Am J Physiol Cell Physiol AJP: Regulatory, Integrative and Comparative Physiology
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Am J Physiol Cell Physiol 282: C451-C460, 2002. First published October 31, 2001; doi:10.1152/ajpcell.00333.2001
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Vol. 282, Issue 3, C451-C460, March 2002

220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patterns

Emily K. Blue1,*, Zoe M. Goeckeler2,*, Yijun Jin1, Ling Hou1, Shelley A. Dixon1, B. Paul Herring1, Robert B. Wysolmerski2,3, and Patricia J. Gallagher1

1 Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, Indiana 46202; and Departments of 2 Anesthesiology and 3 Pathology, St. Louis University School of Medicine, St. Louis, Missouri 63104

To better understand the distinct functional roles of the 220- and 130-kDa forms of myosin light chain kinase (MLCK), expression and intracellular localization were determined during development and in adult mouse tissues. Northern blot, Western blot, and histochemical studies show that the 220-kDa MLCK is widely expressed during development as well as in several adult smooth muscle and nonmuscle tissues. The 130-kDa MLCK is highly expressed in all adult tissues examined and is also detectable during embryonic development. Colocalization studies examining the distribution of 130- and 220-kDa mouse MLCKs revealed that the 130-kDa MLCK colocalizes with nonmuscle myosin IIA but not with myosin IIB or F-actin. In contrast, the 220-kDa MLCK did not colocalize with either nonmuscle myosin II isoform but instead colocalizes with thick interconnected bundles of F-actin. These results suggest that in vivo, the physiological functions of the 220- and 130-kDa MLCKs are likely to be regulated by their intracellular trafficking and distribution.

contraction; actin; myosin; myosin light chain kinase; smooth muscle; nonmuscle myosin light chain kinase; endothelium; fibroblast

* E. K. Blue and Z. M. Goeckeler contributed equally to this work.




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