Smooth muscle contractility is modulated by myosin tail-S2-LMM hinge region interaction
| Autor: | Anne F. Martin, Richard J. Paul, Shuang Cai, D. G. Ferguson |
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| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Myosin light-chain kinase Meromyosin Physiology Immunoelectron microscopy Blotting Western Guinea Pigs Muscle Smooth macromolecular substances Cell Biology Smooth muscle contraction Myosins Biology Microscopy Electron Myosin head Biochemistry Myosin Biophysics medicine Animals MYH7 medicine.symptom Muscle Contraction Muscle contraction |
| Zdroj: | American Journal of Physiology-Cell Physiology. 269:C1126-C1132 |
| ISSN: | 1522-1563 0363-6143 |
| DOI: | 10.1152/ajpcell.1995.269.5.c1126 |
| Popis: | The functional significance of two major smooth muscle myosin isoforms, which differ in the nonenzymic COOH-terminal tail region, is not known. We report here that a 13-amino acid peptide, which mimics a region of the tail unique to the SM1 myosin isoform, inhibits contraction velocity in permeabilized smooth muscle. This peptide is shown to bind to the S2-light meromyosin (LMM) hinge region of myosin using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, photoaffinity labeling, and immunoelectron microscopy. Our results suggest that novel intermolecular contacts between the tail and S2-LMM hinge regions of adjacent myosin molecules in the thick filament may modulate contractility and provide a basis for distinct isoform function. |
| Databáze: | OpenAIRE |
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