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*
Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden; and
Istitut für Klinische Molekularbiologie und Tumorgenetik, Gesellschaft für Strahlung und Umweltforschung-Forschungszentrum für Umwelt und Gesundheit, Munich, Germany
We have compared the subunit composition and enzymatic activity of
purified 26S proteasomes from Burkitt’s lymphoma (BL) cells and in
vitro EBV-transformed lymphoblastoid cell lines (LCLs) of normal B cell
origin. Low expression of the IFN-
-regulated ß low molecular mass
polypeptide (Lmp)2, Lmp7, and MECL-1 was demonstrated in a panel of
seven BL lines that express the germinal center cell phenotype of the
original tumor. Coexpression of Lmp2 and Lmp7 with the constitutively
expressed subunits 
and MB1 was demonstrated in the BL lines by
immunoprecipitation and two-dimensional gel fractionation of the 20S
proteasomes. Coexpression of these subunits correlated with reduced
levels of chymotrypsin- and trypsin-like activities detected by the
cleavage of fluorogenic substrates. Down-regulation of Lmp2 and Lmp7
and decreased chymotrypsin- and trypsin-like activities were also
observed in purified proteasomes from a c-myc-transfected
subline of the ER/EB2–5 LCL that has adopted a BL-like phenotype. A
synthetic peptide analogue of the immunodominant epitope from the EBV
nuclear Ag 4 (E4416–424Y) was cleaved by proteasomes from BLs and A1,
while proteasomes from LCLs were inactive. Cleavage of the E4416–424Y
peptide was not affected by treatment of the BL cells with IFN-
despite both significant up-regulation of Lmp2 and Lmp7 and
reconstitution of chymotrypsin and trypsin-like activities against
fluorogenic substrates to LCL-like levels. The results demonstrate that
B cell lines representing different stages of B cell activation and
differentiation express proteasomes with different subunit compositions
and enzymatic activity. This may result in the generation of a distinct
set of endogenous peptides and influence the immunogenicity of these
cells.
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