calreticulin
Dernière mise à jour 18 Aug 2020
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La CALR gene provides instructions for making a multi-functional protein called calreticulin. This protein is found in several parts of the cell, including inside a structure called the endoplasmic reticulum (ER), in the fluid-filled space inside the cell (the cytoplasm), and at the outer surface of the cell. The ER is involved in protein processing and transport, and within this structure, calreticulin plays a role in ensuring the proper folding of newly formed proteins. The ER is also a storage location for charged calcium atoms (calcium ions), and calreticulin is involved in maintaining the correct levels of calcium ions in this structure. Through calcium regulation and other mechanisms, calreticulin is thought to play a role in the control of gene activity, cell growth and division (proliferation) and movement (migration), the attachment of cells to one another (adhesion), and regulation of programmed cell death (apoptosis). The function of this protein is important for immune system function and wound healing.
Normal function
La CALR gene provides instructions for making a multi-functional protein called calreticulin. This protein is found in several parts of the cell, including inside a structure called the endoplasmic reticulum (ER), in the fluid-filled space inside the cell (the cytoplasm), and at the outer surface of the cell. The ER is involved in protein processing and transport, and within this structure, calreticulin plays a role in ensuring the proper folding of newly formed proteins. The ER is also a storage location for charged calcium atoms (calcium ions), and calreticulin is involved in maintaining the correct levels of calcium ions in this structure. Through calcium regulation and other mechanisms, calreticulin is thought to play a role in the control of gene activity, cell growth and division (proliferation) and movement (migration), the attachment of cells to one another (adhesion), and regulation of programmed cell death (apoptosis). The function of this protein is important for immune system function and wound healing.
Conditions referring to this gene or chromosome
Other names
calregulin
calreticulin precursor
cC1qR
CRP55
CRT
endoplasmic reticulum resident protein 60
epididymis secretory sperm binding protein Li 99n
ERp60
FLJ26680
grp60
HACBP
HEL-S-99n
RO
Sicca syndrome antigen A (autoantigen Ro; calreticulin)
SSA
Lectures complémentaires et références
- calreticulin; MedlinePlus, National Library of Medicine.
- Gold LI, Eggleton P, Sweetwyne MT, Van Duyn LB, Greives MR, Naylor SM, Michalak M, Murphy-Ullrich JE. Calreticulin: non-endoplasmic reticulum functions in physiology and disease. FASEB J. 2010 Mar;24(3):665-83. doi: 10.1096/fj.09-145482. Epub 2009 Nov 25.
- Klampfl T, Gisslinger H, Harutyunyan AS, Nivarthi H, Rumi E, Milosevic JD, Them NC, Berg T, Gisslinger B, Pietra D, Chen D, Vladimer GI, Bagienski K, Milanesi C, Casetti IC, Sant'Antonio E, Ferretti V, Elena C, Schischlik F, Cleary C, Six M, Schalling M, Schonegger A, Bock C, Malcovati L, Pascutto C, Superti-Furga G, Cazzola M, Kralovics R. Somatic mutations of calreticulin in myeloproliferative neoplasms. N Engl J Med. 2013 Dec 19;369(25):2379-90. doi: 10.1056/NEJMoa1311347. Epub 2013 Dec 10.
- Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J. 2009 Feb 1;417(3):651-66. doi: 10.1042/BJ20081847.
- Nangalia J, Massie CE, Baxter EJ, Nice FL, Gundem G, Wedge DC, Avezov E, Li J, Kollmann K, Kent DG, Aziz A, Godfrey AL, Hinton J, Martincorena I, Van Loo P, Jones AV, Guglielmelli P, Tarpey P, Harding HP, Fitzpatrick JD, Goudie CT, Ortmann CA, Loughran SJ, Raine K, Jones DR, Butler AP, Teague JW, O'Meara S, McLaren S, Bianchi M, Silber Y, Dimitropoulou D, Bloxham D, Mudie L, Maddison M, Robinson B, Keohane C, Maclean C, Hill K, Orchard K, Tauro S, Du MQ, Greaves M, Bowen D, Huntly BJP, Harrison CN, Cross NCP, Ron D, Vannucchi AM, Papaemmanuil E, Campbell PJ, Green AR. Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2. N Engl J Med. 2013 Dec 19;369(25):2391-2405. doi: 10.1056/NEJMoa1312542. Epub 2013 Dec 10.
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