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CALR / Calreticulin

calreticulin

Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin but calreticulin is not a Ro/SS-A antigen. Earlier papers referred to calreticulin as an Ro/SS-A antigen but this was later disproven. Increased autoantibody titer against human calreticulin is found in infants with complete congenital heart block of both the IgG and IgM classes.

Gene Name:	calreticulin
Synonyms:	CALR, Calregulin, CC1qR, CRP55, CRT, CRTC, ERp60, Grp60, RO, SSA, Calreticulin, HACBP
Target Sequences:	NM_004343 NP_004334.1 P27797

Publications (16)

Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells. Woods AJ, Roberts MS, Choudhary J, Barry ST, Mazaki Y, Sabe H, Morley SJ, Critchley DR, Norman JC. The Journal of biological chemistry. 2002 277:6428-37. (ICC) [PubMed:11704675]

A dominant negative mutation of neuronal connexin 36 that blocks intercellular permeability. Placantonakis D, Cicirata F, Welsh JP. Brain research. Molecular brain research. 2002 98:15-28. (ICC) [PubMed:11834292]

C1q-calreticulin induced oxidative neurotoxicity: relevance for the neuropathogenesis of Alzheimer's disease. Luo X, Weber GA, Zheng J, Gendelman HE, Ikezu T. Journal of neuroimmunology. 2003 135:62-71. [PubMed:12576225]

Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility. Ho HC, Suarez SS. Biology of reproduction. 2003 68:1590-6. (ICC; Bovine) [PubMed:12606347]

Calreticulin--an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix. Somogyi E, Petersson U, Hultenby K, Wendel M. Matrix biology : journal of the International Society for Matrix Biology. 2003 22:179-91. [PubMed:12782144]

Novel role of phospholipase C-delta1: regulation of liver mitochondrial Ca2+ uptake. Knox CD, Belous AE, Pierce JM, Wakata A, Nicoud IB, Anderson CD, Pinson CW, Chari RS. American journal of physiology. Gastrointestinal and liver physiology. 2004 287:G533-40. (WB; Rat) [PubMed:15107298]

Transient calnexin interaction confers long-term stability on folded K+ channel protein in the ER. Khanna R, Lee EJ, Papazian DM. Journal of cell science. 2004 117:2897-908. (WB; Human) [PubMed:15161937]

Human FK506 binding protein 65 is associated with colorectal cancer. Olesen SH, Christensen LL, Srensen FB, Cabezn T, Laurberg S, Orntoft TF, Birkenkamp-Demtrder K. Molecular & cellular proteomics : MCP. 2005 4:534-44. (ICC, IHC, WB; Human) [PubMed:15671042]

A splice variant of the TCR zeta mRNA lacking exon 7 leads to the down-regulation of TCR zeta, the TCR/CD3 complex, and IL-2 production in systemic lupus erythematosus T cells. Tsuzaka K, Setoyama Y, Yoshimoto K, Shiraishi K, Suzuki K, Abe T, Takeuchi T. Journal of immunology (Baltimore, Md. : 1950). 2005 174:3518-25. (ICC; Mouse) [PubMed:15749888]

ATP-sensitive K+-channel subunits on the mitochondria and endoplasmic reticulum of rat cardiomyocytes. Zhou M, Tanaka O, Sekiguchi M, He HJ, Yasuoka Y, Itoh H, Kawahara K, Abe H. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 2005 53:1491-500. (WB; Rat) [PubMed:15983113]

Impaired megakaryocytopoiesis in type 2B von Willebrand disease with severe thrombocytopenia. Nurden P, Debili N, Vainchenker W, Bobe R, Bredoux R, Corvazier E, Combrie R, Fressinaud E, Meyer D, Nurden AT, Enouf J. Blood. 2006 108:2587-95. (WB; Human) [PubMed:16720832]

Identification of human T cell leukemia virus type 1 tax amino acid signals and cellular factors involved in secretion of the viral oncoprotein. Jain P, Mostoller K, Flaig KE, Ahuja J, Lepoutre V, Alefantis T, Khan ZK, Wigdahl B. The Journal of biological chemistry. 2007 282:34581-93. (WB) [PubMed:17897946]

C1q enhances IFN-gamma production by antigen-specific T cells via the CD40 costimulatory pathway on dendritic cells. Baruah P, Dumitriu IE, Malik TH, Cook HT, Dyson J, Scott D, Simpson E, Botto M. Blood. 2009 113:3485-93. (ICC) [PubMed:19171874]

Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. Anderson DJ, Vargas JD, Hsiao JP, Hetzer MW. The Journal of cell biology. 2009 186:183-91. (ICC, WB) [PubMed:19620630] [PMC:PMC2717638]

Enhanced Protein Secretion From Insect Cells by Co-Expression of the Chaperone Calreticulin and Translation Initiation Factor eIF4E. Teng CY, Chang SL, van Oers MM, Wu TY. Molecular biotechnology. 2013 54:68-78. (WB) [PubMed:22555850]

a-Synuclein and ß-synuclein enhance secretion protein production in baculovirus expression vector system. Teng CY, Chang SL, Tsai MF, Wu TY. Applied microbiology and biotechnology. 2013 (WB) [PubMed:23314197]

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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).

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