Caffeine-induced Release of Intracellular Ca2+ from Chinese Hamster Ovary Cells Expressing Skeletal Muscle Ryanodine Receptor
| Autor: | W.-J. Zang, Jiying Zhao, W G Wier, Hiroshi Takeshima, C W Balke, Manjunatha B. Bhat, Jianjie Ma |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
green fluorescent protein
Physiology Muscle Fibers Skeletal Gating chemistry.chemical_compound Cricetinae Image Processing Computer-Assisted Myocyte 0303 health sciences Ryanodine receptor Chinese hamster ovary cell 030302 biochemistry & molecular biology Cardiac muscle excitation–contraction coupling musculoskeletal system 3. Good health Cell biology Electrophysiology medicine.anatomical_structure Chinese hamster ovary cells cardiovascular system Rabbits Fura-2 tissues Ion Channel Gating Intracellular inorganic chemicals medicine.medical_specialty Heart Ventricles Green Fluorescent Proteins CHO Cells Biology Article 03 medical and health sciences calcium sparks Internal medicine Caffeine medicine Animals 030304 developmental biology Dose-Response Relationship Drug Skeletal muscle Ryanodine Receptor Calcium Release Channel Intracellular Membranes Protein Structure Tertiary Rats Luminescent Proteins Endocrinology chemistry Calcium Central Nervous System Stimulants |
| Zdroj: | The Journal of General Physiology |
| ISSN: | 1540-7748 0022-1295 |
| Popis: | The ryanodine receptor (RyR)/Ca2+ release channel is an essential component of excitation–contraction coupling in striated muscle cells. To study the function and regulation of the Ca2+ release channel, we tested the effect of caffeine on the full-length and carboxyl-terminal portion of skeletal muscle RyR expressed in a Chinese hamster ovary (CHO) cell line. Caffeine induced openings of the full length RyR channels in a concentration-dependent manner, but it had no effect on the carboxyl-terminal RyR channels. CHO cells expressing the carboxyl-terminal RyR proteins displayed spontaneous changes of intracellular [Ca2+]. Unlike the native RyR channels in muscle cells, which display localized Ca2+ release events (i.e., “Ca2+ sparks” in cardiac muscle and “local release events” in skeletal muscle), CHO cells expressing the full length RyR proteins did not exhibit detectable spontaneous or caffeine-induced local Ca2+ release events. Our data suggest that the binding site for caffeine is likely to reside within the amino-terminal portion of RyR, and the localized Ca2+ release events observed in muscle cells may involve gating of a group of Ca2+ release channels and/or interaction of RyR with muscle-specific proteins. |
| Databáze: | OpenAIRE |
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