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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Calcium-independent activation of the contractile apparatus in smooth muscle of mouse aorta by protein phosphatase inhibition.

Smooth muscle contraction is primarily regulated by reversible phosphorylation of the 20-kDa light chains of myosin (MLC(20)) involving Ca(2+)-calmodulin-dependent myosin light chain kinase (MLCK) and serine/threonine protein phosphatases (PP).The aim of this study was to investigate the effects of the protein phosphatases (PP) type 1 (PP1) and type 2A (PP2A) inhibitor cantharidin (Cant), its structural analogue endothall (ETA) and microcystin LR (MC) on force of contraction and MLC(20)-phosphorylation in arterial smooth muscle of mouse aorta. Cant increased force of contraction and MLC(20)-phosphorylation in intact arterial rings of mouse aorta in the presence of Ca(2+) whereas ETA and MC were ineffective under the same experimental conditions. In contrast, all compounds induced contraction and led to enhanced MLC(20)-phosphorylation in nominally Ca(2+)-free solution in fibers of mouse aorta permeabilised (skinned) with Triton X-100.In addition, Western blot analysis revealed that skinning of mouse aorta did not result in a loss of PP1 and PP2A compared to intact rings. Thus, both PP must be tightly bound to structural proteins, e.g. myosin. The findings indicate a Ca(2+)-independent mechanism of smooth muscle contraction involving inhibition of PP1- and/or PP2A-activities leading to enhanced force and MLC(20)-phosphorylation of arterial smooth muscle.[1]

References

  1. Calcium-independent activation of the contractile apparatus in smooth muscle of mouse aorta by protein phosphatase inhibition. Knapp, J., Aleth, S., Balzer, F., Schmitz, W., Neumann, J. Naunyn Schmiedebergs Arch. Pharmacol. (2002) [Pubmed]
 
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