Change in surface charge of sarcoplasmic reticulum membrane may elicit conformational change in sulfhydryl groups of membrane proteins to release calcium.
A lipophilic anion, tetraphenylboron (TPB-)-induced Ca2+ release from fragmented sarcoplasmic reticulum (SR) of frog skeletal muscle was monitored by chlortetracycline fluorescence. TPB- caused change in surface charge of the membrane and in the protein conformation with a time course similar to that of the Ca2+ release. Tetraphenylarsonium (TPA+) inhibited these effects of TPB-. Change in surface charge of SR is suggested to cause conformational change in SR membrane proteins, and then result in Ca2+ release from the SR.
Liu
G H
GH
Department of Physiology, Nagoya City University Medical School, Japan.
Oba
T
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D000818:Animals; D002118:Calcium / Q000378:metabolism*; D004594:Electrophysiology; D008565:Membrane Proteins / Q000378:metabolism*; D009132:Muscles / Q000166:cytology; D011487:Protein Conformation / Q000187:drug effects; D011892:Rana catesbeiana; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D013775:Tetraphenylborate / Q000494:pharmacology; D013997:Time Factors
D008565:Membrane Proteins; D013438:Sulfhydryl Compounds; D013775:Tetraphenylborate; D002118:Calcium