English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Reversal of decreased phosphorylation of sarcoplasmic reticulum calcium transport ATPase by 1,25-dihydroxycholecalciferol in experimental uremia

MPS-Authors
/persons/resource/persons232373

Boland,  Ricardo
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons232377

Matthews,  Clifford
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons232375

de Boland,  Ana R.
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons232379

Ritz,  Eberhard
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93324

Hasselbach,  Wilhelm
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Boland, R., Matthews, C., de Boland, A. R., Ritz, E., & Hasselbach, W. (1983). Reversal of decreased phosphorylation of sarcoplasmic reticulum calcium transport ATPase by 1,25-dihydroxycholecalciferol in experimental uremia. Calcified Tissue International, 35(1), 195-201. doi:10.1007/BF02405031.


Cite as: https://hdl.handle.net/21.11116/0000-0003-6334-3
Abstract
When compared to that from sham-operated controls, sarcoplasmic reticulum isolated from skeletal muscle of uremic rabbits had a lower rate of calcium uptake and storing capacity. In vivo administration of 1,25-dihydroxycholecalciferol [1,25(OH)2D3] restored the values in uremic animals toward normal. To obtain information about the mechanisms responsible for these differences, phosphorylation of the calcium transport ATPase was studied. The steady-state levels of phosphoprotein in uremic membranes were lower and returned to normal when the secosteroid was administered. Electrophoresis of the membranes phosphorylated with 32P-inosine triphosphate (32P-ITP) showed that the differences were related to a 100,000 dalton protein. The rate of phosphoprotein formation, determined with 32P-ITP and at 0 degrees C, was considerably lower in uremic than in control animals. Pretreatment with 1,25(OH)2D3 prevented this change. The hypothesis is advanced that the vitamin D metabolite affects the steady-state concentration and rate constant of formation of active sites in the Ca-ATPase. These results may partly explain the altered Ca transport function of the sarcoplasmic reticulum in experimental uremia.