ArticlePloS one2013
Self-oligomerization is essential for enhanced immunological activities of soluble recombinant calreticulin.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Identification of a Novel Antibacterial Function of Mammalian Calreticulin.Biomolecules · 2025Article
- Transcriptome profiling of macrophages persistently infected with human respiratory syncytial virus and effect of recombinantFrontiers in microbiology · 2024Article
- Epitope Mapping of Monoclonal Antibodies to Calreticulin Reveals That Charged Amino Acids Are Essential for Antibody Binding.Antibodies (Basel, Switzerland) · 2021Article
- PCV cap proteins fused with calreticulin expressed into polymers in Escherichia coli with high immunogenicity in mice.BMC veterinary research · 2020Article
- The Biophysical Interaction of the Danger-Associated Molecular Pattern (DAMP) Calreticulin with the Pattern-Associated Molecular Pattern (PAMP) Lipopolysaccharide.International journal of molecular sciences · 2019Article
- Aberrant Glycosylation Augments the Immuno-Stimulatory Activities of Soluble Calreticulin.Molecules (Basel, Switzerland) · 2018Article
- Serum calreticulin as a novel biomarker of juvenile idiopathic arthritis disease activity.European journal of rheumatology · 2017Article
- Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function.Frontiers in cell and developmental biology · 2017Article
- Soluble calreticulin induces tumor necrosis factor-α (TNF-α) and interleukin (IL)-6 production by macrophages through mitogen-activated protein kinase (MAPK) and NFκB signaling pathways.International journal of molecular sciences · 2014Article
- Immunological activity difference between native calreticulin monomers and oligomers.PloS one · 2014Article
- CD1d(hi)CD5⁺ B cells differentiate into antibody-secreting cells under the stimulation with calreticulin fragment.Protein & cell · 2013Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have recently reported that calreticulin (CRT), a luminal resident protein, can be found in the sera of patients with rheumatoid arthritis and also that recombinant CRT (rCRT) exhibits extraordinarily strong immunological activities. We herein further demonstrate that rCRT fragments 18-412 (rCRT/18-412), rCRT/39-272, rCRT/120-308 and rCRT/120-250 can self-oligomerize in solution and are 50-100 fold more potent than native CRT (nCRT, isolated from mouse livers) in activating macrophages in vitro. We narrowed down the active site of CRT to residues 150-230, the activity of which also depends on dimerization. By contrast, rCRT/18-197 is almost completely inactive. When rCRT/18-412 is fractionated into oligomers and monomers by gel filtration, the oligomers maintain most of their immunological activities in terms of activating macrophages in vitro and inducing specific antibodies in vivo, while the monomers were much less active by comparison. Additionally, rCRT/18-412 oligomers are much better than monomers in binding to, and uptake by, macrophages. Inhibition of macrophage endocytosis partially blocks the stimulatory effect of rCRT/18-412. We conclude that the immunologically active site of CRT maps between residues 198-230 and that soluble CRT could acquire potent immuno-pathological activities in microenvironments favoring its oligomerization.
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