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Myosin-Light-Chain Kinase: An enzyme that phosphorylates myosin light chains in the presence of Atp to yield myosin-light chain phosphate and Adp, and requires calcium and Calmodulin. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.

Muscle Contraction

JoVE 10869

In skeletal muscles, acetylcholine is released by nerve terminals at the motor end plate-the point of synaptic communication between motor neurons and muscle fibers. Binding of acetylcholine to its receptors on the sarcolemma allows entry of sodium ions into the cell and triggers an action potential in the muscle cell. Thus, electrical signals from the brain are transmitted to the muscle. Subsequently, the enzyme acetylcholinesterase breaks down acetylcholine to prevent excessive muscle stimulation. Individuals with the disorder myasthenia gravis, develop antibodies against the acetylcholine receptor. This prevents transmission of electrical signals between the motor neuron and muscle fiber and impairs skeletal muscle contraction. Myasthenia gravis is treated using drugs that inhibit acetylcholinesterase (allowing more opportunities for the neurotransmitter to stimulate the remaining receptors) or suppress the immune system (preventing the formation of antibodies). Unlike skeletal muscles, smooth muscles present in the walls of internal organs are innervated by the autonomic nervous system and undergo involuntary contractions. Contraction is mediated by the interaction between two filament proteins-actin and myosin. The interaction of actin and myosin is closely linked to intracellular calcium concentration. In response to neurotransmitter or hormone sig

 Core: Musculoskeletal System

Contractility Measurements of Human Uterine Smooth Muscle to Aid Drug Development

1Harris-Wellbeing Preterm Birth Research Centre, Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, 2School of Biomedical Sciences, The University of Queensland, 3Faculty of Chemistry, Institute of Biological Chemistry, University of Vienna, 4Institute for Molecular Bioscience, University of Queensland, 5Center for Physiology and Pharmacology, Medical University of Vienna

JoVE 56639

 Medicine

Isolation of Retinal Arterioles for Ex Vivo Cell Physiology Studies

1Centre for Experimental Medicine, Queen's University of Belfast, 2Centre for Biomedical Sciences (Education), Queen's University of Belfast, 3Department of Pharmaceutical Chemistry and Pharmacognosy, Naresuan University, 4School of Medicine, Dentistry and Biomedical Sciences, Queen's University of Belfast

JoVE 57944

 Biology

A Multi-well Format Polyacrylamide-based Assay for Studying the Effect of Extracellular Matrix Stiffness on the Bacterial Infection of Adherent Cells

1Department of Biochemistry, Stanford University School of Medicine, 2Department of Mechanical and Aerospace Engineering, University of California San Diego, 3Departments of Biochemistry, Microbiology and Immunology and Howard Hughes Medical Institute, Stanford University School of Medicine

JoVE 57361

 Immunology and Infection

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells

1Oxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, 2Lund University Diabetes Centre, Unit of Molecular Metabolism, Clinical Research Centre, Malmö University HospitalMalmö, 3Institute of Neuroscience of Physiology, Department of Physiology, Metabolic Research Unit, University of Göteborg, 4Oxford National Institute for Health Research, Biomedical Research Centre, 5Life and Medical Sciences, University of Hertfordshire

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JoVE 59491

 JoVE In-Press
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