Immunogold-labeled L-type Calcium Channels are Clustered in the Surface Plasma Membrane Overlying Junctional Sarcoplasmic Reticulum in Guinea-pig Myocytes—Implications for Excitation–contraction Coupling in Cardiac Muscle

2000 ◽  
Vol 32 (11) ◽  
pp. 1981-1994 ◽  
Author(s):  
David V Gathercole ◽  
David J Colling ◽  
Jeremy N Skepper ◽  
Yoshiko Takagishi ◽  
Allan J Levi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Sarcoplasmic Reticulum ◽  
Guinea Pig ◽  
Calcium Channels ◽  
Cardiac Muscle ◽  
Surface Plasma ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Junctional Sarcoplasmic Reticulum

scholarly journals The recombinant dihydropyridine receptor II–III loop and partly structured ‘C’ region peptides modify cardiac ryanodine receptor activity

2005 ◽  
Vol 385 (3) ◽  
pp. 803-813 ◽  
Author(s):  
Angela F. DULHUNTY ◽  
Yamuna KARUNASEKARA ◽  
Suzanne M. CURTIS ◽  
Peta J. HARVEY ◽  
Philip G. BOARD ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Secondary Structure ◽  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Structure Analysis ◽  
Room Temperature ◽  
Random Coil ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling

A physical association between the II–III loop of the DHPR (dihydropryidine receptor) and the RyR (ryanodine receptor) is essential for excitation–contraction coupling in skeletal, but not cardiac, muscle. However, peptides corresponding to a part of the II–III loop interact with the cardiac RyR2 suggesting the possibility of a physical coupling between the proteins. Whether the full II–III loop and its functionally important ‘C’ region (cardiac DHPR residues 855–891 or skeletal 724–760) interact with cardiac RyR2 is not known and is examined in the present study. Both the cardiac DHPR II–III loop (CDCL) and cardiac peptide (Cc) activated RyR2 channels at concentrations >10 nM. The skeletal DHPR II–III loop (SDCL) activated channels at ≤100 nM and weakly inhibited at ≥1 μM. In contrast, skeletal peptide (Cs) inhibited channels at all concentrations when added alone, or was ineffective if added in the presence of Cc. Ca2+-induced Ca2+ release from cardiac sarcoplasmic reticulum was enhanced by CDCL, SDCL and the C peptides. The results indicate that the interaction between the II–III loop and RyR2 depends critically on the ‘A’ region (skeletal DHPR residues 671–690 or cardiac 793–812) and also involves the C region. Structure analysis indicated that (i) both Cs and Cc are random coil at room temperature, but, at 5 °C, have partial helical regions in their N-terminal and central parts, and (ii) secondary-structure profiles for CDCL and SDCL are similar. The data provide novel evidence that the DHPR II–III loop and its C region interact with cardiac RyR2, and that the ability to interact is not isoform-specific.

scholarly journals Localization of Ca2+ + Mg2+-ATPase of the sarcoplasmic reticulum in adult rat papillary muscle.

1982 ◽  
Vol 93 (3) ◽  
pp. 883-892 ◽  
Author(s):  
A O Jorgensen ◽  
A C Shen ◽  
P Daly ◽  
D H MacLennan
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cardiac Muscle ◽  
Papillary Muscle ◽  
Functional Role ◽  
Transverse Tubules ◽  
Contraction Coupling ◽  
Adult Rat ◽  
Sarcoplasmic Reticulum Membrane ◽  
Rat Papillary Muscle ◽  
Junctional Sarcoplasmic Reticulum

Localization of the Ca2+ + Mg2+-ATPase of the sarcoplasmic reticulum in rat papillary muscle was determined by indirect immunofluorescence and immunoferritin labeling of cryostat and ultracryotomy sections, respectively. The Ca2+ + Mg2+-ATPase was found to be rather uniformly distributed in the free sarcoplasmic reticulum membrane but to be absent from both peripheral and interior junctional sarcoplasmic reticulum membrane, transverse tubules, sarcolemma, and mitochondria. This suggests that the Ca2+ + Mg2+-ATPase of the sarcoplasmic reticulum is antigenically unrelated to the Ca2+ + Mg2+-ATPase of the sarcolemma. These results are in agreement with the idea that the sites of interior and peripheral coupling between sarcoplasmic reticulum membrane and transverse tubules and between sarcoplasmic reticulum and sarcolemmal membranes play the same functional role in the excitation-contraction coupling in cardiac muscle.

Junctional Sarcoplasmic Reticulum in Excitation-Contraction-Coupling

1982 ◽  
Vol 40 ◽  
pp. 136-137
Author(s):  
J.R. Sommer ◽  
E. Bossen ◽  
A. Fabiato
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Action Potential ◽  
Muscle Contraction ◽  
Cardiac Cells ◽  
Close Apposition ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Terminal Cisterna ◽  
Voltage Dependent ◽  
Junctional Sarcoplasmic Reticulum

The junctional sarcoplasmic reticulum (JSR, syn. terminal cisterna) is implicated in Ca++storage and release for muscle contraction. Its discrete ultrastructure permits distinction from the rest of the SR (free SR) even when it occurs without plasmalemmal contact, e.g. as extended JSR (EJSR) in bird, and corbular SR (CSR) in mammalian cardiac cells. The close apposition of JSR to plasmalemma via junctional processes is central to proposed mechanisms of translating voltage-dependent charge transfers at the plasmalemma during the action potential into Ca++release from the JSR. These hypotheses are put into question by the existence of EJSR (and CSR) which in birds constitutes 70-80% of the total JSR. An alternate hypothesis proposes, at least for cardiac cells, that Ca++entering the cell during excitation causes additional Ca++to be freed intracellularly. The notion of a chemical transmitter acting by diffusion is attractive because it will allow for the anomalous topography of EJSR, especially since bird cardiac cells have only about half the diameter of their mammalian relatives and have no transverse tubules.

scholarly journals CARDIAC MUSCLE

1968 ◽  
Vol 36 (3) ◽  
pp. 497-526 ◽  
Author(s):  
Joachim R. Sommer ◽  
Edward A. Johnson
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Guinea Pig ◽  
Cardiac Muscle ◽  
Extracellular Space ◽  
Light And Electron Microscopy ◽  
Rabbit Heart ◽  
Contraction Coupling ◽  
The Difference

With light and electron microscopy a comparison has been made of the morphology of ventricular (V) and Purkinje (P) fibers of the hearts of guinea pig, rabbit, cat, dog, goat, and sheep. The criteria, previously established for the rabbit heart, that V fibers are distinguished from P fibers by the respective presence and absence of transverse tubules is shown to be true for all animals studied. No evidence was found of a permanent connection between the sarcoplasmic reticulum and the extracellular space. The sarcoplasmic reticulum (SR) of V fibers formed couplings with the sarcolemma of a transverse tubule (interior coupling) and with the peripheral sarcolemma (peripheral coupling), whereas in P fibers the SR formed only peripheral couplings. The forms of the couplings were identical. The significance, with respect to excitation-contraction coupling, of the difference in the form of the couplings in cardiac versus skeletal muscle is discussed together with the electrophysiological implications of the differing geometries of bundles of P fibers from different animals.

Voltage Sensors and Calcium Channels of Excitation-Contraction Coupling

Physiology ◽  
1988 ◽  
Vol 3 (6) ◽  
pp. 223-227 ◽  
Author(s):  
E Rios ◽  
G Pizarro
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Channels ◽  
Action Potential ◽  
Structural Data ◽  
Excitation Contraction Coupling ◽  
Voltage Sensors ◽  
Contraction Coupling ◽  
Chemical Mediation ◽  
Mechanical Connection

Three mechanisms are proposed for the transduction from action potential to Ca2+ release from the sarcoplasmic reticulum in skeletal muscle: Chemical mediation, a mechanical connection between transverse tubular membrane and sacroplasmic reticulum, and Ca2+-induced release of Ca2+. New biochemical, biophysical, and structural data favor a mechanical connection and add the possibility that Ca2+-induced Ca2+-release is working in parallel.

Avian Extended Junctional SR: 3-D Geometry Rendered in Stereo

1997 ◽  
Vol 3 (S2) ◽  
pp. 247-248
Author(s):  
J.R. Sommer ◽  
T. High ◽  
P. Ingram ◽  
D. Kopf ◽  
R. Nassar ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Muscle Contraction ◽  
Cardiac Myocytes ◽  
Ryanodine Receptor ◽  
Transverse Tubules ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Junctional Sarcoplasmic Reticulum ◽  
Invariant Differentiation

Extended junctional sarcoplasmic reticulum (EJSR) is an invariant differentiation of the sarcoplasmic reticulum (SR) in bird cardiac myocytes (CM) and central to excitation-contraction coupling (ECC). EJSR occurs as both continuous and discontinuous extensions of junctional sarcoplasmic reticulum (JSR), and surrounds and pervades the Z/I band as the “ EJSR Z-rete” whose geometry has mechanistic implications for the function of “couplings” in ECC, in general. “Peripheral coupling(s)” (PC) in birds, and the additional “interior coupling(s)” (IC) at transverse tubules (TT) in mammals, are formed by tight apposition to plasmalemma of JSR, a specialized calcium (Ca) store of the SR. Free SR (FSR; i.e. free of JSR/EJSR specializations) is the rest of the smooth, tubular SR network, which connects intercalated patches of EJSR forming the EJSR Z-retes and, elsewhere, displays both longitudinal and transverse geometries in surrounding the contractile material for the purpose of sequestering Ca after each muscle contraction. Except for EJSR having no plasmalemmal contact, morphologically, EJSR and JSR are homologues:1 both have similar sizes; are studded (approx. 32 nm center-to-center) with junctional processes (JP; ryanodine receptor (RyR)/-Ca-release channels);

Calcium release from cardiac sarcoplasmic reticulum induced by photorelease of calcium or Ins(1,4,5)P3

1990 ◽  
Vol 258 (2) ◽  
pp. H610-H615 ◽  
Author(s):  
J. C. Kentish ◽  
R. J. Barsotti ◽  
T. J. Lea ◽  
I. P. Mulligan ◽  
J. R. Patel ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cardiac Muscle ◽  
Calcium Release ◽  
Force Response ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Excitation Contraction Coupling ◽  
Caged Compounds ◽  
Contraction Coupling ◽  
Inositol 1,4,5 Trisphosphate ◽  
Ventricular Trabeculae

The ability of Ca2+ or inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] to release Ca2+ from cardiac sarcoplasmic reticulum (SR) was investigated using saponin-skinned ventricular trabeculae from rats. To overcome diffusion delays, rapid increases in the concentrations of Ca2+ and Ins(1,4,5)P3 were produced by laser photolysis of “caged Ca2+” (Nitr-5) and “caged Ins(1,4,5)P3”. Photolysis of Nitr-5 to produce a small jump in [Ca2+] from pCa 6.8 to 6.4 induced a large and rapid force response (t1/2 = 0.89 s at 12 degrees C); the source of the Ca2+ that activated the myofibrils was judged to be the SR, since it was blocked by 0.1 mM ryanodine or 5 mM caffeine. A smaller, slower, and less consistent release of SR Ca2+ was produced by photorelease of Ins(1,4,5)P3. The results demonstrate that these caged compounds can be used to study excitation-contraction coupling in skinned multicellular preparations of cardiac muscle. The data are consistent with a major role for Ca2(+)-induced Ca2+ release in cardiac activation, whereas the role for Ins(1,4,5)P3 may be to modulate, rather than directly stimulate, SR Ca2+ release.

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