Myosin light chain kinase colocalizes with nonmuscle myosin IIB in myofibril precursors and sarcomeric Z-lines of cardiomyocytes.

Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility involving actin and myosin II. MLCK is widely present in vertebrate tissues including the myocardium. However, the role of MLCK in cardiomyocyte function is not known.

[Phenotypes of smooth muscle cells in carotid arteries in Takayasu's disease].

The phenotype of smooth-muscle cells (SMC) of carotid arteries in health and Takayasu's disease were studied using immunofluorescence. In contrast to unaffected carotid artery, medial SMC were represented by heterogenic cell population. Many SMC in this disease expressed fibronectin with ED-A sequence, contained cytokeratin 8 and were deprived of h-caldesmon.

Alterations in myocardial ultrastructure and protein expression after a single injection of isoproterenol.

Immunochemical and electron microscopic characterization of rat myocardium was conducted 2 h and 3 weeks after a single injection of isoproterenol in rats. The relative content of several myospecific proteins (KRP--kinase-related protein, desmin), cytoskeletal proteins (tubulin, vinculin, myosin light chain kinase--MLCK) and extracellular matrix protein fibronectin was determined by immunoblotting. Two hours after injection of 50 mg/kg isoproterenol a destruction of some cardiomyocytes, contracture of myofibrils and mild edema of intercellular space was observed.

Alterations in myocardial cytoskeletal and regulatory protein expression following a single Doxorubicin injection.

Immunochemical and ultrastructural studies of the rat heart after a single injection of doxorubicin (2.2 or 0.44 mg/kg) were performed.

[Effect of adriamycin on expression and content of myocardial structural and regulatory proteins].

The biochemical and morphological study of the cytoskeleton and extracellular matrix of rat heart was carried out after single injection of adriamycin (2.2 or 0.44 mg/kg).