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Myosin caldesmon interactions

Sobue, K., Morimoto, K., Inui, M., Kanda, K. and Kakiuchi, S. (1982). Control of actin-myosin interaction of gjzzard smooth muscle by calmodulin- and caldesmon-linked flip-flop mechanism. Biomed. Res. 3, 188-196. [Pg.185]

Apart from the phosphorylation theory, other regulatory mechanisms have also been suggested for smooth muscle contraction. A thin-filament protein that has been proposed as a regulatory component is caldesmon [102], Purified caldesmon is a potent inhibitor of actin-tropomyosin interaction with myosin. The mechanisms by which calcium removes this inhibition are controversial. Furthermore, phosphorylation of caldesmon by a caldesmon kinase in vitro has also been implicated in this... [Pg.82]

The basis of the proposed regulatory function of caldesmon is its ability to inhibit the interaction of myosin with the thin filament. A prerequisite for this is that CD binds to actin. In the native thin filament, TM is also present, and it is found that the presence of TM has effects on CD binding to actin and a very pro-... [Pg.79]

Caldesmon binds to smooth muscle myosin in vitro. The interaction is very dependent on the ionic strength, reaching >10 at ionic strengths below... [Pg.86]

To account for activation of arterial smooth muscle independently of LC20 phosphorylation, attention has been focused on the possible roles of the thin filament-associated regulatory proteins, caldesmon and calponin. Both proteins have been localized in the actomyosin domain of the smooth muscle cell and both have been shown to inhibit actin-activated myosin ATPase by interacting with F-actin, tropomyosin, and/or myosin (Clark et al., 1986 Takahashi et al.,... [Pg.162]

Marston SB, Fraser ID, Huber PA (1994) Smooth muscle caldesmon controls the strong binding interaction between actin-tropomyosin and myosin. J Biol Chem 269 3210432109... [Pg.54]

Tanaka T, Ohta H, Kanda K, Tanaka T, Hidaka H, Sobue K (1990) Phosphorylation of high-Mr caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction betvreen actin and myosin. Eur J Biochem 188 495-500 Tanner JA, Haeberle JR, Meiss RA (1988) Regulation of glycerinated smooth muscle contraction and relaxation by myosin phosphorylation. Am J Physiol 255 C34-C42 Tansey MG, Hori M, Karaki K, Kamm KE, Stull JT (1990) Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscle. FEBS Lett 270 219-221... [Pg.143]

SM) a-actin, myosin heavy chain and caldesmon. In attempts to engineer blood vessels using bioreactor systems, interactions between ECs and SMCs (e.g., EC adhesion to and lining of the inner lumen in contact with cultured SMCs) have improved by subjecting the system to proper mechanical stim-uh. In addition, cyclic strain has been shown to induce stem cell differentiation in SMCs (Park, 2007). [Pg.103]


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See also in sourсe #XX -- [ Pg.87 ]




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