ArticleInternational journal of hematology2004
The protein tyrosine phosphatase CD45 is required for interleukin 6 signaling in U266 myeloma cells.
Article in International journal of hematology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed, 17 citations in OpenAlex.
- IL-6 Induces CD45 Expression on Myeloid Cells.Sultan Qaboos University medical journal · 2025Article
- Expression of CD45 in non-hematopoietic cells: implications in regenerative medicine and disease management.Regenerative medicine · 2024Review
- Making sense of IL-6 signalling cues in pathophysiology.FEBS letters · 2022Review
- Protein Tyrosine Phosphatases in Systemic Sclerosis: Potential Pathogenic Players and Therapeutic Targets.Current rheumatology reports · 2017Review
- Article
- The novel JAK inhibitor AZD1480 blocks STAT3 and FGFR3 signaling, resulting in suppression of human myeloma cell growth and survival.Leukemia · 2011Article
- Sustained activation of c-jun-N-terminal kinase plays a critical role in arsenic trioxide-induced cell apoptosis in multiple myeloma cell lines.Cancer science · 2006Article
- Lyn prevents aberrant inflammatory responses toSignal transduction and targeted therapyArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The objective of this study was to examine whether CD45 mediates interleukin 6 (IL-6) signaling in human multiple myeloma (MM) cells. We chose U266 MM cells as a study model and isolated cells into CD45+ and CD45- subpopulations. CD45+ and CD45- U266 cells were cocultured with bone marrow stromal cells (BMSCs). IL-6-induced proliferation in CD45+ U266 cells was inhibited by vanadate, a potent protein tyrosine phosphatase inhibitor. However, IL-6-independent CD45- U266 cell growth was not affected by vanadate. CD45+ U266 cells, but not CD45- U266 cells, have the capability of cell adhesion concomitant with actin filament polymerization at the adherent cells. Adhesion of CD45+ U266 cells to BMSCs was impaired by vanadate. We clarified the signaling differences between CD45+ and CD45- U266 cells in response to IL-6. In CD45+ U266 cells, IL-6 increased tyrosine phosphorylation of gp130 and STAT3 and stimulated the level of Mcl-1 protein expression. An association between CD45 and the Src-family protein tyrosine kinase, Lyn, was maintained in the presence of IL-6; the formation of the CD45/Lyn complex was impaired by vanadate. Additionally, IL-6-induced Lyn kinase activity in CD45+ U266 cells was increased by the cross-linking of CD45, and this increase was due to the dephosphorylation of Tyr507 at Lyn. In conclusion, IL-6-dependent MM cells require CD45 to initiate IL-6 signaling and to maintain Lyn kinase activity, both of which are essential for cell proliferation and cell adhesion.
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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.