International Immunology, Vol 10, 185-194, Copyright © 1998 by Oxford University Press
E Bruyns, H Kirchgessner, S Meuer and B Schraven
In human and mouse lymphocytes the protein tyrosine phosphatase CD45, a key
molecule involved in T cell activation, non-covalently associates with the
tyrosine kinase p56(lck) and lymphocyte phosphatase-associated
phosphoprotein (LPAP), a 32 kDa phosphoprotein of unknown function. In
order to gain insight into the function of LPAP we have generated an
LPAP-deficient Jurkat variant by means of antisense strategies. Analysis of
the CD45-p56(lck) molecular complex in this cell line revealed that loss of
LPAP does not alter the expression or the enzymatic activity of CD45 or
p56(lck). In addition, the association between CD45 and p56(lck) is not
affected in LPAP-deficient T cells. These data suggest that LPAP does not
regulate the enzymatic activity of CD45 or p56(lck) and is not required for
the association between these two proteins. In order to identify
polypeptides that preferentially associate with LPAP we established a
Jurkat variant expressing a chimeric receptor which was composed of the
extracellular portion of the human HLA-A2.1 molecule and the full-length
LPAP protein. Comparative two-dimensional analysis of CD45 and HLA-A2
immunoprecipitates obtained from these cells following metabolic labeling
resulted in the identification of a 43 kDa protein that preferentially
associates with LPAP under mild detergent conditions.
ARTICLES
Biochemical analysis of the CD45-p56(lck) complex in Jurkat T cells lacking expression of lymphocyte phosphatase-associated phosphoprotein
Institute of Immunology, Immunomodulation Laboratory, Ruprecht-Karls University of Heidelberg, Germany.
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