Michal Opas

TL;DR: Calreticulin is a highly versatile lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors, integrins and transporters.

TL;DR: Calreticulin has been implicated to play a role in many biological systems, including functions inside and outside the ER, indicating that the protein is a multi-process molecule.

TL;DR: It is shown that the calreticulin gene is highly activated in the cardiovascular system during the early stages of cardiac development, and plays a role in cardiac development as a component of the Ca2+/calcineurin/NF-AT/GATA-4 transcription pathway.

TL;DR: Changes in Ca(2+) concentration may play a signaling role in the lumen of the endoplasmic reticulum as well as in the cytosol, and recent studies on calreticulin-deficient and transgenic mice have revealed that calretiulin and the endplasmic Reticulum may be upstream regulators in the Ca( 2+)-dependent pathways that control cellular differentiation and/or organ development.

TL;DR: The protein has well-recognized physiological roles in the ER as a molecular chaperone and Ca(2+)-signalling molecule, but it has also been found in other membrane-bound organelles, at the cell surface and in the extracellular environment, where it has recently been shown to exert a number of physiological and pathological effects.