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KMID : 0360419940300010125
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Korean Journal of Pharmacology
1994 Volume.30 No. 1 p.125 ~ p.136
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Characterization of Calcium Release Channel (Ryanodine Receptor) in Sarcoplasmic Reticulum of Crustacean Skeletal Muscle
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Seok Jeong-Ho
Jung Jung-Koo
Hur Gang-Min
Lee Jea-Heun
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Abstract
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To characterize the SR Ca-release channel protein complex of crustacean, binding, and immunoblot studies were carried out in the crayfish and/or lobster skeletal sarcoplasmic reticulum. Bmax and affinity of crayfish SR to ryanodine were lower than those of lobster SR. AMP (5mM) increased binding significantly in both vesicles (P<0.05). (5mM) or tetracaine(1mM) inhibited binding significantly in both vesicles (P<0.001), but ruthenium red inhibited it moderately. In SDS polyacrylamide gel electrophoretic analysis of crayfish SR vesicles, there was a high molecular weight band that showed similar mobility with Ca-release channel protein of lobster skeletal SR, but more rapid mobility (HMWBr) than that of rabbit skeletal SR (HMWBS). Immunoblot analysis showed that polyclonal Ab to lobster skeletal SR Ca-release channel protein was react with HMWBr of crayfish skeletal SR, but not with that of HMWBs of rabbit skeletal SR. from crayfish skeletal SR vesicles was increased by the increase of extravesicular calcium from to 1mM. This Ca-release phenomenon was similar, but more sensitive in the low concentration of , compared to that from lobster SR vesicles. AMP (5mM) or caffeine (10mM) did not affect to was inhibited slightly () (5mM) or tetracaine (1mM), and moderately (23%) by high concentration of ruthenium red . From the above results, it is suggested that SR Ca-release channel protein of crustacean has different properties from that of the rabbit, and similar properties between crayfish and lobster in functional and immunological aspects, but Ca-release via crayfish channel may be more sensitive to calcium.
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KEYWORD
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Sarcoplasmic reticulum, Ca-release channel, Ryanodine receptor, Crustaceans
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