Cell-free incorporation of newly synthesized myosin subunits into thick myofilaments

1991 ◽  
Vol 12 (2) ◽  
pp. 161-170 ◽  
Author(s):  
Steven M. Goldfine ◽  
Steven Einheber ◽  
Donald A. Fischman
Keyword(s):  
Myosin Subunits

scholarly journals Identification of sequences necessary for the association of cardiac myosin subunits.

1991 ◽  
Vol 113 (3) ◽  
pp. 585-590 ◽  
Author(s):  
E M McNally ◽  
M M Bravo-Zehnder ◽  
L A Leinwand
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Carboxyl Terminus ◽  
Amino Terminus ◽  
Cardiac Myosin ◽  
Amino Acid Region ◽  
Myosin Subunits ◽  
Acid Region

To begin to understand the nature of myosin subunit assembly, we determined the region of a vertebrate sarcomeric myosin heavy chain required for binding of light chain 1. We coexpressed in Escherichia coli segments of the rat alpha cardiac myosin heavy chain which spanned the carboxyl terminus of subfragment 1 and the amino terminus of subfragment 2 with a full-length rat cardiac myosin light chain 1. A 16 amino acid region of the myosin heavy chain (residues 792-808) was shown to be required for myosin light chain 1 binding in an immunoprecipitation assay.

scholarly journals Correlation among the proton charges and molecular masses of myosin subunits

FEBS Letters ◽  
1989 ◽  
Vol 249 (1) ◽  
pp. 8-12 ◽  
Author(s):  
Jean-Jacques Béchet ◽  
Anne d'Albis
Keyword(s):  
Myosin Subunits ◽  
Molecular Masses

Evaluation of myosin light chain phosphorylation in isolated pancreatic acini

1988 ◽  
Vol 254 (1) ◽  
pp. G130-G134 ◽  
Author(s):  
D. B. Burnham ◽  
H. D. Soling ◽  
J. A. Williams
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Specific Activity ◽  
Sucrose Solution ◽  
Myosin Light Chain Phosphorylation ◽  
Pancreatic Acini ◽  
Myosin Subunits ◽  
Sepharose 4B ◽  
Stimulation Of

The role of contractile proteins in secretory granule exocytosis was evaluated by determining whether myosin light chain phosphorylation was altered during stimulation of secretion in mouse pancreatic acini. Acinar myosin was purified by extraction into isosmotic sucrose solution containing 40 mM pyrophosphate followed by ammonium sulfate precipitation and Sepharose 4B-CL chromatography. Myosin was eluted as a single peak of K+-EDTA ATPase activity and was purified over 2,000-fold to a final ATPase specific activity of 0.96 mumol.min-1.mg protein-1. Three major myosin subunits of apparent Mr of 200,000, 20,000, and 17,000 were present in the purified myosin preparation. A fourth protein of Mr 21,000 was also present. Purification of myosin from 32P-labeled acini revealed the Mr 200,000, 21,000, and 20,000 proteins to be heavily labeled. The effect of cholecystokinin octapeptide (CCK-8) on myosin phosphorylation was studied after isolation of myosin from 32P-labeled acinar lysates by immunoprecipitation. Treatment of acini for 1-10 min with a concentration of CCK-8 that gives a maximal secretory response caused a 25-40% increase in light chain labeling. Treatment with a supramaximal CCK-8 concentration produced a 50-80% increase in light chain labeling. Phosphorylation of myosin heavy chain was not significantly affected by secretagogue treatment. These results indicate that stimulation of pancreatic acinar secretion is accompanied by an increase in myosin light chain phosphorylation.

scholarly journals Identification of in vivo phosphorylated myosin subunits

FEBS Letters ◽  
1974 ◽  
Vol 47 (1) ◽  
pp. 149-154 ◽  
Author(s):  
J. McPherson ◽  
C. Fenner ◽  
A. Smith ◽  
D.T. Mason ◽  
J. Wikman-Coffelt
Keyword(s):  
Myosin Subunits

scholarly journals Expression of ventricular myosin subunits in the atria of children with congenital heart malformations.

1991 ◽  
Vol 69 (6) ◽  
pp. 1601-1607 ◽  
Author(s):  
Q W Shi ◽  
U Danilczyk ◽  
J X Wang ◽  
Y P See ◽  
W G Williams ◽  
...  
Keyword(s):  
Congenital Heart ◽  
Congenital Heart Malformations ◽  
Ventricular Myosin ◽  
Myosin Subunits ◽  
Heart Malformations

scholarly journals Exchange in myosin subunits during amoebo-plasmodial transition in the life cycle of Physarum plasmodium

1986 ◽  
Vol 40 ◽  
pp. 142
Author(s):  
Kazuhiro Kohama ◽  
Hiromi Takano-Ohmuro ◽  
Taro Q.P. Uyeda ◽  
Takeshi Tanaka ◽  
Toshikazu Yamaguchi ◽  
...  
Keyword(s):  
Life Cycle ◽  
Myosin Subunits

Myosin subunits and contractile properties of single fibers from hypokinetic rat muscles

1987 ◽  
Vol 63 (6) ◽  
pp. 2293-2300 ◽  
Author(s):  
P. J. Reiser ◽  
C. E. Kasper ◽  
R. L. Moss
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Contractile Properties ◽  
Hindlimb Suspension ◽  
Maximal Velocity ◽  
Adult Rats ◽  
Single Fibers ◽  
Myosin Subunits ◽  
Change In The Mean ◽  
The Mean

The effects of prolonged hypokinesia on the contractile properties and myosin isozymes of single fibers from the synergistic fast-twitch plantaris (PL) and slow-twitch soleus (SOL) skeletal muscles of adult rats were studied after 28 days of hindlimb suspension. There was a 31% increase in the mean maximal velocity of unloaded shortening (Vmax) among fibers from SOL with no change in the mean Vmax of fibers from PL after suspension. The myosin heavy and light chain (MHC and MLC) composition of bundles and the MHC composition of single fibers from control and suspended muscles were examined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. There was a marked increase in the relative amount of fast-type MHC's in hypokinetic SOL and a smaller increase in the amount of fast-type MHC's in the PL. Relatively minor changes occurred in the MLC's during hypokinesia. As Vmax increased among individual fibers from control and suspended muscles, the relative amount of fast-type MHC's increased. The results demonstrate that the myosin isozyme composition of skeletal muscle, especially the heavy chains, is altered during hypokinesia, and this finding provides an explanation for changes in Vmax of rat single muscle fibers under the same conditions.

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