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| Titel: |
Calreticulin and cellular adhesion/migration-specific signalling pathways |
| Auteur: |
Eva Szabo Sylvia Papp Michal Opas |
| Verschenen in: |
Journal of applied biomedicine |
| Paginering: | Jaargang 4 (2005) nr. 1 pagina's 45-52 |
| Jaar: |
2005 |
| Inhoud: |
Calreticulin is a Ca2+-binding protein of the ER/SR, from where it acts as a chaperone, and affectscalcium homeostasis, gene expression and cell adhesion. Cell adhesion to the extracellular matrix cangenerate transmembrane signals important for cell survival and migration. In a variety of cell types,integrin stimulation by ECM proteins, such as fibronectin, leads to changes in intracellular proteintyrosine phosphorylation. Tyrosine phosphorylation leads to the co-localization of focal adhesion kinase,vinculin and paxillin at focal contacts. Interaction between focal adhesion kinase and paxillin is criticalfor the activation of signaling cascades involved in cell survival and motility. Fibroblasts either over- orunderexpressing calreticulin show differences in their adhesive properties, which are related to thecalmodulin/CaMKII pathway. Inhibition of these pathways causes the weekly adhesive calreticulinunderexpressing cells to behave like the calreticulin overexpressers, through increased spreading andincreased levels of focal adhesion kinase, paxillin and fibronectin. We propose that calreticulin, via itsCa2+-homeostatic effects, may affect fibronectin synthesis and matrix assembly by modulating fibronectingene expression, and by influencing formation of cellular adhesions, both of which are instrumental inmatrix assembly and remodelling. Interestingly, it appears that besides the calmodulin/CaMKII pathway,differential calreticulin expression also modulates the c-src pathway. |
| Uitgever: |
University of South Bohemia (provided by DOAJ) |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
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