scholarly journals Doublet discharge stimulation increases sarcoplasmic reticulum Ca2+release and improves performance during fatiguing contractions in mouse muscle fibres

2013 ◽  
Vol 591 (15) ◽  
pp. 3739-3748 ◽  
Author(s):  
Arthur J. Cheng ◽  
Nicolas Place ◽  
Joseph D. Bruton ◽  
Hans-Christer Holmberg ◽  
Håkan Westerblad

The ultrastructure of the trochanteral depressor muscle of the oriental rat flea is described. It is shown to be similar to that of the tubular leg muscles of other insects except in the volume and arrangement of the sarcoplasmic reticulum. The sarcoplasmic reticulum occupies approximately 18% of the volume of the muscle fibres. It is in three configurations: a regular array of parallel tubules opposite the A-band, a collar of sacculi involved in the formation of the dyads at the edge of the A-band and a loosely woven arrangement of tubules around the I-band. This tripartite arrangement of the sarcoplasmic reticulum and its large surface area is discussed in relation to the action of the muscle as the main propulsive muscle in the jump of the flea.


2008 ◽  
Vol 586 (11) ◽  
pp. 2799-2805 ◽  
Author(s):  
Nicolas Place ◽  
Takashi Yamada ◽  
Joseph D. Bruton ◽  
Håkan Westerblad

1990 ◽  
Vol 240 (1297) ◽  
pp. 197-210 ◽  

Immunolabelling with a 5 nm gold probe was used to localize dystrophin at the ultrastructural level in human muscle. The primary antibody was monoclonal, raised against a segment (amino acids 1181-1388) from the rod domain of dystrophin. The antibody (Dy4/6D3) is specific for dystrophin and shows no immunoreactivity with any protein from mdx mouse muscle or from patients with a gene deletion spanning part of the molecule recognized by the antibody (Nicholson et al . 1989 a ; England et al . 1990). Using this antibody, labelling was almost entirely confined to a narrow 75 nm rim at the periphery of the muscle fibres. Histograms of the distance from the gold probe to the cytoplasmic face of the plasma membrane and of the distance between gold probes (nearest neighbour in a plane parallel with the plasma membrane) displayed modes at approximately 15 nm and 120 nm, respectively. The distribution of the probe was the same in longitudinal and transverse sections of the muscle. These observations suggest that the rod portion of the dystrophin mole­cule is normally arranged close to the cytoplasmic face of the plasma membrane and that the molecules form an interconnecting network. Labelling was not associated with the transverse tubular system.


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