Go toArchive
Browse byFacets
Bookbag ( 0 )
'1' in keywords Facet   section ZfN Section C  [X]
Facet   Publication Year 1990  [X]
Results  1 Item
Sorted by   
Publication Year
1Author    Virginia Massheimer, LuisM. Fernandez, AnaR. De BolandRequires cookie*
 Title    Stimulation of Calmodulin Binding to Skeletal Muscle Membrane Proteins by 1,25-Dihydroxy-Vitamin D 3  
 Abstract    Previous work has shown that 1,25-dihydroxy-vitamin D 3 rapidly increases calmodulin lev­ els of skeletal muscle membranes without altering the muscle cell calmodulin content. There­ fore, the effects of the sterol on the binding of calmodulin to specific muscle membrane pro­ teins 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 D 3. Proteins of mitochondria and microsomes isolated by differential centrifugation were sep­ arated on sodium dodecyl sulfate polyacrylamide gels. Calmodulin-binding proteins were identified by a [125I]calmodulin gel overlay procedure followed by autoradiography. 1,25-Di-hydroxy-vitamin D 3 increased the binding of labelled calmodulin to a major, calcium-inde­ pendent, calmodulin-binding protein of 28 Kda localized in microsomes, and to minor calmo­ dulin-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 cal­ modulin. 1,25-Dihydroxy-vitamin D 3 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-de-pendent phosphorylation of membrane calmodulin-binding proteins. These changes may play a role in the stimulation of muscle Ca uptake by the sterol. 
  Reference    Z. Naturforsch. 45c, 663—670 (1990); received October 2/November 3 1989 
  Published    1990 
  Keywords    1, 25-Dihydroxy-Vitamin D 3, Skeletal Muscle, Muscle Membranes, Calmodulin Binding, Protein Phosphorylation 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0663.pdf 
 Identifier    ZNC-1990-45c-0663 
 Volume    45