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Sialylation of the B lymphocyte molecule CD22 by alpha 2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion.
J Biol Chem. 1994 Apr 22; 269(16):11783-6.JB

Abstract

The B cell surface receptor CD22 binds several sialoglycoproteins containing sialic acid in alpha 2,6 linkage, on the surface of B and T lymphocytes. Because lymphocytes adhere tightly to fibroblasts transfected with CD22 cDNA, it would appear reasonable to suggest that regulatory mechanisms might have evolved which prevent undesired CD22-mediated leukocyte aggregation. Here we provide evidence for the existence of at least one mechanism that might regulate CD22 interaction with ligands on adjacent cells. We demonstrate that sialylation of CD22 by beta-galactoside alpha 2,6-sialyltransferase abrogates CD22-mediated lymphocyte adhesion, and that adhesion can be restored by removal of alpha 2,6-linked sialic acid residues from the CD22 molecule. Taken together, our results suggest that alpha 2,6-sialyltransferase can both promote and inhibit CD22-ligand interactions. These observations provide the first direct evidence that receptor-ligand interactions mediated by an Ig superfamily molecule are under the control of a specific glycosyltransferase.

Authors+Show Affiliations

Department of Pathology, Massachusetts General Hospital.No affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8163475

Citation

Braesch-Andersen, S, and I Stamenkovic. "Sialylation of the B Lymphocyte Molecule CD22 By Alpha 2,6-sialyltransferase Is Implicated in the Regulation of CD22-mediated Adhesion." The Journal of Biological Chemistry, vol. 269, no. 16, 1994, pp. 11783-6.
Braesch-Andersen S, Stamenkovic I. Sialylation of the B lymphocyte molecule CD22 by alpha 2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion. J Biol Chem. 1994;269(16):11783-6.
Braesch-Andersen, S., & Stamenkovic, I. (1994). Sialylation of the B lymphocyte molecule CD22 by alpha 2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion. The Journal of Biological Chemistry, 269(16), 11783-6.
Braesch-Andersen S, Stamenkovic I. Sialylation of the B Lymphocyte Molecule CD22 By Alpha 2,6-sialyltransferase Is Implicated in the Regulation of CD22-mediated Adhesion. J Biol Chem. 1994 Apr 22;269(16):11783-6. PubMed PMID: 8163475.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sialylation of the B lymphocyte molecule CD22 by alpha 2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion. AU - Braesch-Andersen,S, AU - Stamenkovic,I, PY - 1994/4/22/pubmed PY - 1994/4/22/medline PY - 1994/4/22/entrez SP - 11783 EP - 6 JF - The Journal of biological chemistry JO - J Biol Chem VL - 269 IS - 16 N2 - The B cell surface receptor CD22 binds several sialoglycoproteins containing sialic acid in alpha 2,6 linkage, on the surface of B and T lymphocytes. Because lymphocytes adhere tightly to fibroblasts transfected with CD22 cDNA, it would appear reasonable to suggest that regulatory mechanisms might have evolved which prevent undesired CD22-mediated leukocyte aggregation. Here we provide evidence for the existence of at least one mechanism that might regulate CD22 interaction with ligands on adjacent cells. We demonstrate that sialylation of CD22 by beta-galactoside alpha 2,6-sialyltransferase abrogates CD22-mediated lymphocyte adhesion, and that adhesion can be restored by removal of alpha 2,6-linked sialic acid residues from the CD22 molecule. Taken together, our results suggest that alpha 2,6-sialyltransferase can both promote and inhibit CD22-ligand interactions. These observations provide the first direct evidence that receptor-ligand interactions mediated by an Ig superfamily molecule are under the control of a specific glycosyltransferase. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/8163475/Sialylation_of_the_B_lymphocyte_molecule_CD22_by_alpha_26_sialyltransferase_is_implicated_in_the_regulation_of_CD22_mediated_adhesion_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(17)32640-6 DB - PRIME DP - Unbound Medicine ER -