The variable coupling between force and myosin light chain phosphorylation in Triton-skinned chicken gizzard fibre bundles: role of myosin light chain phosphatase

1995 ◽  
Vol 429 (5) ◽  
pp. 708-715 ◽  
Author(s):  
Ulrike S. Schmidt ◽  
Monika Troschka ◽  
Gabriele Pfitzer
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Myosin Light Chain Phosphorylation ◽  
Myosin Light Chain Phosphatase ◽  
Fibre Bundles ◽  
Chicken Gizzard ◽  
Variable Coupling

scholarly journals Role of Myosin Light Chain Phosphorylation in the Regulation of Cytokinesis

2001 ◽  
Vol 26 (6) ◽  
pp. 639-644 ◽  
Author(s):  
Fumio Matsumura ◽  
Go Totsukawa ◽  
Yoshihiko Yamakita ◽  
Shigeko Yamashiro
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Myosin Light Chain Phosphorylation

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.

Role of myosin II activity and the regulation of myosin light chain phosphorylation in astrocytomas

2007 ◽  
Vol 65 (1) ◽  
pp. 12-24 ◽  
Author(s):  
Bodour Salhia ◽  
Jeong Hyun Hwang ◽  
Christian A. Smith ◽  
Mitsutoshi Nakada ◽  
Fiona Rutka ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Myosin Ii ◽  
Myosin Light Chain Phosphorylation
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