ArticleThe Journal of experimental medicine1996
CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation.
Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 198 citations in OpenAlex.
- Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling.Life science alliance · 2021Article
- Putting the brakes on phagocytosis: "don't-eat-me" signaling in physiology and disease.EMBO reports · 2021Review
- B Cell Siglecs-News on Signaling and Its Interplay With Ligand Binding.Frontiers in immunology · 2018Review
- Targeting CD22 with the monoclonal antibody epratuzumab modulates human B-cell maturation and cytokine production in response to Toll-like receptor 7 (TLR7) and B-cell receptor (BCR) signaling.Arthritis research & therapy · 2017Article
- Viewing Siglecs through the lens of tumor immunology.Immunological reviews · 2017Review
- Promising Role of Toll-Like Receptor 8 Agonist in Concert with Prostratin for Activation of Silent HIV.Journal of virology · 2017Article
- Article
- Nanoscale organization and dynamics of the siglec CD22 cooperate with the cytoskeleton in restraining BCR signalling.The EMBO journal · 2016Article
- Mechanism and function of monoclonal antibodies targeting siglec-15 for therapeutic inhibition of osteoclastic bone resorption.The Journal of biological chemistry · 2014Article
- Rethinking mechanisms of autoimmune pathogenesis.Journal of autoimmunity · 2013Review
- CD22 is required for protection against West Nile virus Infection.Journal of virology · 2013Article
- Substrate specificity of protein tyrosine phosphatases 1B, RPTPα, SHP-1, and SHP-2.Biochemistry · 2011Article
- Regulation of B cell functions by the sialic acid-binding receptors siglec-G and CD22.Frontiers in immunology · 2011Article
- CD22 EXON 12 deletion as a pathogenic mechanism of human B-precursor leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Syk and pTyr'd: Signaling through the B cell antigen receptor.Biochimica et biophysica acta · 2009Review
- Regulation of B-cell entry into the cell cycle.Immunological reviews · 2008Review
- Dendritic cell-dependent inhibition of B cell proliferation requires CD22.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- CD22: an inhibitory enigma.Immunology · 2008Review
- Rapid T cell receptor-mediated SHP-1 S591 phosphorylation regulates SHP-1 cellular localization and phosphatase activity.Journal of leukocyte biology · 2007Article
- Cytotoxic activity of gemtuzumab ozogamicin (Mylotarg) in acute myeloid leukemia correlates with the expression of protein kinase Syk.Leukemia · 2006Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Cross-linking B cell antigen receptor (BCR) elicits early signal transduction events, including activation of protein tyrosine kinases, phosphorylation of receptor components, activation of phospholipase C-gamma (PLC-gamma), and increases in intracellular free Ca2+. In this article, we report that cross-linking the BCR led to a rapid translocation of cytosolic protein tyrosine phosphatase (PTP) 1C to the particulate fraction, where it became associated with a 140-150-kD tyrosyl-phosphorylated protein. Western blotting analysis identified this 140-150-kD protein to be CD22. The association of PTP-1C with CD22 was mediated by the NH2-terminal Src homology 2 (SH2) domain of PTP-1C. Complexes of either CD22/PTP-1C/Syk/PLC-gamma(1) could be isolated from B cells stimulated by BCR engagement or a mixture of hydrogen peroxidase and sodium orthovanadate, respectively. The binding of PLC-gamma(1) and Syk to tyrosyl-phosphorylated CD22 was mediated by the NH2-terminal SH2 domain of PLC-gamma(1) and the COOH-terminal SH2 domain of Syk, respectively. These observations suggest that tyrosyl-phosphorylated CD22 may downmodulate the activity of this complex by dephosphorylation of CD22, Syk, and/or PLC-gamma(1). Transient expression of CD22 and a null mutant of PTP-1C (PTP-1CM) in COS cells resulted in an increase in tyrosyl phosphorylation of CD22 and its interaction with PTP-1CM. By contrast, CD22 was not tyrosyl phosphorylated or associated with PTP-1CM in the presence of wild-type PTP-1C. These results suggest that tyrosyl-phosphorylated CD22 may be a substrate for PTP-1C regulates tyrosyl phosphorylation of CD22.
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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.