Influence of the cardiac myosin hinge region on contractile activity
| Autor: | Paul Norton, Henry S. Slayter, Giovanni Cuda, James B. Caulfield, Sarkis S. Margossian, James R. Sellers, John W. Krueger |
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| Rok vydání: | 1991 |
| Předmět: |
Sarcomeres
Turkeys Myosin light-chain kinase ATPase Molecular Sequence Data Radioimmunoassay Antigen-Antibody Complex macromolecular substances Myosins Sarcomere Dogs Cardiac Myosins Myosin Animals Humans Myocyte Amino Acid Sequence Actin Multidisciplinary biology Heart Muscle Smooth Rats Microscopy Electron Biochemistry Gizzard Avian biology.protein Biophysics Peptides Myofibril Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 88:4941-4945 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.88.11.4941 |
| Popis: | The participation of cardiac myosin hinge in contractility was investigated by in vitro motility and ATPase assays and by measurements of sarcomere shortening. The effect on contractile activity was analyzed using an antibody directed against a 20-amino acid peptide within the hinge region of myosin. This antibody bound specifically at the hinge at a distance of 55 nm from the S1/S2 junction, was specific to human, dog, and rat cardiac myosins, did not crossreact with gizzard or skeletal myosin, and had no effect on ATPase activity of purified S1 and myofibrils. However, it completely suppressed the movement of actin filaments in in vitro motility assays and reduced active shortening of sarcomeres of skinned cardiac myocytes by half. Suppression of motion by the anti-hinge antibody may reflect a mechanical constraint imposed by the antibody upon the mobility of the S2 region of myosin. The results suggest that the steps in the mechanochemical energy transduction can be separately influenced through S2. |
| Databáze: | OpenAIRE |
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