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Beschreibung

Caldesmon is a protein component of the thin filaments of smooth muscle myofibrils. It is also localized in the stress fibers of fibroblasts. Caldesmon was identified as a Ca2+/Calmodulin-binding protein with molecular weight of 120-150kDa (H-Caldesmon) and 70-80kDa (L-Caldesmon). H-Caldesmon is the primary isoform in smooth muscle while L-Caldesmon is most abundant in non-muscle cells. Caldesmon is capable of binding two calmodulin molecules, one at either end of the protein. Additionally, Caldesmon is an actin, myosin, and tropomyosin-binding protein. Human L-Caldesmon is a protein of 538 amino acids with mobility of 80kDa. In vitro, L-Caldesmon inhibits the actomyosin ATPase in an F-Actin-dependent manner. L-Caldesmon may play an important function in motile processes such as secretion and organelle movement.