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  • Sarcoplasmic reticulum  (2)
  • Ca^2^+  (1)
  • Electronopaque diffusion tracers  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism 750 (1983), S. 134-140 
    ISSN: 0005-2760
    Keywords: (Rat aorta muscle cell) ; Ca^2^+ ; Phospholipase A"2
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 200 (1979), S. 367-382 
    ISSN: 1432-0878
    Keywords: Ruthenium red ; Skeletal muscle ; Cardiac muscle ; Membrane permeability ; Sarcoplasmic reticulum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effects of ruthenium red (RR) on amphibian and mammalian skeletal muscles and mammalian myocardium were examined. In skeletal muscle cells, a discrete pattern of staining can be brought about within the lumina of the terminal cisternae (junctional sarcoplasmic reticulum [SR]) by sequential exposure to RR and OsO4. After prolonged immersion in RR solution, formation of pentalaminar segments (“zippering”) occurs at various points along the longitudinal (“network”) SR tubules. Zippering can be elicited in skeletal SR at any stage of preparation prior to postfixation with OsO4. By means of dispersive X-ray analysis, both ruthenium and osmium were seen to be deposited in skeletal muscle junctional SR, and ruthenium was detected in the myoplasm as well. In skeletal muscles whose T tubules were ruptured by exposure to glycerol, the pattern of SR staining and zippering resulting from ruthenium-osmium treatment was not affected. These findings indicate that RR is capable of passage across the sarcolemma of skeletal muscle and that this passage does not occur solely under conditions in which the plasma membrane is damaged. In contrast, RR does not opacify or modify any region of the SR of cardiac muscle. However, after this treatment, randomly distributed opaque bodies, composed of parallel lamellar structures, appear throughout the myocardial cells. A few of these bodies are associated with lipid droplets, but the rest are of unknown origin. The failure of the SR of cardiac muscle to stain after exposure to ruthenium dye (even though this material enters these cells) suggests that the chemical composition of cardiac SR is significantly different from that of skeletal muscle SR.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 116 (1971), S. 20-36 
    ISSN: 1432-0878
    Keywords: Mammalian cardiac muscle ; T system ; Longitudinal tubules ; Electronopaque diffusion tracers ; Excitation-contraction coupling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Colloidal ThO2 particles (diameter of ∼ 60 Å) were used as electron-opaque markers to trace the “intracellular” compartments continuous with the bulk interstitial fluid of guinea pig ventricular muscle. Beating and quiescent hearts in a Langendorff preparation were perfused for 30 min with oxygenated Ringer solution containing 1% ThO2. The hearts were immediately fixed by perfusing with glutaraldehyde solution. The colloidal ThO2 particles entered into many of the T tubules and into longitudinallyrunning tubules. No differences in distribution of ThO2 were observed in a heart which was not exposed to ThO2 until after it was fixed. Tracer did not penetrate into the intercalated disk clefts in the guinea pig hearts and one frog heart used for comparison. Tubular profiles filled with ThO2 were not seen in frog heart, an observation which confirms the absence of T tubules in this amphibian. It is concluded that, in mammalian cardiac muscle, the lumens of the longitudinal tubules are continuous with the lumens of the T tubules, forming an extensively interconnected T-L tubular system. Hence, every myofibril has close access to a fluid-filled space which is continuous with the interstitial fluid and which may be of similar cationic composition; such an arrangement should facilitate excitation-contraction coupling.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 134 (1972), S. 1-11 
    ISSN: 1432-0878
    Keywords: Muscle ultrastructure ; (Na+, K+)-ATPase localization ; Sarcotubules ; Sarcoplasmic reticulum ; Junctional SR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary ATPase activity sensitive to ouabain was examined in both cardiac (ventricular) and skeletal (tibialis anterior) muscle cells of the mouse. Short-term fixation was combined with incubation in a medium designed to reduce artifactual deposition of lead phosphate. With incubation medium containing Na+ and K+, Pb3 (PO4)2 precipitate appears throughout the sarcoplasmic reticulum (SR) of both cardiac and skeletal cells. The precipitate generally is heavier in the junctional SR than in network SR, although the two regions are interconnected. Ouabain (1 mM) eliminates activity in the network SR of myocardial cells, but only reduces it in skeletal muscle cells. The total ATPase activity of junctional cisternae of the SR of myocardial cells does not appear to be reduced by ouabain, whereas the activity of the terminal cisternae of skeletal muscle is substantially diminished. The use of an incubation medium containing zero K+ reduces the level of activity, but not consistently. These data suggest that (Na+, K+)-ATPase is present in the network SR of both cardiac and skeletal muscle cells, and probably in the terminal cisternae of skeletal muscle cells.
    Type of Medium: Electronic Resource
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