Shortening-Deactivation and Stretch-Activation During Spontaneous Contraction and Relaxation of Bivalve Cardiac Muscles

Author(s):  
C. Pizza ◽  
A. Donoian ◽  
S. Booker ◽  
Ying Sun
2000 ◽  
Vol 203 (18) ◽  
pp. 2713-2722 ◽  
Author(s):  
R.K. Josephson ◽  
J.G. Malamud ◽  
D.R. Stokes

The asynchronous muscles of insects are characterized by asynchrony between muscle electrical and mechanical activity, a fibrillar organization with poorly developed sarcoplasmic reticulum, a slow time course of isometric contraction, low isometric force, high passive stiffness and delayed stretch activation and shortening deactivation. These properties are illustrated by comparing an asynchronous muscle, the basalar flight muscle of the beetle Cotinus mutabilis, with synchronous wing muscles from the locust, Schistocerca americana. Because of delayed stretch activation and shortening deactivation, a tetanically stimulated beetle muscle can do work when subjected to repetitive lengthening and shortening. The synchronous locust muscle, subjected to similar stimulation and length change, absorbs rather than produces work.


Author(s):  
J.P. Schroeter ◽  
M.A. Goldstein ◽  
J.P. Bretaudiere ◽  
L.H. Michael ◽  
R.L. Sass

We have recently established the existence of two structural states of the Z band lattice in cross section in cardiac as well as in skeletal muscle. The two structural states are related to the contractile state of the muscle. In skeletal muscle at rest, the Z band is in the small square (ss) lattice form, but tetanized muscle exhibits the basket weave (bw) form. In contrast, unstimu- lated cardiac muscle exhibits the bw form, but cardiac muscles exposed to EGTA show the ss form.We have used two-dimensional computer enhancement techniques on digitized electron micrographs to compare each lattice form as it appears in both cardiac and skeletal muscle. Both real space averaging and fourier filtering methods were used. Enhanced images were displayed as grey-scale projections, as contour maps, and in false color.There is only a slight difference between the lattices produced by the two different enhancement techniques. Thus the information presented in these images is not likely to be an artifact of the enhancement algorithm.


1971 ◽  
Vol 49 (3) ◽  
pp. 883-898 ◽  
Author(s):  
A. Nakamura ◽  
F. Sreter ◽  
J. Gergely

Tryptic and chymotryptic light meromyosin paracrystals from red and cardiac muscles of rabbit show a negative and positive staining pattern with uranyl acetate and phosphotungstate that sharply differs from that of white muscle light meromyosin paracrystals. The main periodicity of about 430 A is the same regardless of the source of light meromyosin. The results are discussed in terms of the molecular structure and the functional properties of various myosins.


2014 ◽  
Vol 115 (2) ◽  
pp. 263-272 ◽  
Author(s):  
Johanna Schleifenbaum ◽  
Mario Kassmann ◽  
István András Szijártó ◽  
Hantz C. Hercule ◽  
Jean-Yves Tano ◽  
...  

1983 ◽  
Vol 258 (13) ◽  
pp. 8395-8401
Author(s):  
K Yamamoto ◽  
C Moos
Keyword(s):  

2020 ◽  
Vol 168 (2) ◽  
pp. 125-137 ◽  
Author(s):  
Eri Ohto-Fujita ◽  
Saaya Hayasaki ◽  
Aya Atomi ◽  
Soichiro Fujiki ◽  
Toshiyuki Watanabe ◽  
...  

Abstract αB-crystallin is highly expressed in the heart and slow skeletal muscle; however, the roles of αB-crystallin in the muscle are obscure. Previously, we showed that αB-crystallin localizes at the sarcomere Z-bands, corresponding to the focal adhesions of cultured cells. In myoblast cells, αB-crystallin completely colocalizes with microtubules and maintains cell shape and adhesion. In this study, we show that in beating cardiomyocytes α-tubulin and αB-crystallin colocalize at the I- and Z-bands of the myocardium, where it may function as a molecular chaperone for tubulin/microtubules. Fluorescence recovery after photobleaching (FRAP) analysis revealed that the striated patterns of GFP-αB-crystallin fluorescence recovered quickly at 37°C. FRAP mobility assay also showed αB-crystallin to be associated with nocodazole-treated free tubulin dimers but not with taxol-treated microtubules. The interaction of αB-crystallin and free tubulin was further confirmed by immunoprecipitation and microtubule sedimentation assay in the presence of 1–100 μM calcium, which destabilizes microtubules. Förster resonance energy transfer analysis showed that αB-crystallin and tubulin were at 1–10 nm apart from each other in the presence of colchicine. These results suggested that αB-crystallin may play an essential role in microtubule dynamics by maintaining free tubulin in striated muscles, such as the soleus or cardiac muscles.


1994 ◽  
Vol 24 (7) ◽  
pp. 1769-1778 ◽  
Author(s):  
R.Douglas Ensley ◽  
Martha Ives ◽  
Liping Zhao ◽  
Mischelle McMillan ◽  
Jane Shelby ◽  
...  

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