Physical properties of myosin from aortic smooth muscle

Frederiksen, Dixie W.

doi:10.1021/bi00576a003

Cited by 18 publications

(3 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Myosin from atrium and ventricle was prepared essentially according to the methods described by Shiverick (28) and Frederiksen (7). Crude myosin extracts for pyrophosphate gel electrophoresis were prepared by the HOH prescription (12).…”

Section: Myosin Preparationmentioning

confidence: 99%

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

Hoffmann

Siegert

1987

Basic Res Cardiol

View full text Add to dashboard Cite

Two distinct types of native isomyosins, referred to as human fetal HF and human ventricular myosin HV-3, have been identified in the human fetal heart during two different periods of gestation and in the neonatal state, whose relative parts change with development. In the adult ventricle, only HV-3 was found. Two myosin isoforms designated as HA-3 and HA-1 occur in the atrial myocardium of the normal human heart, which are electrophoretically distinct from the fetal isoenzymes. In fetal tissue, the myosin light chain complement is composed of atrial and ventricular light chains. In support of recent results, we also found identical spots from the atrial ALC-1 and the fetal light chain FLC, suggesting a homology between them. Apart from the light chains typical for this tissue, the atrial myocardium also contains ventricular light chains. Therefore we hypothesize that atrial myosin consists of two atrial isoenzymes and presumably of a ventricular type, too. Differences between atrial and ventricular myosin from human hearts were demonstrated by measuring the temperature dependence of the Ca2+-ATPase.

show abstract

Section: Myosin Preparationmentioning

confidence: 99%

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

Hoffmann

Siegert

1987

Basic Res Cardiol

View full text Add to dashboard Cite

show abstract

“…Troponin C was prepared from rabbit skeletal muscle as described by Perry and Cole (4). Myosin was prepared from rabbit skeletal muscle according to the method of Fredricksen (5) . Myosin light chain kinase (MLCK) was purified from chicken gizzard by using the procedure of Adelstein and Klee (6), and MLCK from turkey gizzard was a gift of Drs .…”

mentioning

confidence: 99%

Identification of calmodulin-binding proteins in chicken embryo fibroblasts.

Burgess¹,

Watterson²,

Eldik³

1984

The Journal of Cell Biology

View full text Add to dashboard Cite

We recently reported the detection of multiple classes of calmodulin-binding proteins in subcellular fractions of chicken embryo fibroblasts by using a gel binding procedure (Van Eldik, L.J., and W.H. Burgess, 1983, J. Biol. Chem., 258:4539-4547). In this report we identify many of these calmodulin-binding proteins and provide further evidence for the existence of multiple classes of calmodulin-binding proteins based on the interaction of these proteins with calmodulin and other calcium-modulated proteins. The fact that, in some cases, the same calmodulin-binding protein can bind troponin C and S100 alpha suggests that similar functional domains may be present in these distinct calcium-modulated proteins. We also have used protocols based on purification steps for calmodulin-binding proteins and calmodulin-regulated activities from other systems, in conjunction with enzymatic assays and various immunological methods, to identify many of the calmodulin-binding proteins in chicken embryo fibroblasts. The identities of these proteins suggest in vivo roles for calmodulin in the regulation of cell shape and motility, cyclic nucleotide metabolism, and possibly nucleic acid and protein turnover in fibroblasts.

show abstract

“…Either bipolar filaments were formed that were too short to correspond to those thought to exist in vivo (Hanson & Lowy, 1964;Shoenberg, 1969;Kaminer, 1969;Wachsberger & Pepe, 1974) or longer filaments lacking central bare zones were formed, whose morphology suggested the association of only anti-parallel units tebrate smooth muscles. Both myosins have similar physical properties, as determined by measurements of sedimentation, viscosity, and amino acid composition (Lowey & Cohen, 1962;Huriaux et al, 1965; Wachsberger & Kaldor, 1971;Groschel-Stewart, 1971;Frederiksen, 1979). They contain heavy and light chains (Murphy & Megerman, 1977) and can be cleaved into heavy and light meromyosins (Cohen et al, 1961;Huriaux, 1965; Barany et al, 1966).…”

mentioning

confidence: 99%

Polymerization of myosin from smooth muscle of the calf aorta

Megerman¹,

Lowey²

1981

Biochemistry

View full text Add to dashboard Cite

Myosin from smooth muscle of the calf aorta has been found to be similar to rabbit skeletal muscle myosin in molecular weight, sedimentation coefficient, and amino acid composition. When dialyzed at low ionic strength, it also forms polymers that exist in equilibrium with the "monomer", the position of this equilibrium being sensitive to ionic strength, pH, and hydrostatic pressure. The self-association reactions for smooth muscle myosin differ, however, from those observed for skeletal muscle myosin in several ways: (1) aorta myosin polymerizes at a higher ionic strength to form a smaller polymer; (2) between pH 6 and 8, only one polymer boundary is observed; (3) the result of varying total protein concentration on the myosin-polymer equilibrium cannot be analyzed by the Gilbert theory for a simple two-species system, as was possible with skeletal myosin. This more complex polymerization behavior may be related to differences in the mode of assembly between smooth and skeletal muscle myosin.

show abstract

Physical properties of myosin from aortic smooth muscle

Cited by 18 publications

References 30 publications

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

Identification of calmodulin-binding proteins in chicken embryo fibroblasts.

Polymerization of myosin from smooth muscle of the calf aorta

Contact Info

Product

Resources

About