ArticleImmunology1997
Expression of rat CD59: functional analysis confirms lack of species selectivity and reveals that glycosylation is not required for function.
Article in Immunology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- A cryptic non-GPI-anchored cytosolic isoform of CD59 controls insulin exocytosis in pancreatic β-cells by interaction with SNARE proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- GluR3 autoantibodies destroy neural cells in a complement-dependent manner modulated by complement regulatory proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000Article
- Human and rodent decay-accelerating factors (CD55) are not species restricted in their complement-inhibiting activities.Immunology · 2000Article
- Surface antigen expression and complement susceptibility of differentiated neuroblastoma clones.The American journal of pathology · 2000Article
- Production and functional characterization of a soluble recombinant form of mouse CD59.Immunology · 2000Article
- Protection of human breast cancer cells from complement-mediated lysis by expression of heterologous CD59.Clinical and experimental immunology · 1999Article
- Characterization in vitro and in vivo of the pig analogue of human CD59 using new monoclonal antibodies.Immunology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
This study reports the expression and functional characterization of the rat analogue of the human complement regulatory molecule CD59. We here describe the expression in chinese hamster ovary (CHO) cells of rat CD59 and a modified rat CD59 in which an N-glycosylation site at Asn-16 has been deleted by point mutation. The complement-inhibiting capacity of these two forms of rat CD59 has been analysed and compared. Expressed rat CD59 efficiently inhibited complement lysis of CHO cells when rat serum was used as a source of complement and also inhibited lysis by complement from all other species tested, confirming that rat CD59 displayed little or no species restriction of activity. Blocking of expressed rat CD59 with a monoclonal antibody abrogated the inhibition of lysis for all sources of complement, confirming that the expressed molecule was responsible for the protection. The glycosylation mutant had a much reduced molecular weight on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) (12,000 MW as compared with 20,000-28,000 MW for unmutated), confirming that it was unglycosylated. However, the glycosylation mutant had complement-inhibitory activity which was at least as potent as that of the unmutated molecule, demonstrating that the large, N-linked carbohydrate moiety was not required for function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.