Calreticulin inhibits commitment to adipocyte differentiation
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Post-publication record
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Abstract
Calreticulin, an endoplasmic reticulum (ER) resident protein, affects many critical cellular functions, including protein folding and calcium homeostasis. Using embryonic stem cells and 3T3-L1 preadipocytes, we show that calreticulin modulates adipogenesis. We find that calreticulin-deficient cells show increased potency for adipogenesis when compared with wild-type or calreticulin-overexpressing cells. In the highly adipogenic crt(-/-) cells, the ER lumenal calcium concentration was reduced. Increasing the ER lumenal calcium concentration led to a decrease in adipogenesis. In calreticulin-deficient cells, the calmodulin-Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) pathway was up-regulated, and inhibition of CaMKII reduced adipogenesis. Calreticulin inhibits adipogenesis via a negative feedback mechanism whereby the expression of calreticulin is initially up-regulated by peroxisome proliferator-activated receptor gamma (PPAR gamma). This abundance of calreticulin subsequently negatively regulates the expression of PPAR gamma, lipoprotein lipase, CCAAT enhancer-binding protein alpha, and aP2. Thus, calreticulin appears to function as a Ca(2+)-dependent molecular switch that regulates commitment to adipocyte differentiation by preventing the expression and transcriptional activation of critical proadipogenic transcription factors.
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The record
- Venue
- The Journal of Cell Biology
- Topic
- Endoplasmic Reticulum Stress and Disease
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- University of AlbertaUniversity of Toronto
- Funders
- —
- Keywords
- CalreticulinAdipogenesisBiologyCell biologyEndoplasmic reticulumCalcium-binding proteinMolecular biologyInternal medicineCalcium
- Has abstract in OpenAlex
- yes