Spontaneous and ligand-induced endocytosis of CD23 (Fc epsilon receptor II) from the surface of B lymphocytes generates a 16-kDa intracellular fragment.

Abstract:

:It has been reported that the 45-kDa low-affinity Fc epsilon receptor (Fc epsilon RII) on B cells is cleaved spontaneously from the cell surface to release soluble fragments. This study demonstrates an additional fate of the Fc epsilon RII. 125I-labeled CD23+ B cells were cultured for 24 h at 37 degrees C. After lysis, cell extracts were immunoprecipitated with CD23 monoclonal antibodies. Using this methodology, we demonstrated that an increasing amount of the labeled Fc epsilon RII becomes progressively resistant to externally applied trypsin, indicating that a fraction of the cell surface receptors are internalized. In parallel, a labeled 16-kDa material, recognized by CD23 monoclonal antibodies directed to the lectin-like domain of the Fc epsilon-RII appears inside the cells. Chloroquine does not affect internalization of the Fc epsilon RII, but completely abolishes the formation of the intracellular fragment, suggesting that the receptor is processed by proteolytic cleavage in acidic organelle. In addition, the internalization is enhanced in the presence of CD23 monoclonal antibodies. These data demonstrate that Fc epsilon RII can be internalized by ligand-induced endocytosis and subsequently cleaved in an intracellular compartment. These results also support the view that the Fc epsilon RII is involved in antigen focusing and antigen presentation.

journal_name

Eur J Immunol

authors

Grenier-Brossette N,Bourget I,Akoundi C,Bonnefoy JY,Cousin JL

doi

10.1002/eji.1830220634

keywords:

subject

Has Abstract

pub_date

1992-06-01 00:00:00

pages

1573-7

issue

6

eissn

0014-2980

issn

1521-4141

journal_volume

22

pub_type

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