Myosin Light Chain
Myosin Light Chain - Related Videos
10:30
A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
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Cited by 4 •
2013
The botulinum neurotoxin type A light chain (BoNT/A LC) is a metalloprotease that enters motor neurons, cleaves its substrate SNAP-25, and disrupts neurotransmission, thereby resulting in flaccid paralysis. Utilizing a high-throughput-compatible FRET-based assay, large libraries of small molecules can be screened for their impact on BoNT/A LC enzymatic activity.
05:57
A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry
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Cited by 13 •
2017
Here, we present a protocol for rapid muscle fiber analyses, which allows improved staining quality, and thereby automatic acquisition and quantification of fiber populations using the freely available software ImageJ.
03:39
Inverted Motility Assay: An In Vitro Technique to Visualize Myosin Movement on Immobilized Actin Filaments
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2025
In this video, we perform an in vitro motility assay to analyze the actin-myosin interactions. The gliding movement of actin filaments on immobilized myosin molecules is visualized using fluorescence microscopy.
10:12
A Sensitive and Specific Quantitation Method for Determination of Serum Cardiac Myosin Binding Protein-C by Electrochemiluminescence Immunoassay
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Cited by 16 •
2013
Measuring biomarkers in complex biological samples is increasingly guiding clinical decision-making. We describe a highly sensitive method to simultaneously measure cardiac myosin binding protein-C, creatine kinase MB, and cardiac troponin I in serum samples from subjects with myocardial infarction and healthy control subjects.
01:28
Electron Transport Chains
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2019
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle. The ETC is comprised of...
FAQs
In smooth muscle, the key sequence is calcium elevation, calmodulin binding, activation of myosin light-chain kinase, and regulatory light-chain phosphorylation. Phosphorylation changes the myosin state so it can interact productively with actin, linking an intracellular calcium signal to force generation. This pathway provides a mechanistic basis for studying contraction in vascular, airway, and gastrointestinal tissues.
The balance between myosin light-chain kinase and myosin phosphatase helps determine the phosphorylation state of the regulatory light chain. Kinase activity promotes the contractile state described for smooth muscle, whereas phosphatase removes the phosphorylation signal. Examining both opposing activities is therefore more informative than considering phosphorylation alone when interpreting changes in smooth-muscle force regulation.
Although the regulatory pathway is especially described in smooth muscle, myosin light chains are associated with force generation in cardiac and skeletal muscle as well as other actin-based movements. The physiological meaning of a change therefore depends on the tissue being studied. This broader context helps distinguish a vascular or motility finding from a muscle-injury finding.
Altered phosphorylation can serve as evidence that regulation of actin interaction and force generation has changed. In smooth muscle, such findings may be relevant to vascular tone or airway and gastrointestinal motility. They do not by themselves identify a disease, but they help researchers connect molecular regulation with functional changes in tissues.
Circulating light-chain levels provide a complementary signal to phosphorylation measurements. Whereas phosphorylation reflects a regulatory state within the studied system, circulating levels can inform research into muscle injury and disease. Using both types of information may help separate questions about how contraction is controlled from questions about whether muscle damage or disease-related change is present.
It is relevant wherever actin-based force or movement has clinical importance. Smooth-muscle studies can address vascular tone, airway behavior, and gastrointestinal motility, while cardiac and skeletal muscle research can examine muscle function. Measurements of regulation or circulating levels connect these settings to broader questions about contraction, muscle injury, and disease.