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CALR  -  calreticulin

Bos taurus

 
 
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Disease relevance of CALR

 

High impact information on CALR

 

Biological context of CALR

 

Anatomical context of CALR

 

Associations of CALR with chemical compounds

 

Physical interactions of CALR

  • Using RNA mobility shift, UV cross-linking, and in vitro degradation assays, followed by mass-spectrometric analysis, we identified calreticulin as a specific destabilizing trans-acting factor that binds to a 10-nucleotide cis-acting element (CAE(2181-2190)) in the 3'-untranslated region of GLUT-1 mRNA [13].
 

Other interactions of CALR

  • CL-43 as well as conglutinin, binds to the collectin receptor (C1qR) localized on many types of cells identified as a surface variant of calreticulin [14].
  • Inhibition of phospholipase A2 activity by calmodulin, S-100, calregulin, parvalbumin, troponin-C, or CAB-48 was not observed [15].
 

Analytical, diagnostic and therapeutic context of CALR

  • The binding of calreticulin to IgG was used for the development of immunoassay and the relative affinity of the lectin-substrate association was indirectly measured [9].
  • Development of a radioimmunoassay for quantitation of calregulin in bovine tissues [1].
  • Gel permeation chromatography of bovine brain 100 000 g supernatant in the presence or absence of calcium has resolved a single peak of calregulin by RIA [1].
  • Expression analyses of the corresponding gene in different developmental stages and tissues were performed by RT-PCR and Western-blot, which indicated a ubiquitous expression of the B. microplus calreticulin gene and demonstrated its presence in saliva [10].

References

  1. Development of a radioimmunoassay for quantitation of calregulin in bovine tissues. Khanna, N.C., Waisman, D.M. Biochemistry (1986) [Pubmed]
  2. Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum. Trombetta, E.S., Helenius, A. J. Cell Biol. (2000) [Pubmed]
  3. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. Rodan, A.R., Simons, J.F., Trombetta, E.S., Helenius, A. EMBO J. (1996) [Pubmed]
  4. Conformational changes induced by binding of divalent cations to calregulin. Khanna, N.C., Tokuda, M., Waisman, D.M. J. Biol. Chem. (1986) [Pubmed]
  5. Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration. Orr, A.W., Elzie, C.A., Kucik, D.F., Murphy-Ullrich, J.E. J. Cell. Sci. (2003) [Pubmed]
  6. Calreticulin is a binding protein for muramyl dipeptide and peptidoglycan in RK13 cells. Chen, D., Duggan, C., Reden, T.B., Kooragayala, L.M., Texada, D.E., Langford, M.P. Biochemistry (2004) [Pubmed]
  7. Covalent structure of bovine brain calreticulin. Matsuoka, K., Seta, K., Yamakawa, Y., Okuyama, T., Shinoda, T., Isobe, T. Biochem. J. (1994) [Pubmed]
  8. Comparison of cDNAs from bovine brain coding for two isoforms of calreticulin. Liu, N., Fine, R.E., Johnson, R.J. Biochim. Biophys. Acta (1993) [Pubmed]
  9. Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (Glc1Man9GlcNAc2) substrate. Patil, A.R., Thomas, C.J., Surolia, A. J. Biol. Chem. (2000) [Pubmed]
  10. Cloning and partial characterization of a Boophilus microplus (Acari: Ixodidae) calreticulin. Ferreira, C.A., Da Silva Vaz, I., da Silva, S.S., Haag, K.L., Valenzuela, J.G., Masuda, A. Exp. Parasitol. (2002) [Pubmed]
  11. Xanthurenic acid provokes formation of unfolded proteins in endoplasmic reticulum of the lens epithelial cells. Malina, H.Z. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  12. A single purification procedure for the major resident proteins of the ER lumen: endoplasmin, BiP, calreticulin and protein disulfide isomerase. Rowling, P.J., McLaughlin, S.H., Pollock, G.S., Freedman, R.B. Protein Expr. Purif. (1994) [Pubmed]
  13. Calreticulin destabilizes glucose transporter-1 mRNA in vascular endothelial and smooth muscle cells under high-glucose conditions. Totary-Jain, H., Naveh-Many, T., Riahi, Y., Kaiser, N., Eckel, J., Sasson, S. Circ. Res. (2005) [Pubmed]
  14. Conglutinin, CL-43 and CL-46--three bovine collectins. Dec, M., Wernicki, A. Polish journal of veterinary sciences (2006) [Pubmed]
  15. Inhibition of phospholipase A2 by protein I. Khanna, N.C., Hee-Chong, M., Severson, D.L., Tokuda, M., Chong, S.M., Waisman, D.M. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
 
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