Proteins contractile

In the presence of calcium, the primary contractile protein, myosin, is phosphorylated by the myosin light-chain kinase initiating the subsequent actin-activation of the myosin adenosine triphosphate activity and resulting in muscle contraction. Removal of calcium inactivates the kinase and allows the myosin light chain to dephosphorylate myosin which results in muscle relaxation. Therefore the general biochemical mechanism for the muscle contractile process is dependent on the avaUabUity of a sufficient intraceUular calcium concentration. 

Contractile proteins Myosin 520 43 A band Contracts with actin... 

Studies on muscle contraction carried out between 1930 and 1960 heralded the modem era of research on cytoskeletal stmctures. Actin and myosin were identified as the major contractile proteins of muscle, and detailed electron microscopic studies on sarcomeres by H.E. Huxley and associates in the 1950s produced the concept of the sliding filament model, which remains the keystone to an understanding of the molecular mechanisms responsible for cytoskeletal motility. 

The principal molecular constituent of thin filaments is actin. Actin has been highly conserved during the course of evolution and is present in all eukaryotes, including single-celled organisms such as yeasts. Actin was first extracted and purified from skeletal muscle, where it forms the thin filaments of sarcomeres. It also is the main contractile protein of smooth muscle. Refined techniques for the detection of small amounts of actin (e.g., immunofluorescence microscopy, gel electrophoresis, and EM cytochemistry) subsequently confirmed the presence of actin in a great variety of nonmuscle cells. Muscle and nonmuscle actins are encoded by different genes and are isoforms. 

Four different localizations of fatigue can be identified (a) decreased central command (b) decreased activation of the muscle membrane and the T-tubular system (c) decreased Ca release from the SR and (d) decreased response to the Ca release by the contractile proteins. The first two are partly extra-muscular while c and d are intramuscular responses to the excitation of the muscle membrane and often defined as excitation-contraction coupling. 

From this brief summary of excitation-contraction coupling it is obvious that Ca is an important link between the activated membrane and the contractile proteins, and thus a regulator of tension development. Westerblad et al. (1991) defined three factors which explain the force decrease in fatigued muscle reduced Ca " release from the SR, reduced Ca sensitivity of the myofilaments, and reduced maximum Ca -activated tension. 

Fatigue during intermittent tetanic stimulation is caused by three mechanisms (a) decreased maximum Ca activated tension, (b) decreased sensitivity of the contractile proteins, and (c) decreased Ca release from the SR. 

Assays. Protein concentrations were measured by the method of Bradford (18) and the various contractile protein ATPase activities by tRe method of Martin and Doty (19). Gel electrophoresis was carried out by the method of Ames (20) on 1.5 ran polyacrylamide slabs using the discontinuous SDS buffer system of Laemnli (21). Dried gels were scanned at 550 nm for densiometry measurements. 

The author gratefully acknowledges the cooperation of Dr. Roger Cooke, the Department of Biochemistry and Biophysics, U.C.S.F., for contractile protein-related materials and assays. 

Actin and myosin molecules, and thrombosthenin, are contractile proteins that enable platelets to contract. 

Volume 82. Structural and Contractile Proteins (Part A Extracellular Matrix) Edited by Leon W. Cunningham and Dixie W. Frederiksen... 

Roshchina V.V. (2005a). Contractile proteins in chemical signal transduction in plant microspores. Biological Bulletin, Ser. Biol. 3 281-286. 

Mechanical functions of cells require interactions between integral membrane proteins and the cyto-skeleton. These functions include organization of signaling cascades, formation of cell junctions and regulation of cell shape, motility, endo- and exocytosis. Several different families of membrane-associated proteins mediate specific interactions among integral membrane proteins, cytoskeletal proteins and contractile proteins. Many of these linker proteins consist largely of various combinations of conserved protein-association domains, which often occur in multiple variant copies. 

Bolton-. The SR normally underlies the rows of caveolae. Between those are the dense bars where the contractile proteins are attached. It seems likely that the caveolae contain receptors and channels, and that the SR occurs under the voltage-dependent channels. 

The anatomical unit of muscle is an elongated cell called a fibre. Each individual fibre cell consists of myofibrils which are bundles of contractile protein filaments composed of actin and myosin (Figure 7.1). Differences in structure indicate that muscles have evolved to perform particular functions. Although the structure of fibres, myofibrils and filaments of actin and myosin, is similar in all muscle types, their arrangement, action and control allow identification of three tissue types ... 

Contractile proteins which form the myofibrils are of two types myosin ( thick filaments each approximately 12 nm in diameter and 1.5 (im long) and actin ( thin filaments 6nm diameter and 1 (Am in length). These two proteins are found not only in muscle cells but widely throughout tissues being part of the cytoskeleton of all cell types. Filamentous actin (F-actin) is a polymer composed of two entwined chains each composed of globular actin (G-actin) monomers. Skeletal muscle F-actin has associated with it two accessory proteins, tropomyosin and troponin complex which are not found in smooth muscle, and which act to regulate the contraction cycle (Figure 7.1). 

A large and diverse group of proteins, including enzymes, cytoskeleton, contractile proteins, and receptors, have been shown to be modified by calpains. Thus, a number of enzymes such as tyrosine hydrolase, tryptophan hydrolase, transglutaminase, protein kinase C, and membrane Ca2+-ATPase are activated by calpain proteolysis [38]. Several receptor proteins, in particular receptors for steroid hormones, growth factors, and adrenaline, are modulated by calpains, which participate also in platelet activation, cell fusion, and mitosis [39], Although the physiological roles of calpains continue to be un-... 

Thrombosthenin, the Contractile Protein from Blood Platelets and Its Relation to Other Contractile Proteins M. Bettex-Galland and E. F. LOscher... 

From this series, compound MCI-154 (CAS 98326-33-1) (30) has been investigated in detail [95,96]. In vivo studies (anaesthetized dogs) revealed that doses of 0.3-100 tg/kg (i.v. administration) of MCI-154 produce dose-dependent increases in dF/dtmax and cardiac output, and decreases in arterial blood pressure and total peripheral resistance. The positive inotropic effect of (30) has been found to be superior to that exhibited by amrinone and milrinone [97,98]. It has been stated that MCI-154 exerts its activity probably by increasing the calcium-ion sensitivity of the contractile protein system of the cardiac skinned fibres [99,100]. A recent investigation suggests that inhibition of phosphodiesterase III is an important component of its cardiotonic activity [101]. 

Since musculature shows a structure with oriented contractile proteins, cells and fibres (see Section 2) diffusion is not expected to be isotropic. Assessment... 

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