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- Title
Calreticulin: a multiface glycoprotein.
- Authors
Lewandowski, Krzysztof
- Abstract
Calreticulin (CALR) is a highly conserved multi-function protein participating in various cellular processes, including glycoprotein chaperoning, the regulation of Ca2+ homeostasis, antigen processing and presentation for adaptive immune response, cell adhesion/migration, cell proliferation, immunogenic cell death, gene expression and RNA stability. The presence of CALR exon 9 gene mutations [type 1 (del 52nt) and type 2 (ins5nt)] may result in an abnormal CALR structure due to the loss of its ER-retention sequence, CALR extra-ER localisation, and its abnormal function. Recently published data documented that CALRins5 -- in comparison to CALRdel52, differentially activated the inositolrequiring enzyme 1α/Xboxbinding protein 1 pathway of the unfolded protein response system (UPR) to drive malignancy. The RNA sequencing studies confirmed the differential up-regulation of the activating transcription factor 6 (ATF6) in the UPR in CALRins5- versus CALRdel52- and CALRwt expressing cells. Due to the physiological role of CALR and the key role of calcium ions homeostasis and calcium ions flow in platelets, it is possible that CALR mutations are responsible for abnormal CALR-associated cellular storage of calcium ions (including megakaryocytes and platelets) and an increased risk of bleeding during prophylactic administration of aspirin in patients with CALR-mutated myeloproliferative neoplasms.
- Subjects
CALRETICULIN; UNFOLDED protein response; CALCIUM ions; INTRACELLULAR calcium; MYELOPROLIFERATIVE neoplasms; ASPIRIN; MYELOFIBROSIS
- Publication
Acta Haematologica Polonica, 2022, Vol 53, Issue A, p4
- ISSN
0001-5814
- Publication type
Article