Abstract
Calreticulin is a 46-kDa Ca 2+-binding chaperone found across a diverse range of species. The protein is involved in the regulation of intracellular Ca 2+ homeostasis and endoplasmic reticulum (ER) Ca 2+ storage capacity. Calreticulin is also an important molecular chaperone involved in “quality control” within secretory pathways. The protein contains structurally and functionally unique domains with specialized functions. Studies on calreticulin knockout mice indicate that the protein is essential in early cardiac development. The protein also plays an important role in autoimmunity and cancer.
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