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Study identified MYLK3 mutations associated with familial dilated cardiomyopathy. In vitro experiments and immunohistochemistry suggested that the MYLK3 mutations identified in this study result in markedly reduced levels of protein expression and myosin light chain 2 phosphorylation.
This study demonstrates that cyclic stretch disrupts tight junctions and adherens junctions by a JNK2, c-Src, and MLCK-dependent mechanism.
Biochemical and physiological regulation of cardiac myocyte contraction by cardiac-specific myosin light chain kinase.
These findings suggest that hepatitis B virus X protein disrupts stress fiber formation and triggers apoptosis via an MLCK and a PTEN-dependent pathway.
Integrated cDNA expression analysis of failing human myocardia uncovered a novel protein kinase, cardiac-specific myosin light chain kinase (cardiac-MLCK), which acts on MLC2v.
data indicate that the IL-1beta-induced increase in MLCK protein expression and Caco-2 TJ permeability was mediated by an increase in MLCK expression and activity and by an NF-kappaB-dependent increase in MLCK gene transcription
Pharmacological study revealed that lamellipodia formation mediated by arp2/3 and contractility regulated by myosin light chain kinase (MLCK) were responsible for the intriguing turning behavior of T cells climbing the ramp-like structures.
Acanthopanax senticosus polysaccharide pretreatment may be associated with inhibition of the NF-kappaB/MLCK pathway and concomitant amelioration of LPS-induced tight junction dysfunction of intestinal epithelium in endotoxemia
that MLCK is competing with centrally active ROCK for a limiting pool of monomer with which to drive lamellar filament assembly
This study demonstrated that catchlike property during dynamic performance in mouse hindlimb muscles with (wild-type) and without MLCK(-/-) ) the primary mechanism for PTP (myosin phosphorylation).
Ablation of cardiac Mylk3 suggests that Mylk3 plays a pivotal role in the transition from compensated to decompensated hypertrophy via cardiac myocyte atrophy and sarcomeric disorganization.
Data suggest that galectin-3 in hepatocellular carcinoma cells promotes cell migration by inducing RhoA GTPase activity, activating Mlck, up-regulating phosphorylation of MLC2 (myosin light chain 2), and inducing actin rearrangement.
epithelial MLCK-activated brush border fanning by IFN-gamma promotes adherence and internalization of normally noninvasive enteric bacteria
MLCK may regulate the structure and the motility of stereocilia through F-actin polymerization.
Silencing TNFR2, but not TNFR1, resulted in restoration of epithelial tight junction (TJ) associated with decreased MLCK expression.
Calcium regulation of MLCK facilitates GLUT4-mediated glucose uptake in 3T3-L1 adipocytes.
nmMLCK has a critical role in thrombin-induced endothelial cell inflammation and lung PMN infiltration
these studies show that the IL-1beta-induced increase in intestinal tight junction permeability was regulated by p38 kinase activation of ATF-2 and by ATF-2 regulation of MLCK gene activity
analysis of differential contributions of MLCK to signaling in smooth muscles
MLCK-dependent MLC phosphorylation mediates intestinal epithelial barrier dysfunction after severe burn injury.
Nonmuscle myosin light-chain kinase contributes to atherosclerosis by regulating endothelial barrier function and monocyte migration via mechanisms involving not only kinase-mediated MLC phosphorylation but also Src activation.
guanylyl cyclase C signaling plays a protective role in the integrity of the intestinal mucosal barrier by regulating myosin light chain kinase activation and tight junction disassembly.
cMLCK appears to be the predominant protein kinase that maintains basal RLC phosphorylation that is required for normal physiological cardiac performance in vivo
Ubiquitously expressed smooth muscle MLCK activity in MLCK null mice may be sufficient, but is not necessary for cytokinesis and early morphogenesis; other Ca2+-dependent kinases can phosphorylate myosin light-chain (20) and induce contraction in embryos.
MLCK is involved in egg polarity because inhibitors prevent sperm chromatin-induced cortical reorganization.
Inhibiting MLCK increases the number of apoptotic cells and retards the growth of mammary cancer cells in mice.
Phosphorylation of cardiac myosin heavy chains (see MYH7B, MIM 609928) and light chains (see MYL2, MIM 160781) by a kinase, such as MYLK3, potentiates the force and rate of cross-bridge recruitment in cardiac myocytes (Chan et al., 2008
, cardiac-MyBP-C associated Ca/CaM kinase
, cardiac-MyBP-C-associated Ca/CaM kinase
, putative myosin light chain kinase 3
, cardiac MLCK
, cardiac-specific myosin light chain kinase
, myosin light chain kinase 3
, Putative myosin light chain kinase 3