Journal
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
Volume 282, Issue 3, Pages C451-C460Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpcell.00333.2001
Keywords
contraction; actin; myosin; myosin light chain kinase; smooth muscle; nonmuscle myosin light chain kinase; endothelium; fibroblast
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Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R29HL045788, R01HL058571, R01HL045788, R01HL054118] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R01 HL058571, R01 HL054118-03, HL 45788, R01 HL045788, R01 HL054118, HL 58571, HL 54118] Funding Source: Medline
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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.
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