Functional expression of cDNA encoding the calcium release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum in COS-1 cells

Biochemistry ◽  
1993 ◽  
Vol 32 (14) ◽  
pp. 3743-3753 ◽  
Author(s):  
S. R. Wayne Chen ◽  
Donna M. Vaughan ◽  
Judith A. Airey ◽  
Roberto Coronado ◽  
David H. MacLennan
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Functional Expression ◽  
Rabbit Skeletal Muscle ◽  
Calcium Release Channel ◽  
Release Channel

scholarly journals Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum.

1988 ◽  
Vol 92 (1) ◽  
pp. 1-26 ◽  
Author(s):  
J S Smith ◽  
T Imagawa ◽  
J Ma ◽  
M Fill ◽  
K P Campbell ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Binding Capacity ◽  
Ruthenium Red ◽  
Rabbit Skeletal Muscle ◽  
Permeability Ratio ◽  
Calcium Release Channel ◽  
Release Channel

The ryanodine receptor of rabbit skeletal muscle sarcoplasmic reticulum was purified as a single 450,000-dalton polypeptide from CHAPS-solubilized triads using immunoaffinity chromatography. The purified receptor had a [3H]ryanodine-binding capacity (Bmax) of 490 pmol/mg and a binding affinity (Kd) of 7.0 nM. Using planar bilayer recording techniques, we show that the purified receptor forms cationic channels selective for divalent ions. Ryanodine receptor channels were identical to the Ca-release channels described in native sarcoplasmic reticulum using the same techniques. In the present work, four criteria were used to establish this identity: (a) activation of channels by micromolar Ca and millimolar ATP and inhibition by micromolar ruthenium red, (b) a main channel conductance of 110 +/- 10 pS in 54 mM trans Ca, (c) a long-term open state of lower unitary conductance induced by ryanodine concentrations as low as 20 nM, and (d) a permeability ratio PCa/PTris approximately equal to 14. In addition, we show that the purified ryanodine receptor channel displays a saturable conductance in both monovalent and divalent cation solutions (gamma max for K and Ca = 1 nS and 172 pS, respectively). In the absence of Ca, channels had a broad selectivity for monovalent cations, but in the presence of Ca, they were selectively permeable to Ca against K by a permeability ratio PCa/PK approximately equal to 6. Receptor channels displayed several equivalent conductance levels, which suggest an oligomeric pore structure. We conclude that the 450,000-dalton polypeptide ryanodine receptor is the Ca-release channel of the sarcoplasmic reticulum and is the target site of ruthenium red and ryanodine.

scholarly journals Functional expression of the calcium release channel from skeletal muscle ryanodine receptor cDNA

FEBS Letters ◽  
1989 ◽  
Vol 259 (1) ◽  
pp. 217-221 ◽  
Author(s):  
Reinhold Penner ◽  
Erwin Neher ◽  
Hiroshi Takeshima ◽  
Seiichiro Nishimura ◽  
Shosaku Numa
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Functional Expression ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Receptor Cdna

scholarly journals The ryanodine receptor/junctional channel complex is regulated by growth factors in a myogenic cell line.

1991 ◽  
Vol 114 (2) ◽  
pp. 303-312 ◽  
Author(s):  
A R Marks ◽  
M B Taubman ◽  
A Saito ◽  
Y Dai ◽  
S Fleischer
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Channels ◽  
Cell Line ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Contractile Protein ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Receptor Mrnas

The ryanodine receptor/junctional channel complex (JCC) forms the calcium release channel and foot structures of the sarcoplasmic reticulum. The JCC and the dihydropyridine (DHP) receptor in the transverse tubule are two of the major components involved in excitation-contraction (E-C) coupling in skeletal muscle. The DHP receptor is believed to serve as the voltage sensor in E-C coupling. Both the JCC and DHP receptor, as well as many skeletal muscle-specific contractile protein genes, are expressed in the BC3H1 muscle cell line. In the present study, we find that during differentiation of BC3H1 cells, induced by mitogen withdrawal, induction of the JCC and DHP receptor mRNAs is temporally similar to that of the skeletal muscle contractile protein genes alpha-tropomyosin and alpha-actin. Our data suggest that there is coordinate regulation of both the contractile protein genes (which have been studied in detail previously) and the genes encoding the calcium channels involved in E-C coupling. Induction of both calcium channels is accompanied by profound changes in BC3H1 cell morphology including the development of many components of mature skeletal muscle cells, despite lack of myoblast fusion. Visualized by electron microscopy, the JCC appears as "foot structures" located in the dyad junction between the plasmalemma and the sarcoplasmic reticulum of the BC3H1 cells. Development of foot structures is concomitant with JCC mRNA expression. Expression of the JCC and DHP receptor mRNAs and formation of the foot structures are inhibited specifically by fibroblast growth factor.

scholarly journals Effect of gadolinium on the ryanodine receptor/sarcoplasmic reticulum calcium release channel of skeletal muscle

FEBS Journal ◽  
2004 ◽  
Vol 272 (2) ◽  
pp. 464-471 ◽  
Author(s):  
Sándor Sárközi ◽  
Csaba Szegedi ◽  
Balázs Lukács ◽  
Michel Ronjat ◽  
István Jóna
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Sarcoplasmic Reticulum Calcium
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