Fiber stress

The protective film is broken in certain places on the lithium surface by the stress. Fiber-like lithium grows, like an extrusion of lithium, through these broken holes in the film. If the deposition current is small enough and the stress is therefore small, the protective film will probably not break. In this case, the deposited lithium may be particle-like or amorphous. 

Stress fibers are parallel bundles of actin filaments that develop in the cytoplasm of fibroblasts from the cortical actin network in response to mechanical tension. These often bind to the plasma membrane at focal contacts and, through transmembrane linker glycoproteins, to the extracellular matrix. Thus, actin filaments of stress fibers indirectly Join to the inner face of the plasma membrane through molecular assemblies of attachment proteins, which include an actin-capping protein, a-actinin, vinculin, and talin (Small, 1988). 

Fibronectin receptor is a two-chain glycoprotein of the integrin family that serves as a transmembrane linker by binding to talin on the cytoplasmic side and to fibronectin on the external side of the membrane. The pull exerted by stress fibers on attached structures may be produced by bipolar assemblies of nonmuscle myosin molecules producing a sliding of actin filaments of opposite polarity. 

The cytoskeleton enables cultured fibroblasts to respond to the physical characteristics of a solid surface by the formation of adhesion plaques and stress fibers (Burridge et al., 1988). 

It is most unlikely that the sole functions of mysoin-Il in nonmuscle cells are to provide the contractile force to bisect cells during cytokinesis and for the contractility of stress fibers. Myosin-II is present in a variety of cell types at moderate concentrations in tissues such as brain, which are almost totally non-mitotic and do... 

Ridley, A.J., Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70,389-399. 

However, 2 also affected the regulation of actin stress fiber formation [19]. Rho proteins are involved in the regulation of various cytoskeletal structures, and RhoB is believed to be one of the prime targets of FTase inhibitors. Rho B is apparently both geranylgeranylated and farnesylated [20, 21]. If cells were treated with 2, vesicular localization of Rho B was inhibited. Thus 2 may also inhibit the farnesylation of Rho B, thereby interfering with actin stress fiber formation [22]. 

Any of the cytoskeletal proteins that cross-link cytoskel-etal filaments into colinear arrays, such as the action of a-actinin in promoting the formation of actin stress fibers. Bundling proteins typically contain pairs of binding sites for attachment to cytoskeletal filaments. 

FIGURE 1-9 The three types of cytoskeletal filaments. The upper panels show epithelial cells photographed after treatment with antibodies that bind to and specifically stain (a) actin filaments bundled together to form "stress fibers," (b) microtubules radiating from the cell center, and (c) intermediate filaments extending throughout the cytoplasm. For these experiments, antibodies that specifically recognize actin, tubu-... 

Diviani, D., Soderling, J., and Scott, J. D. (2001). AKAP-Lbc anchors protein kinase A and nucleates G alpha 12-selective Rho-mediated stress fiber formation. J. Biol. Chem. 276, 44247-44257. 

Seifert, G. J., Lawson, D., and Wiche, G. (1992). Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell Biol. 59, 138-147. 

Arora, P.D., P.A. Janmey, and C.A. McCulloch. 1999. A role for gelsolin in stress fiber-dependent cell... 

In addition to Ras, a number of other proteins are known to be substrates for FTase (many of unknown identity or function, determined by 2-D gel shift experiments in the presence and absence of FTI) these may also play a part in determining relative susceptibility to FTase inhibition.46 In particular, RhoB, a farnesylated protein involved with the formation of actin stress fibers and cytoskeletal organization, has been implicated in the growth-inhibitory consequences of FTase inhibition.47,48 Another study using the FTI 19 found that growth inhibition in soft agar of a panel of human tumor cell lines correlated with the mutational status of the H-and N-Ras proteins, but not with K-Ras mutations.49 In this study also, cells with genetic defects in addition to ras were sensitive to FTase inhibition. 

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