Can oligomeric myosin participate in smooth muscle contraction? 1985

S Horio, and T Yamada, and H Shimizu, and H Ishikawa

An experimental model was constructed to examine the possible fact that myosin oligomers take a part in smooth muscle contraction. Single fibres prepared from glycerinated rabbit skeletal muscle were emptied of myosin and then irrigated with purified chicken gizzard myosin. This was a good preparation in which to see the structural change of gizzard myosin and its interaction with actin filaments under the electron microscope. The structure of gizzard myosin was thoroughly changed by varying the concentration of free Mg2+ in the bathing solution. Myosin thick filaments were formed at the position of the A-band longitudinally bridging adjacent I-segments at high concentration of free Mg2+, while most of them disappeared from the A-band and some localized in the I-segment at low concentration of free Mg2+. When this preparation was induced to contract isometrically, it showed quite different sarcomere patterns at high and low concentrations of free Mg2+. Tensions developed by this preparation were of the same magnitude at high and low concentrations of free Mg2+, which were approximately 5% of that developed by glycerinated skeletal muscle fibres. The shortening of the prepared fibre in a contracting medium was almost the same at varying concentrations of free Mg2+. The relation between the structural organization and the contracting nature of the prepared fibre as the concentration of free Mg2+ was varied is discussed in this paper with respect to the significance of oligomeric myosin in smooth muscle contraction.

UI MeSH Term Description Entries
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D009119 Muscle Contraction A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments. Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D009130 Muscle, Smooth Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed) Muscle, Involuntary,Smooth Muscle,Involuntary Muscle,Involuntary Muscles,Muscles, Involuntary,Muscles, Smooth,Smooth Muscles
D009218 Myosins A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D005895 Gizzard, Avian The posterior portion of the avian stomach located between the PROVENTRICULUS and INTESTINE. It consists of a thick muscular wall and small stones (gastroliths) that function to mechanically grind SEEDS and other ingested objects. Gizzard,Ventriculus,Avian Gizzard,Avian Gizzards,Gizzards,Gizzards, Avian
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D066298 In Vitro Techniques Methods to study reactions or processes taking place in an artificial environment outside the living organism. In Vitro Test,In Vitro Testing,In Vitro Tests,In Vitro as Topic,In Vitro,In Vitro Technique,In Vitro Testings,Technique, In Vitro,Techniques, In Vitro,Test, In Vitro,Testing, In Vitro,Testings, In Vitro,Tests, In Vitro,Vitro Testing, In

Related Publications

S Horio, and T Yamada, and H Shimizu, and H Ishikawa
June 2000, Nature cell biology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
August 1991, Biochemical and biophysical research communications,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
June 1998, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
July 2009, American journal of physiology. Heart and circulatory physiology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
January 2005, Advances in experimental medicine and biology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
May 1991, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
July 1985, The American journal of physiology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
January 2020, Frontiers in physiology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
January 1992, Japanese journal of pharmacology,
S Horio, and T Yamada, and H Shimizu, and H Ishikawa
August 1982, Nature,
Copied contents to your clipboard!