Stimulation of Calmodulin Binding to Skeletal Muscle Membrane Proteins by 1,25-Dihydroxy-Vitamin D 3

1990 ◽  
Vol 45 (6) ◽  
pp. 663-670 ◽  
Author(s):  
Virginia Massheimer ◽  
Luis M. Fernandez ◽  
Ana R. de Boland
Keyword(s):  
Skeletal Muscle ◽  
Vitamin D ◽  
Membrane Proteins ◽  
Binding Proteins ◽  
Sodium Dodecyl ◽  
Muscle Membrane ◽  
Calmodulin Binding ◽  
Ca Uptake ◽  
Vitamin D 3 ◽  
Stimulation Of

Abstract Previous work has shown that 1,25-dihydroxy-vitamin D 3 rapidly increases calmodulin levels of skeletal muscle membranes without altering the muscle cell calmodulin content. Therefore, the effects of the sterol on the binding of calmodulin to specific muscle membrane proteins were investigated. Soleus muscles from vitamin D-deficient chicks were treated in vitro for short intervals (5-15 min) with physiological concentrations of 1,25-dihydroxy-vitamin D3. Proteins of mitochondria and microsomes isolated by differential centrifugation were separated on sodium dodecyl sulfate polyacrylamide gels. Calmodulin-binding proteins were identified by a [125I]calmodulin gel overlay procedure followed by autoradiography. 1,25-Dihydroxy- vitamin D3 increased the binding of labelled calmodulin to a major, calcium-independent, calmodulin-binding protein of 28 Kda localized in microsomes, and to minor calmodulin- binding proteins of 78 and 130 Kda proteins localized in mitochondria. The binding of [125I]calmodulin to these proteins was abolished by flufenazine or excess non-radioactive calmodulin. 1,25-Dihydroxy-vitamin D3 rapidly increased muscle tissue Ca uptake and cyclic AM P levels and stimulated the phosphorylation of several membrane proteins including those whose calmodulin-binding capacity potentiates. Analogously to the sterol, forskolin increased membrane calmodulin content, calmodulin binding to the 28 Kda microsomal protein and 45Ca uptake by soleus muscle preparations. Forskolin also induced a similar profile of changes in muscle membrane protein phosphorylation as the hormone. These results suggest that 1,25- dihydroxy-vitamin D 3 affects calmodulin distribution in muscle cells through cyclic AMP-dependent phosphorylation of membrane calmodulin-binding proteins. These changes may play a role in the stimulation of muscle Ca uptake by the sterol.

Excitation-induced Ca2+uptake in rat skeletal muscle

1999 ◽  
Vol 276 (2) ◽  
pp. R331-R339 ◽  
Author(s):  
H. Gissel ◽  
T. Clausen
Keyword(s):  
Skeletal Muscle ◽  
Electrical Stimulation ◽  
Initial Rate ◽  
Low Frequency ◽  
Channel Blockers ◽  
Ca Uptake ◽  
Edl Muscle ◽  
Isotonic Contractions ◽  
Progressive Accumulation ◽  
Stimulation Of

In isolated rat extensor digitorum longus (EDL) muscle mounted for isometric contractions, chronic low-frequency electrical stimulation was found to lead to an increased uptake of45Ca (154% above control after 240 min) and a progressive accumulation of Ca2+ (85% above control after 240 min). In soleus, however, this treatment led to a small, but significant, increase in 45Ca uptake (30% above control after 180 min) but no significant accumulation of Ca2+. In muscles mounted for isotonic contractions without any external load, electrical stimulation gave rise to a larger45Ca uptake and accumulation of Ca2+ in both EDL and soleus. These uptakes of Ca2+ coincided with an accumulation of Na+. During isometric or isotonic contractions, stimulation at 40 Hz increased the initial (60 s) rate of 45Ca uptake in soleus muscle 15- and 30-fold, respectively. The stimulation-induced increase in 45Ca uptake was only reduced by 17% by the Ca2+-channel blockers nifedipine and verapamil but was blocked by tetrodotoxin. The initial rate of stimulation-induced 22Na and45Ca uptake was correlated ( r = 0.80; P < 0.003). Stimulation of Na+ channels with veratridine increased 45Ca uptake by 93 and 139% in soleus and EDL, respectively ( P < 0.001), effects that were abolished by tetrodotoxin. The results indicate that in skeletal muscle, excitation induces a considerable influx of Ca2+, mediated by Na+ channels.

1,25-Dihydroxyvitamin D-stimulated calmodulin binding proteins: a sustained effect on distal tubules

2002 ◽  
Vol 282 (1) ◽  
pp. F77-F84 ◽  
Author(s):  
Emmanuel K. O. Siaw ◽  
Marian R. Walters
Keyword(s):  
Vitamin D ◽  
Time Course ◽  
Binding Proteins ◽  
Day Treatment ◽  
Rat Kidney ◽  
Vitamin D Receptors ◽  
Dihydroxyvitamin D ◽  
Calmodulin Binding ◽  
1,25 Dihydroxyvitamin D

The tubular localization of 1,25-dihydroxyvitamin D[1,25(OH)2D3]-stimulated calmodulin binding proteins (CaMBP-Ds) in the rat kidney and the specificity of their induction were characterized to better understand renal responses to protracted 1,25(OH)2D3 treatment in vivo. None of the other hormones tested (parathyroid hormone, calcitonin, estradiol-17β, testosterone, progesterone, hydrocortisone, or dexamethasone) stimulated the CaMBP-Ds, whereas maximal 1,25(OH)2D3 stimulation occurred after a 5- to 7-day treatment with 100 ng/day 1,25(OH)2D3. With the exception of the more ubiquitously distributed CaMBP-D150, the CaMBP-Ds were localized in distal, but not proximal, tubule preparations. 1,25(OH)2D3 induction of vitamin D receptors and the CaMBP-Ds was similar with respect to dose-response and time course. Finally, the CaMBP-Ds remained elevated for at least 4 wk after 1,25(OH)2D3 withdrawal. Because the vitamin D-stimulated renal CaMBP-Ds are principally proteins of the distal tubule, they may be associated with renal regulation of Ca2+ homeostasis. The sustained induction of CaMBP-Ds is important in addressing the question of whether their induction is a function of normal Ca2+ homeostasis or a pathophysiological consequence of hypervitaminosis D and hypercalcemia.

scholarly journals Cachectin/tumor necrosis factor mediates changes of skeletal muscle plasma membrane potential.

1986 ◽  
Vol 164 (4) ◽  
pp. 1368-1373 ◽  
Author(s):  
K J Tracey ◽  
S F Lowry ◽  
B Beutler ◽  
A Cerami ◽  
J D Albert ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Transmembrane Potential ◽  
Muscle Membrane ◽  
Membrane Function ◽  
Muscle Plasma Membrane ◽  
Transmembrane Potential Difference ◽  
Cellular Dysfunction ◽  
Necrosis Factor ◽  
Stimulation Of

Lethal infections are associated with cellular dysfunction as evidenced by a decrease in the resting transmembrane potential difference (Em) of skeletal muscle fibers. Endotoxin stimulation of macrophages evokes production of cachectin, a protein that has been implicated as a mediator of the lethal effects of endotoxemia. In the present study, rat skeletal muscle fiber Em decreased when incubated with recombinant human cachectin. The reduction of Em induced by cachectin occurred in a dose-related fashion and was inhibited by mAb against the monokine. Infusion of cachectin induced a decline of skeletal muscle Em in vivo, and suggests that cachectin may acutely mediate alterations of skeletal muscle membrane function after infection.

Myogenesis of normal and dystrophic chick embryonic skeletal muscle cells in vitro: biosynthesis of plasma membrane proteins

1980 ◽  
Vol 58 (10) ◽  
pp. 1156-1164 ◽  
Author(s):  
Paul C. Holland ◽  
George A. Cates ◽  
Byron S. Wenger ◽  
Barbara L. Raney
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membranes ◽  
Protein Biosynthesis ◽  
Sodium Dodecyl ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Plasma Membrane Proteins ◽  
Dystrophic Muscle

Plasma membranes were prepared from primary cell cultures of normal and genetically dystrophic chick embryonic pectoral muscle. These membranes were analyzed both by one-dimensional sodium dodecyl sulphate – polyacrylamide slab gel electrophoresis and by two-dimensional electrophoresis using isoelectric focusing in the first dimension. No marked and reproducible abnormalities could be detected in the synthesis, or accumulation, of plasma membrane proteins of dystrophic muscle cells maintained in culture for periods of up to 6 days. Analysis of the relative rates of protein turnover, analysis of fucose incorporation into plasma membrane proteins, and comparison of iodinated cell surface proteins also failed to reveal distinct abnormalities in plasma membranes derived from cultured dystrophic muscle cells. Although the results obtained do not rule out an early defect in plasma membrane protein biosynthesis during the development of dystrophic skeletal muscle in vivo, they do demonstrate that the synthesis and assembly of at least the major plasma membrane proteins occur normally during the initial phases of terminal differentiation of isolated dystrophic skeletal muscle cells in tissue culture.

Calmodulin Binding Proteins In Platelet Actomypsin

1981 ◽  
Author(s):  
L Muszbek ◽  
J Harsfalvi
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Binding Proteins ◽  
Troponin I ◽  
Polyacrylamide Gel Electrophoresis ◽  
Regulatory System ◽  
Inhibitory Protein ◽  
Calmodulin Binding ◽  
Actomyosin Complex

Platelet actomyosin (thrombosthenin) possesses a myosin-linked Ca2+ regulation and Ca2+ sensitivity is conferred to it by calmodulin through myosin light chain kinase. Calmodulin binding proteins if they are present in the actomyosin complex may have an important regulatory role in the contractile mechanism of platelet activation. To test this possibility an aceton powder was made from platelet actomyosin and extracted with an 8 M urea containing buffer. The extract was examined for the presence of calmodulin binding proteins by alkaline urea polyacrylamide gel electrophoresis. It was shown by this technique that some proteins in the actomyosin complex can form a Ca2+ dependent complex with both calmodulin and skeletal muscle troponin C (TNC is closely related to calmodulin) even in the presence of 8 M urea. Calmodulin binding proteins could be isolated from the extract by affinity chromatography in 8 M urea on TNC-Agarose column. 3 major proteins of 270 K, 6l K and 23 K molecular weight were eluted by EGTA and each of them was able to bind to calmodulin or TNC if Ca2+was present. At least one of these calmodulin binding proteins exerted a troponin I like effect when tested on reconstituted skeletal muscle actomyosin and the 23 K protein showed a close similarity to troponin I. the inhibitory protein of the actin linked Ca2+ regulatory system in skeletal muscle. It is presumed that calmodulin binding proteins may have a dual role in the regulation of platelet actomyosin. They can inhibit the Ca2+ dependent phosphorylation of myosin light chain and one or more of them may also exert an actin linked inhibitory effect.

scholarly journals Effects of a high fat diet and Metformin on skeletal muscle membrane proteins and fiber size in young mice

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Rachel E Botchlett ◽  
Shih‐Lung Woo ◽  
Hang Xu ◽  
Honggui Li ◽  
Choadong Wu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Membrane Proteins ◽  
High Fat Diet ◽  
Muscle Membrane ◽  
High Fat ◽  
Fiber Size ◽  
Young Mice
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