期刊
JOURNAL OF LEUKOCYTE BIOLOGY
卷 90, 期 1, 页码 5-19出版社
FEDERATION AMER SOC EXP BIOL
DOI: 10.1189/jlb.0710404
关键词
sialic acids; O-linked; cell surface marker
资金
- Swedish Children's Cancer Foundation
- Sahlgrenska University Hospital Foundation
- Willhelm and Martina Lundgrens Foundation
- Mucosal Immunobiology and Vaccine Center (MIVAC)
A screen of cell surface markers differentially expressed during peripheral B cell differentiation identified that the CD45RB epitope detected by the mAb MEM-55 was highly expressed on CD27(+) memory B cells and absent on CD27(-) naive B cells. IgG(+) CD27(-) memory and a previously unacknowledged CD27-population in blood also expressed high levels of CD45RB(MEM55). Naive and memory B cells from tonsils followed the pattern observed in blood, and CD38(high) B cells had a bimodal expression pattern when analyzed using flow cytometry. No CD38(high) GC B cells, however, expressed the CD45RB(MEM55) epitope when assayed using immunohistochemistry. Rather, CD38(high)CD45RB(MEM55high) B cells had a distinct cellular phenotype and were localized outside of GCs. CD45RB epitopes, detected by other antibody clones, were expressed at high levels through B cell differentiation, and no changes in splicing of the CD45RB exon were observed during B cell differentiation. Instead, B cells regulated their expression of the CD45RB(MEM55) epitope through site-specific modifications of an O-linked glycochain. CD4(+) T cells differentially spliced CD45 but did not vary the glycosylation of the CD45RB(MEM55) epitope, and CD8(+) cells modified CD45RB(MEM55) expression in a similar manner as B cells. Monocytes expressed the CD45RB exon but not the CD45RB(MEM55) epitope. As CD45 is a highly expressed tyrosine phosphatase that regulates antigen receptor signaling strength in lymphocytes, we conclude that regulated O-linked glycosylation of CD45RB can be used to follow B cell differentiation and that this regulation may be involved in fine-tuning antigen signaling in the cell. J. Leukoc. Biol. 90: 5-19; 2011.
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