aggregation of microtubule-associated tau proteins into abnormal filaments. Paired hehcal filaments (PHF) are the most characteristic cytoskeletal alterations affecting numerous neurons in AD. Using a combined immunocytochemical and biochemical approach (Iqbal et al., 1989) demonshated for the first time that the microtubule-associated protein tau, a normal brain cytoskeletal protein, is a component of the PHF. The authors also indicated for the first time that posttranslational modification of tau such as phosphorylation might occur which would allow it to assemble either alone or together... [Pg.650]

The biochemical changes associated with adhesion have been the subject of several recent reviews (Baruch, 1999 Baruch et al., 2002 Cooke et al., 2001, 2004b, 2005 Sherman et al., 2003). Included have been discussions of cytoskeletal alterations, modifications of intrinsic membrane proteins of the red cell such as band 3, exposure of phosphatidyl-serine (PS), parasite-encoded proteins exported into the red cell cytosol and associated with the cytoskeleton (i.e. KAHRP, P. falciparum erythrocyte surface protein-3 (PfEMP3), MESA, and those exposed on the surface, i.e. PfEMPl, sub-telomeric variant open reading frame (STEVOR) and repetitive interspersed family of genes (RIFINS) involved in re-modelling of the infected erythrocyte). [Pg.191]

Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations. The Journal of Biological Chemistry, 278, 45082—45093. [Pg.565]

Mirabelli, F., Salis, A., Vairetti, M., Bellomo, G., Thor, H. and Orrenius, S. (1989) Cytoskeletal alterations in human platelets exposed to oxidative stress are mediated by oxidative and calcium-dependent mechanisms. Arch. Biochem. Biophys. 270 478-488. [Pg.497]

Verdugo-Gazdik ME, Simic D, Opsahl AC, Tengowski MW (2006) Investigating cytoskeletal alterations as a potential marker of retinal and lens drug-related toxicity. Assay and Drug Development Technologies 4 695-707. [Pg.213]

Fentie, I. H., and Roisen, F. J., 1993, The effects of cytoskeletal altering agents on the surface topography of GMl in Neuro2a neuroblastoma cell membranes, J. Neurochem. 22 498-506. [Pg.231]

Antibiotics alter the normal colonic flora, leading to loss of colonization resistance, which is the ability of the normal flora to protect against overgrowth of pathogens, especially when the anaerobic flora are depleted [15], In CDAD, the altered colonization resistance can allow for the overgrowth of C. difficile in the colon. The bacteria produces two toxins which cause disease (toxin A, an enterotoxin, and toxin B, a cytotoxin). The toxins of C. difficile inactivate Rho proteins, which results in the loss of cytoskeletal integrity in enterocytes. Cellular damage results in fluid loss, exudation and diarrhea. The most severe form of C. difficile diarrhea is pseudomembranous colitis, which can cause severe colitis, toxic colon and rarely colon perforation and death. [Pg.82]

DeCaprio AP, O Neill EA. 1985. Alterations in rat axonal cytoskeletal proteins induced by in vitro and in vivo 2,5-hexanedione exposure. Toxicol Appl Pharmacol 78 235-247. [Pg.232]

Banan A, Zhang LJ, Shaikh M, Fields JZ, Farhadi A, and Keshavarzian A [2004] Theta-isoform of PKC is required for alterations in cytoskeletal dynamics and barrier permeability in intestinal epithelium a novel function for PKC-theta. Am J Physiol 287 C218-C234... [Pg.365]

Only a very small reduction in the number of acid-insoluble SH-groups in platelets was seen in the presence of feverfew extract [52]. A change in the high molecular weight protein pattern was only seen after the platelets had been activated. Such changes are indicative of polymerization of the proteins and the formation of S-S bridges and this can lead to disturbances in membrane-cytoskeletal interactions. Uptake of [ " C]arachidonic acid into phospholipids was inhibited by feverfew [53], which may be a result of altered cytoskeletal-membrane interaction. [Pg.232]


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