Clearly, the structural links between actin filaments and integrins are regulated in at least some cell types, and it would not be unreasonable to hypothesize that agents known to alter cell behavior may do so by affecting the expression or function of actin binding proteins such as vinculin, talin, paxillin and integrins that are recruited to focal adhesions (Mwakikunga et al., 2011).
Actin binding protein expression is altered in uterine luminal epithelium by clomiphene citrate, a synthetic estrogen receptor modulator.
In motile cells, actin dynamics are activated by extracellular stimuli, which in turn trigger intracellular signaling, including Rhofamily small GTPases, focal adhesion kinases, cofilin, LIM kinases, capping proteins, polymerization complexes, and other
actin binding proteins (ABPs) [18, 19].
54),55) These conformational changes are mediated along the actin filament, especially in the presence of the
actin binding proteins tropomyosin and troponin.
Increased glucose levels are known to stimulate a variety of responses within GMC including remodeling of cytoskeletal elements like actin and
actin binding proteins [24].
Actin-based movements and remodeling are sensitive to [Ca.sup.2+] changes which are affecting a plethora of
actin binding proteins. Fine astrocytic processes contain mostly actin cytoskeleton, and the actin-binding protein alpha-actinin aggregates at the tip of growing filopodia in cultured astrocytes [22].