scholarly journals MicroRNA Regulation of Nonmuscle Myosin Light Chain Kinase Expression in Human Lung Endothelium

2013 ◽  
Vol 49 (1) ◽  
pp. 58-66 ◽  
Author(s):  
Djanybek M. Adyshev ◽  
Nurgul Moldobaeva ◽  
Brandon Mapes ◽  
Venkate Elangovan ◽  
Joe G. N. Garcia
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Human Lung ◽  
Nonmuscle Myosin ◽  
Microrna Regulation ◽  
Lung Endothelium ◽  
Kinase Expression

scholarly journals Quantitative distribution and colocalization of non-muscle myosin light chain kinase isoforms and cortactin in human lung endothelium

2010 ◽  
Vol 80 (1) ◽  
pp. 75-88 ◽  
Author(s):  
Mary Brown ◽  
Djanybek Adyshev ◽  
Vytautus Bindokas ◽  
Jaideep Moitra ◽  
Joe G.N. Garcia ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Human Lung ◽  
Quantitative Distribution ◽  
Lung Endothelium ◽  
Muscle Myosin

scholarly journals Myosin light chain kinase (MYLK) coding polymorphisms modulate human lung endothelial cell barrier responses via altered tyrosine phosphorylation, spatial localization, and lamellipodial protrusions

2018 ◽  
Vol 8 (2) ◽  
pp. 204589401876417 ◽  
Author(s):  
Ting Wang ◽  
Mary E. Brown ◽  
Gabriel T. Kelly ◽  
Sara M. Camp ◽  
Joseph B. Mascarenhas ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Tyrosine Phosphorylation ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Human Lung ◽  
Disease Risk ◽  
Spatial Localization ◽  
Cell Periphery ◽  
Nucleotide Polymorphisms

Sphingosine 1-phosphate (S1P) is a potent bioactive endogenous lipid that signals a rearrangement of the actin cytoskeleton via the regulation of non-muscle myosin light chain kinase isoform (nmMLCK). S1P induces critical nmMLCK Y464 and Y471 phosphorylation resulting in translocation of nmMLCK to the periphery where spatially-directed increases in myosin light chain (MLC) phosphorylation and tension result in lamellipodia protrusion, increased cell-cell adhesion, and enhanced vascular barrier integrity. MYLK, the gene encoding nmMLCK, is a known candidate gene in lung inflammatory diseases, with coding genetic variants (Pro21His, Ser147Pro, Val261Ala) that confer risk for inflammatory lung injury and influence disease severity. The functional mechanisms by which these MYLK coding single nucleotide polymorphisms (SNPs) affect biologic processes to increase disease risk and severity remain elusive. In the current study, we utilized quantifiable cell immunofluorescence assays to determine the influence of MYLK coding SNPs on S1P-mediated nmMLCK phosphorylation and translocation to the human lung endothelial cell (EC) periphery . These disease-associated MYLK variants result in reduced levels of S1P-induced Y464 phosphorylation, a key site for nmMLCK enzymatic regulation and activation. Reduced Y464 phosphorylation resulted in attenuated nmMLCK protein translocation to the cell periphery. We further conducted EC kymographic assays which confirmed that lamellipodial protrusion in response to S1P challenge was retarded by expression of a MYLK transgene harboring the three MYLK coding SNPs. These data suggest that ARDS/severe asthma-associated MYLK SNPs functionally influence vascular barrier-regulatory cytoskeletal responses via direct alterations in the levels of nmMLCK tyrosine phosphorylation, spatial localization, and lamellipodial protrusions.

scholarly journals Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating β2 integrins

2008 ◽  
Vol 9 (8) ◽  
pp. 880-886 ◽  
Author(s):  
Jingsong Xu ◽  
Xiao-Pei Gao ◽  
Ramaswamy Ramchandran ◽  
You-Yang Zhao ◽  
Stephen M Vogel ◽  
...  
Keyword(s):  
Light Chain ◽  
Lung Inflammation ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Nonmuscle Myosin ◽  
Β2 Integrins
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