Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22

Joseph Tuscano, Pablo Engel, Thomas F. Tedder, Alka Agarwal, John H. Kehrl

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

CD22 is a B lymphocyte-specific membrane protein that functions as an adhesion molecule via its interactions with a subset of α2-6-linked sialic acid-containing glycoproteins. Engagement of CD22 with a monoclonal antibody (HB22.23) that blocks the binding of CD22 to its ligands results in rapid CD22 tyrosine phosphorylation and in increased association of CD22 with p53/56lyn kinase, p85 phosphatidyl inositol-3 kinase, and p72syk kinase. Synthetic peptides that span various regions of the intracellular portion of CD22 were used to map potential kinase binding sites. All three kinases associated with a tyrosine-phosphorylated peptide that spans tyrosine amino acid residues 822 and 842, implicating this as an important region in mediating CD22 signal transduction. In addition, purified p56lyn directly bound to the same peptide. Engagement of CD22 with HB22.23 was sufficient to stimulate normal B cell proliferation. This study further substantiates the importance of CD22 as a B lymphocyte signaling molecule and begins to unravel the mechanisms by which CD22 cross-linking can alter B cell function.

Original languageEnglish (US)
Pages (from-to)1246-1252
Number of pages7
JournalEuropean Journal of Immunology
Volume26
Issue number6
DOIs
StatePublished - Jun 1996
Externally publishedYes

Fingerprint

Sialic Acid Binding Ig-like Lectin 2
Phosphatidylinositols
Signal Transduction
B-Lymphocytes
Phosphotransferases
Tyrosine
Peptides
N-Acetylneuraminic Acid
Glycoproteins
Membrane Proteins
Binding Sites
Monoclonal Antibodies
Phosphorylation
Cell Proliferation
Ligands
Amino Acids

Keywords

  • Cd22
  • p53/56lyn
  • p72syk
  • Phosphatidyl inositol-3 kinase

ASJC Scopus subject areas

  • Immunology

Cite this

Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. / Tuscano, Joseph; Engel, Pablo; Tedder, Thomas F.; Agarwal, Alka; Kehrl, John H.

In: European Journal of Immunology, Vol. 26, No. 6, 06.1996, p. 1246-1252.

Research output: Contribution to journalArticle

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AB - CD22 is a B lymphocyte-specific membrane protein that functions as an adhesion molecule via its interactions with a subset of α2-6-linked sialic acid-containing glycoproteins. Engagement of CD22 with a monoclonal antibody (HB22.23) that blocks the binding of CD22 to its ligands results in rapid CD22 tyrosine phosphorylation and in increased association of CD22 with p53/56lyn kinase, p85 phosphatidyl inositol-3 kinase, and p72syk kinase. Synthetic peptides that span various regions of the intracellular portion of CD22 were used to map potential kinase binding sites. All three kinases associated with a tyrosine-phosphorylated peptide that spans tyrosine amino acid residues 822 and 842, implicating this as an important region in mediating CD22 signal transduction. In addition, purified p56lyn directly bound to the same peptide. Engagement of CD22 with HB22.23 was sufficient to stimulate normal B cell proliferation. This study further substantiates the importance of CD22 as a B lymphocyte signaling molecule and begins to unravel the mechanisms by which CD22 cross-linking can alter B cell function.

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