Calcium-modulated contractile proteins associated with the eucaryotic centrosome

1986 ◽  
Vol 6 (2) ◽  
pp. 193-197 ◽  
Author(s):  
J. L. Salisbury ◽  
A. T. Baron ◽  
D. E. Coling ◽  
V. E. Martindale ◽  
M. A. Sanders
Keyword(s):  
Contractile Proteins

Electron Microscopy of Cytoplasmic Contractile Proteins

1978 ◽  
Vol 36 (3) ◽  
pp. 606-614 ◽  
Author(s):  
T.D. Pollard ◽  
P. Maupin
Keyword(s):  
Electron Microscopy ◽  
Actin Filaments ◽  
Three Dimensional ◽  
Uranyl Acetate ◽  
Contractile Proteins ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Cytoplasmic Matrix ◽  
Computer Image Processing ◽  
Nonmuscle Cells

In this paper we review some of the contributions that electron microscopy has made to the analysis of actin and myosin from nonmuscle cells. We place particular emphasis upon the limitations of the ultrastructural techniques used to study these cytoplasmic contractile proteins, because it is not widely recognized how difficult it is to preserve these elements of the cytoplasmic matrix for electron microscopy. The structure of actin filaments is well preserved for electron microscope observation by negative staining with uranyl acetate (Figure 1). In fact, to a resolution of about 3nm the three-dimensional structure of actin filaments determined by computer image processing of electron micrographs of negatively stained specimens (Moore et al., 1970) is indistinguishable from the structure revealed by X-ray diffraction of living muscle.

Platelet Contractile Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1634-1637 ◽  
Author(s):  
Thomas D Pollard
Keyword(s):  
Contractile Proteins

Studies of arterial intimal contractile proteins

1977 ◽  
Vol 9 (11) ◽  
pp. 47-47
Author(s):  
Y. Kira ◽  
K. Ebisawa ◽  
T. Koizumi ◽  
Y. Ito
Keyword(s):  
Contractile Proteins

Endotoxin administration alters the force vs. pCa relationship of skeletal muscle fibers

2000 ◽  
Vol 278 (4) ◽  
pp. R891-R896 ◽  
Author(s):  
G. Supinski ◽  
D. Nethery ◽  
T. M. Nosek ◽  
L. A. Callahan ◽  
D. Stofan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Force ◽  
Fiber Type ◽  
Contractile Proteins ◽  
Hill Coefficient ◽  
Control Group ◽  
Fiber Types ◽  
Endotoxin Administration ◽  
Generating Capacity ◽  
The Hill

Recent work indicates that endotoxemia elicits severe reductions in skeletal muscle force-generating capacity. The subcellular alterations responsible for these decrements have not, however, been fully characterized. One possibility is that the contractile proteins per se are altered in endotoxemia and another is that the mechanism by which these proteins are activated is affected. The purpose of the present study was to assess the effects of endotoxin administration on the contractile proteins by examining the maximum calcium-activated force (Fmax) and calcium sensitivity of single Triton-skinned fibers of diaphragm, soleus, and extensor digitorum longus (EDL) muscles taken from control and endotoxin-treated (8 mg/kg) rats. Fibers were mounted on a force transducer and sequentially activated by serial immersion in solutions of increasing Ca2+ concentration (i.e., pCa 6.0 to pCa 5.0); force vs. pCa data were fit to the Hill equation. All fibers were typed at the conclusion of studies using gel electrophoresis. Fmax, the calcium concentration required for half-maximal activation (Ca50), and the Hill coefficient were compared as a function of muscle and fiber type for the control and endotoxin-treated animals. Control group Fmax was similar for diaphragm, soleus, and EDL fibers, i.e., 112.34 ± 2.64, 111.55 ± 3.66, and 104.05 ± 4.33 kPa, respectively. Endotoxin administration reduced the average Fmax for fibers from all three muscles to 80.25 ± 2.30, 72.47 ± 2.97, and 78.32 ± 2.43 kPa, respectively ( P < 0.001 for comparison of each to control). All fiber types in diaphragm, soleus, and EDL muscles manifested similar endotoxin-related reductions in Fmax. The Ca50 and the Hill coefficient for all fiber types and all muscles were unaffected by endotoxin administration. We speculate that these alterations in the intrinsic properties of the contractile proteins represent a major mechanism by which endotoxemia reduces muscle force-generating capacity.

HSP27 in signal transduction and association with contractile proteins in smooth muscle cells

1999 ◽  
Vol 277 (2) ◽  
pp. G445-G454 ◽  
Author(s):  
Adenike I. Ibitayo ◽  
Jeanette Sladick ◽  
Sony Tuteja ◽  
Otto Louis-Jacques ◽  
Hirotaka Yamada ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Protein Kinase ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Contractile Proteins ◽  
Mitogen Activated Protein Kinase ◽  
Signal Transduction Cascade ◽  
Kinase C ◽  
Mitogen Activated Protein

Sustained smooth muscle contraction is mediated by protein kinase C (PKC) through a signal transduction cascade leading to contraction. Heat-shock protein 27 (HSP27) appears to be the link between these two major events, i.e., signal transduction and sustained smooth muscle contraction. We have investigated the involvement of HSP27 in signal transduction and HSP27 association with contractile proteins (e.g., actin, myosin, tropomyosin, and caldesmon) resulting in sustained smooth muscle contraction. We have carried out confocal microscopy to investigate the cellular reorganization and colocalization of proteins and immunoprecipitation of HSP27 with actin, myosin, tropomyosin, and caldesmon as detected by sequential immunoblotting. Our results indicate that 1) translocation of Raf-1 to the membrane when stimulated with ceramide is inhibited by vasoactive intestinal peptide (VIP), a relaxant neuropeptide; 2) PKC-α and mitogen-activated protein kinase translocate and colocalize on the membrane in response to ceramide, and PKC-α translocation is inhibited by VIP; 3) HSP27 colocalizes with actin when contraction occurs; and 4) HSP27 immunoprecipitates with actin and with the contractile proteins myosin, tropomyosin, and caldesmon. We propose a model in which HSP27 is involved in sustained smooth muscle contraction and modulates the interaction of actin, myosin, tropomyosin, and caldesmon.

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