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Articles in PresS, published online ahead of print October 31, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00333.2001
Submitted on July 19, 2001
Accepted on October 23, 2001
1 Physiology, Indiana University School of Medicine, Indianapolis, IN, USA
2 Anesthesiology & Pathology, St. Louis University School of Medicine, St. Louis, MO, USA
3 Genetic Disease Research Institute, National Institutes of Health, Bethesda, MD, USA
* To whom correspondence should be addressed. E-mail: pgallag{at}iupui.edu.
To better understand the distinct functional roles of the 220 and 130 kDa forms of myosin light chain kinase (MLCK), the expression and intracellular localization was determined during development and in adult mouse tissues. Northern, western and histochemical studies show that the 220 kDa MLCK is widely expressed during development as well as in several adult smooth and nonmuscle tissues. The 130 kDa MLCK is highly expressed in all adult tissues examined and is also detectable during embryonic development. Co-localization studies examining the distribution of 130 kDa and 220 kDa mouse MLCKs revealed that the 130 kDa MLCK co-localizes with nonmuscle myosin-IIA but not with IIB or F-actin. In contrast, the 220 kDa MLCK did not co-localize with either nonmuscle myosin II isoform but instead co-localizes 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.
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