Journal
JOURNAL OF EXPERIMENTAL MEDICINE
Volume 195, Issue 9, Pages 1199-1205Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1084/jem.20011796
Keywords
signal transduction; SHP-1; calcium; siglec; tyrosine phosphorylation
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Funding
- NCI NIH HHS [R01CA66600] Funding Source: Medline
- NIAID NIH HHS [AI15803] Funding Source: Medline
- NIAMS NIH HHS [AR43773] Funding Source: Medline
- NIDDK NIH HHS [P01DK50654, P01 DK050654] Funding Source: Medline
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CD22, a negative regulator of B cell antigen receptor signaling, binds glycoconjugates terminating in alpha2, 6 sialic acid. The physiological ligand(s) for CD22 remain unknown. We asked whether the sialic acid binding domains are necessary for CD22 to function as a negative regulator. We generated two mutants that lack sialic acid binding activity and expressed them in a novel CD22(-/-) murine B cell line. Anti-IgM activated B cells expressing either CD22 mutant had greater Ca2+ responses than cells expressing wild-type CD22. Each valiant also had reduced CD22 tyrosine phosphorylation and Src homology 2 domain-containing protein tyrosine phosphatase-1 association. These data suggest that the alpha2, 6 sialic acid ligand binding activity of CD22 is critical for its negative regulatory functions.
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