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Am J Physiol Cell Physiol 282: C94-C104, 2002. First published September 5, 2001; doi:10.1152/ajpcell.00257.2001
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Vol. 282, Issue 1, C94-C104, January 2002

Differences in calmodulin and calmodulin-binding proteins in phasic and tonic smooth muscles

Pawel T. Szymanski1, Grazyna Szymanska2, and Raj K. Goyal1

1 Center for Swallowing and Motility Disorders, Harvard Medical School, West Roxbury Department of Veterans Affairs Medical Center, West Roxbury 02132; and 2 Department of Biology, Boston College, Chestnut Hill, Massachusetts 02467

To determine whether densities of calmodulin (CaM) and CaM-binding proteins are related to phasic and tonic behavior of smooth muscles, we quantified these proteins in the opossum esophageal body (EB) and lower esophageal sphincter (LES), which represent phasic and tonic smooth muscles, respectively. Gel electrophoresis, immunoprecipitation, Western blot, and hemagglutinin epitope-tagged CaM (HA-CaM) overlay assay with quantitative scanning densitometry and phosphorylation measurements were used. Total protein content in the two smooth muscles was similar (~30 mg protein/g frozen tissue). Total tissue concentration of CaM was significantly (25%) higher in EB than in LES (P < 0.05). HA-CaM-binding proteins were qualitatively similar in LES and EB extracts. Myosin, myristoylated alanine-rich C kinase substrate protein, Ca2+/CaM kinase II, and calponin contents were also similar in the two muscles. However, content and total activity of myosin light chain kinase (MLCK) and content of caldesmon (CaD) were three- to fourfold higher in EB than in LES. Increased CaM and MLCK content may allow for a wide range of contractile force varying from complete relaxation in the basal state to a large-amplitude, high-velocity contraction in EB phasic muscle. Increased content of CaD, which provides a braking mechanism on contraction, may further contribute to the phasic contractile behavior. In contrast, low CaM, MLCK, and CaD content may be responsible for a small range of contractile force seen in tonic muscle of LES.

caldesmon; calcium/calmodulin kinase II; hemagglutinin epitope-tagged calmodulin; lower esophageal sphincter; myristoylated alanine-rich C kinase substrate protein; myosin light chain kinase; visceral smooth muscles


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