Biochemistry of Smooth Muscle Contraction

Biochemistry of smooth muscle myosin light chain kinase.
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Zhi, and R. Padre , Myosin Light Chain Kinase.

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This valuable resource provides a systematic account of the biochemistry of smooth muscle contraction. As a comprehensive guide to this rapidly growing area. In the intact body, the process of smooth muscle cell contraction is regulated principally by receptor and mechanical (stretch) activation of the contractile proteins myosin and actin. Energy released from ATP by myosin ATPase activity results in the cycling of the myosin cross-bridges with actin for contraction.

Singer, S. Abraham, and C. Hofmann and N. Cornwell, P. Komalavilas, L. Macmillan-Crow, and N. Di Salvo, N. Kaplan, and L. Silver, and D. Chapter References. Subject Index.

Biochemical events associated with activation of smooth muscle contraction.

This book is an absolute must for anyone working in the smooth muscle field. It is ideal for students embarking on studies of smooth muscle and will get them up to speed with developments in this field up to approximately mid I intend to use this book extensively in a postgraduate course on 'Smooth Muscle Structure and Function My copy is already grubby from regular use!

The book provides comprehensive information on most of the important topics in this area The book summarizes nicely the major concepts and provides useful references. Few important aspects of smooth muscle are left uncovered Much in its pages will be of use to those either working or merely interested in the field. It covers all aspects of the fine structure of the contractile apparatus, signal transduction and regulation by calcium and protein phosphorylation, and the detailed mechanism and energetics of contraction.

From the vantage point of an outsider, it has been exciting for me to see how extensively this field has developed. The application of new methodologies, including those of molecular biology, has led to remarkable progress in elucidating the structure and assembly of the contractile machinery, including the complex interactions that take place between contractile elements.

This book, illustrates well how far these new technologies have taken us and where they might lead us tomorrow. We are always looking for ways to improve customer experience on Elsevier. We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit. If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website. Thanks in advance for your time. Skip to content.

Search for books, journals or webpages All Pages Books Journals. View on ScienceDirect. Editors: Michael Barany. Hardcover ISBN: Imprint: Academic Press. Fay FS: Isometric contractile properties of single isolated smooth muscle cells. Nature —, Hellstrand P, Johansson B: The force-velocity relation in phasic contraction of venous smooth muscle.

Uvelius B: Shortening velocity, active force, and homogeneity of contraction during electrically evoked twitches in smooth muscle from rabbit urinary bladder. Science —, Am J Physiol C - C, Hellstrand P, Johansson B: Analysis of the length response to a force step in smooth muscle from rabbit urinary bladder. Acta Physiol Scand 22 , Mulvany MJ: The undamped and damped series elastic components of a vascular smooth muscle.

Biophys J —, J Physiol 44 , Cecchi G, Griffiths PJ, Taylor S: Muscular contraction: kinetics of crossbridge attachment studied by high frequency stiffness measurements. Science 70—72, Peterson JW: Relation of stiffness, energy metabolism, and isometric tension in a vascular smooth muscle. Basel: S Karger, , 79— Cooke PH, Fay FS: Correlation between fiber length, ultrastructure, and the length-tension relationship of mammalion smooth muscle. J Cell Biol —, J Gen Physiol 85—, Gordon AR: Contraction of detergent treated smooth muscle. Peterson JW: Vandate ion inhibits actomyosin interaction in chemically skinned vascular smooth muscle.

Biochem Biophys Res Commun , J Biol Chem —, Saida K: A method of skinning smooth muscle fibers with A Biomed Res 2: —, J Gen Physiol , Biochemistry —, Taenia coli. Experientia —, Bremel RD: Myosin linked calcium regulation in vertebrate smooth muscle. Arch Biochem Biophys —, Sobieszek A, Bremel RD: Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin.

Eur J Biochem 49—60, J Biochem , J Gen Physiol —, Izant JG, Lazarides E: Invariance and heterogeneity in the major structural and regulatory proteins of chick muscle cells revealed by two-dimensional gel electrophoresis. Biochem Biophys Res Commun 35—41, Carsten ME: Uterine smooth muscle: troponin.

The biophysics and biochemistry of smooth muscle contraction.

Biochem J —, Walters M, Marston SB: Phosphorylation of the calcium ion-regulated thin filaments from vascular smooth muscle: a new regulatory mechanism? Achilles tendinitis [13] [14] and patellar tendonitis [15] also known as jumper's knee or patellar tendonosis have been shown to benefit from high-load eccentric contractions. In vertebrate animals , there are three types of muscle tissues: skeletal, smooth, and cardiac. Skeletal muscle constitutes the majority of muscle mass in the body and is responsible for locomotor activity. Smooth muscle forms blood vessels , gastrointestinal tract , and other areas in the body that produce sustained contractions.

Cardiac muscle make up the heart, which pumps blood.

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Skeletal and cardiac muscles are called striated muscle because of their striped appearance under a microscope, which is due to the highly organized alternating pattern of A bands and I bands. Excluding reflexes, all skeletal muscles contractions occur as a result of conscious effort originating in the brain. The brain sends electrochemical signals through the nervous system to the motor neuron that innervates several muscle fibers.

Other actions such as locomotion, breathing, and chewing have a reflex aspect to them: the contractions can be initiated both consciously or unconsciously. A neuromuscular junction is a chemical synapse formed by the contact between a motor neuron and a muscle fiber. The sequence of events that results in the depolarization of the muscle fiber at the neuromuscular junction begins when an action potential is initiated in the cell body of a motor neuron, which is then propagated by saltatory conduction along its axon toward the neuromuscular junction.

Acetylcholine diffuses across the synapse and binds to and activates nicotinic acetylcholine receptors on the neuromuscular junction.

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  • Muscle contraction - Wikipedia;

The membrane potential then becomes hyperpolarized when potassium exits and is then adjusted back to the resting membrane potential. This rapid fluctuation is called the end-plate potential [18] The voltage-gated ion channels of the sarcolemma next to the end plate open in response to the end plate potential. These voltage-gated channels are sodium and potassium specific and only allow one through. This wave of ion movements creates the action potential that spreads from the motor end plate in all directions. The remaining acetylcholine in the synaptic cleft is either degraded by active acetylcholine esterase or reabsorbed by the synaptic knob and none is left to replace the degraded acetylcholine.

Excitation—contraction coupling is the process by which a muscular action potential in the muscle fiber causes the myofibrils to contract. DHPRs are located on the sarcolemma which includes the surface sarcolemma and the transverse tubules , while the RyRs reside across the SR membrane. The close apposition of a transverse tubule and two SR regions containing RyRs is described as a triad and is predominantly where excitation—contraction coupling takes place.

Excitation—contraction coupling occurs when depolarization of skeletal muscle cell results in a muscle action potential, which spreads across the cell surface and into the muscle fiber's network of T-tubules , thereby depolarizing the inner portion of the muscle fiber. Depolarization of the inner portions activates dihydropyridine receptors in the terminal cisternae, which are in close proximity to ryanodine receptors in the adjacent sarcoplasmic reticulum.

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The activated dihydropyridine receptors physically interact with ryanodine receptors to activate them via foot processes involving conformational changes that allosterically activates the ryanodine receptors. Note that the sarcoplasmic reticulum has a large calcium buffering capacity partially due to a calcium-binding protein called calsequestrin. The near synchronous activation of thousands of calcium sparks by the action potential causes a cell-wide increase in calcium giving rise to the upstroke of the calcium transient.

The sliding filament theory describes a process used by muscles to contract. It is a cycle of repetitive events that cause a thin filament to slide over a thick filament and generate tension in the muscle. However the actions of elastic proteins such as titin are hypothesised to maintain uniform tension across the sarcomere and pull the thick filament into a central position. Crossbridge cycling is a sequence of molecular events that underlies the sliding filament theory. A crossbridge is a myosin projection, consisting of two myosin heads, that extends from the thick filaments. The binding of ATP to a myosin head detaches myosin from actin , thereby allowing myosin to bind to another actin molecule.

Once attached, the ATP is hydrolyzed by myosin, which uses the released energy to move into the "cocked position" whereby it binds weakly to a part of the actin binding site. The remainder of the actin binding site is blocked by tropomyosin. Unblocking the rest of the actin binding sites allows the two myosin heads to close and myosin to bind strongly to actin.

The power stroke moves the actin filament inwards, thereby shortening the sarcomere. Myosin then releases ADP but still remains tightly bound to actin.

At the end of the power stroke, ADP is released from the myosin head, leaving myosin attached to actin in a rigor state until another ATP binds to myosin. A lack of ATP would result in the rigor state characteristic of rigor mortis. Once another ATP binds to myosin, the myosin head will again detach from actin and another crossbridges cycle occurs.