chaperone; promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis.
ohne Gefährdungspotential
Somatic mutations in calreticulin (CALR) are present in approximately 40% of patients with myeloproliferative neoplasms (MPNs). The CALR mutations associated with MPNs occur exclusively in the last exon of the gene (exon 9). These mutations are insertions and/or deletions that result in a ‘frameshift' to a specific alternative reading frame, leading to the synthesis of a novel C-terminal peptide in the mutants that consists predominantly of positively charged amino acids. Expression of the most prevalent mutant CALR (del52) can induce cytokine independence in Ba/F3 cells. Transgenic mice expressing this mutant CALR developed essential thrombocythemia, a form of MPN.
Die ursächliche Beteiligung des wildtypischen Proteins an der Entstehung von Tumoren ist nicht gezeigt.
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Elf S et al., Cancer Discov. 2016;6(4):368-381.
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