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CD3- large granular lymphocytes recognize a heat-inducible immunogenic
determinant associated with the 72-kD heat shock protein on human sarcoma
cells
G Multhoff, C Botzler, M Wiesnet, G Eissner and R Issels
GSF-Institut fur Klinische Hamatologie, Munchen, Germany.
Traditionally, heat shock proteins (HSPs) are believed to be located
intracellularly, where they perform a variety of chaperoning functions.
Recently, evidence has accumulated that some tumor cells express HSPs on
the cell surface. The present study confirms this finding and correlates
HSP72 cell surface expression, induced by nonlethal heat shock, with an
increased sensitivity to interleukin-2-stimulated CD3- natural killer (NK)
cells. After nonlethal heat shock, a monoclonal antibody directed against
the major heat-inducible 72-kD HSP (HSP72) stains the cell surface of
sarcoma cells (ie, Ewing's sarcoma cells or osteosarcoma cells) but not
that of normal cells (ie, peripheral blood lymphocytes, fibroblasts,
phytohemagglutin-stimulated blasts, B- lymphoblastoid cell lines) or of
mammary carcinoma cell line MX-1 carcinoma cells. In this study, we show
for the first time a correlation of HSP72 cell surface expression with an
increased susceptibility to lysis by NK effector cells. This finding is
supported by the following points: (1) HLA-disparate effector cells show
similar, elevated lysis of HSP72+ heat-treated sarcoma cells; (2) CD(3-) NK
cells, but not CD3+ cytotoxic T lymphocytes, are responsible for the
recognition of heat-shocked sarcoma cells; (3) by antibody-blocking
studies, an immunogenic HSP72 determinant, which is expressed selectively
on the cell surface of heat-treated sarcoma cells could be correlated with
NK recognition; (4) the reported phenomenon is independent of a
heat-induced, transient downregulation of major histocompatibility complex
(MHC) class-I expression; and (5) blocking of MHC class-I-restricted
recognition, using either MHC class-I- specific monoclonal antibody W6/32
on the target cells or alpha/beta T- cell receptor monoclonal antibody WT31
on effector cells, also has no inhibitory effect on the lysis of HSP72+
tumor cells. Finally, our in vitro data might have further clinical
implications with respect to HSP72 as a stress-inducible, sarcoma-specific
NK recognition structure.
Volume 86,
Issue 4,
pp. 1374-1382,
08/15/1995
Copyright © 1995 by The American Society of Hematology
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