Polyclonal B cell activation by a B cell differentiation factor, B151-TRF2. II. Evidence for interaction of B151-TRF2 with glycoprotein on B cell membrane via recognition of terminal N-acetyl-D-glucosamine residue(s).

Y Katoh; S Ono; Y Takahama; K Miyake; T Hamaoka

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PubMed · 3489778

Polyclonal B cell activation by a B cell differentiation factor, B151-TRF2. II. Evidence for interaction of B151-TRF2 with glycoprotein on B cell membrane via recognition of terminal N-acetyl-D-glucosamine residue(s).

Y Katoh·S Ono·Y Takahama·K Miyake·T Hamaoka

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Abstract

We investigated the role of carbohydrates in the interaction of a B cell differentiation factor designated as B151-TRF2 derived from B151K12 T cell hybridoma with the corresponding receptor on B cells. Induction of polyclonal differentiation of unprimed B cells into IgM-secreting cells by B151-TRF2 was specifically inhibited by addition of N-acetyl-D-glucosamine (GlcNAc) but not by structurally unrelated monosaccharides such as D-galactose, D-glucose, and N-acetyl-D-galactosamine (GalNAc). Absorption of B151-TRF2 activity with spleen cells was specifically inhibited by the presence of GlcNAc. These results indicate that GlcNAc residues are involved in the interaction of B151-TRF2 with the receptor on B cells. To gain insight into mechanism by which GlcNAc inhibits B151-TRF2-mediated B cell responses, the existence of GlcNAc residues was examined on the B151-TRF2 molecule and the corresponding receptor on the B cell surface. The results revealed that B151-TRF2 molecule was not bound to various lectin-coupled agarose beads so far tested, suggesting absence of carbohydrate moieties on the B151-TRF2 molecule. By contrast, pretreatment of spleen cells with trypsin or glycosidase mixture abolished their ability to absorb B151-TRF2 activity. Moreover, B151-TRF2-absorbing ability of spleen cells disappeared by the pretreatment with beta-N-acetylglucosaminidase, which cleaves terminal GlcNAc. The fact that pnitrophenyl (PNP)-GlcNAc specifically inhibited such enzyme activity on target cells indicates that terminal GlcNAc on the B cell surface plays a crucial role in the interaction with B151-TRF2 molecule. Interestingly, it was also found that B151-TRF2 activity was trapped and eluted from GlcNAc-coupled agarose beads. Taken collectively, these results strongly suggest that B cell membrane receptors for B151-TRF2 comprise glycoproteins with a terminal GlcNAc residue(s), and that binding of B151-TRF2 with terminal GlcNAc on the receptor is important for the subsequent activation of B cells.

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Acetylglucosamine Acetylglucosaminidase Animals Antibody Formation B-Lymphocytes Binding Sites Cell Differentiation Glucosamine Growth Substances Interleukin-4 Lectins Lymphocyte Activation Lymphokines Mice Receptors, Immunologic Spleen Journal Article Research Support, Non-U.S. Gov't

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Y Katoh, S Ono, Y Takahama, K Miyake, T Hamaoka. 1986-11-01. Polyclonal B cell activation by a B cell differentiation factor, B151-TRF2. II. Evidence for interaction of B151-TRF2 with glycoprotein on B cell membrane via recognition of terminal N-acetyl-D-glucosamine residue(s).. https://pubmed.ncbi.nlm.nih.gov/3489778/

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