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Differential effects of myosin light chain kinase inhibition on contractility, force development and myosin light chain 20 phosphorylation of rat cervical and thoracic duct lymphatics
Author(s) -
Nepiyushchikh Zhanna V.,
Chakraborty Sanjukta,
Wang Wei,
Davis Michael J.,
Zawieja David C.,
Muthuchamy Mariappan
Publication year - 2011
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.218446
Subject(s) - myosin light chain kinase , lymphatic system , myosin , tonic (physiology) , phosphorylation , contractility , thoracic duct , muscle contraction , microbiology and biotechnology , anatomy , myosin light chain phosphatase , biology , chemistry , endocrinology , immunology
Non‐Technical Summary The contractile activities of lymphatic muscle cells, which are the key for the lymphatic function, vary between lymphatic beds. We show that pressure‐dependent changes and myosin light chain kinase (MLCK) inhibition differentially affect myosin light chain 20 (MLC 20 ) phosphorylation in lymphatic muscle, thereby controlling the contractile behaviour of thoracic duct and cervical lymphatics. Our findings suggest that pressure‐induced changes in lymphatic contractile function act through MLC 20 di‐phosphorylation to modulate lymphatic tonic contractions, whereas the MLCK inhibitor ML‐7 affects both mono‐ and di‐phosphorylation of MLC 20 and consequently decreases tonic contractions. In addition, our data indicate that ML‐7 affects pacemaking activity of lymphatic muscle, and thereby decreases the lymphatic phasic contraction frequency. Thus the statuses of MLC 20 phosphorylation play essential roles in regulating the contractile activities of lymphatics.