Linked Life Data

18255058

Source:http://linkedlifedata.com/resource/pubmed/id/18255058

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pubmed-article:18255058pubmed:abstractTextWe studied the phosphorylation (activation status) of c-Src and CaMKII in MEFs either wild type for calreticulin, calreticulin-null, or rescued with full-length calreticulin. We found that calreticulin-null cells were poorly spread on the substratum and formed few, if any, focal contacts. Fibronectin expression and deposition were lower in calreticulin-null MEFs compared to calreticulin-expressing cells, which also exhibited increased c-Src and CaMKII phosphorylation (activity). Plating MEFs on preformed fibronectin rescued the poor adhesive phenotype of calreticulin-null cells, and caused a decrease in c-Src Y418 phosphorylation (activity). c-Src inhibition caused the calreticulin-null MEFs to become well spread on the substratum and to make many prominent focal contacts. Calmodulin and CaMKII inhibition caused similar results, along with a notable increase in paxillin phosphorylation (activation). To test if the calcium storage function of calreticulin was responsible for these effects, we manipulated intracellular [Ca(2+)]. Lowering [Ca(2+)](ER) caused an increase in c-Src phosphorylation and a decrease in fibronectin abundance. Conversely, increasing [Ca(2+)] caused opposite effects. These results suggest that calreticulin regulates both the c-Src and calmodulin/CaMKII pathways, enabling cells to be better spread on the substratum by allowing greater fibronectin deposition and increased focal contact formation.lld:pubmed
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pubmed-article:18255058pubmed:articleTitleKinase-dependent adhesion to fibronectin: regulation by calreticulin.lld:pubmed
pubmed-article:18255058pubmed:affiliationDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.lld:pubmed
pubmed-article:18255058pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18255058pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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