The CR2/CD19 complex on human B cells contains the src-family kinase Lyn

C. J. van Noesel; A. C. Lankester; G. M. van Schijndel; R. A. van Lier

The CR2/CD19 complex on human B cells contains the src-family kinase Lyn

C. J. van Noesel, A. C. Lankester, G. M. van Schijndel, R. A. van Lier

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Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

The complement receptor 2 (CR2 or CD21) can be found in non-covalent association with the B lymphocyte specific CD19 complex at the surface of mature human B cells. Upon ligation of the B cell antigen receptor complex (BCR), members of the CR2-CD19 complex may associate with membrane immunoglobulin (mlg). Moreover, CD19 and CD21 ligands, either murine mAb, C3d fragments or Epstein-Barr virus, are known to have profound effects on B cell activation. We here show that CD19 is tightly linked to the non-receptor src kinase Lyn and that the CD19 glycoprotein itself serves as a substrate for a yet undefined serine/threonine kinase present within the complex. In the process of antigen recognition, mlg and the CR2-CD19 complex may bind different sites of a complement-opsonized antigenic particle. We hypothesize that in this process, approximation to the BCR allows CD19-associated Lyn kinase to phosphorylate potential substrates within the antigen-receptor complex, thereby effecting its coupling to the intracellular compartment

Original language	English
Pages (from-to)	699-705
Journal	International Immunology
Volume	5
Issue number	7
Publication status	Published - 1993

Cite this

@article{9db5148c9daf476a8a133db2c4bf934a,

title = "The CR2/CD19 complex on human B cells contains the src-family kinase Lyn",

abstract = "The complement receptor 2 (CR2 or CD21) can be found in non-covalent association with the B lymphocyte specific CD19 complex at the surface of mature human B cells. Upon ligation of the B cell antigen receptor complex (BCR), members of the CR2-CD19 complex may associate with membrane immunoglobulin (mlg). Moreover, CD19 and CD21 ligands, either murine mAb, C3d fragments or Epstein-Barr virus, are known to have profound effects on B cell activation. We here show that CD19 is tightly linked to the non-receptor src kinase Lyn and that the CD19 glycoprotein itself serves as a substrate for a yet undefined serine/threonine kinase present within the complex. In the process of antigen recognition, mlg and the CR2-CD19 complex may bind different sites of a complement-opsonized antigenic particle. We hypothesize that in this process, approximation to the BCR allows CD19-associated Lyn kinase to phosphorylate potential substrates within the antigen-receptor complex, thereby effecting its coupling to the intracellular compartment",

author = "{van Noesel}, {C. J.} and Lankester, {A. C.} and {van Schijndel}, {G. M.} and {van Lier}, {R. A.}",

year = "1993",

language = "English",

volume = "5",

pages = "699--705",

journal = "International Immunology",

issn = "0953-8178",

publisher = "Oxford University Press",

number = "7",

}

TY - JOUR

T1 - The CR2/CD19 complex on human B cells contains the src-family kinase Lyn

AU - van Noesel, C. J.

AU - Lankester, A. C.

AU - van Schijndel, G. M.

AU - van Lier, R. A.

PY - 1993

Y1 - 1993

N2 - The complement receptor 2 (CR2 or CD21) can be found in non-covalent association with the B lymphocyte specific CD19 complex at the surface of mature human B cells. Upon ligation of the B cell antigen receptor complex (BCR), members of the CR2-CD19 complex may associate with membrane immunoglobulin (mlg). Moreover, CD19 and CD21 ligands, either murine mAb, C3d fragments or Epstein-Barr virus, are known to have profound effects on B cell activation. We here show that CD19 is tightly linked to the non-receptor src kinase Lyn and that the CD19 glycoprotein itself serves as a substrate for a yet undefined serine/threonine kinase present within the complex. In the process of antigen recognition, mlg and the CR2-CD19 complex may bind different sites of a complement-opsonized antigenic particle. We hypothesize that in this process, approximation to the BCR allows CD19-associated Lyn kinase to phosphorylate potential substrates within the antigen-receptor complex, thereby effecting its coupling to the intracellular compartment

AB - The complement receptor 2 (CR2 or CD21) can be found in non-covalent association with the B lymphocyte specific CD19 complex at the surface of mature human B cells. Upon ligation of the B cell antigen receptor complex (BCR), members of the CR2-CD19 complex may associate with membrane immunoglobulin (mlg). Moreover, CD19 and CD21 ligands, either murine mAb, C3d fragments or Epstein-Barr virus, are known to have profound effects on B cell activation. We here show that CD19 is tightly linked to the non-receptor src kinase Lyn and that the CD19 glycoprotein itself serves as a substrate for a yet undefined serine/threonine kinase present within the complex. In the process of antigen recognition, mlg and the CR2-CD19 complex may bind different sites of a complement-opsonized antigenic particle. We hypothesize that in this process, approximation to the BCR allows CD19-associated Lyn kinase to phosphorylate potential substrates within the antigen-receptor complex, thereby effecting its coupling to the intracellular compartment

M3 - Article

C2 - 7690241

SN - 0953-8178

VL - 5

SP - 699

EP - 705

JO - International Immunology

JF - International Immunology

IS - 7

ER -