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*
Institute for Immunology, University Hospital, Hamburg, Germany; and
The Jackson Laboratory, Bar Harbor, ME 04609
T cells proteolytically shed the ectodomains of several cell
surface proteins and, thereby, can alter their responsiveness and can
release soluble intercellular regulators. ART2.2 is a GPI-anchored
ecto-ADP-ribosyltransferase (ART) related to ADP-ribosylating bacterial
toxins. ART2.2 is expressed exclusively by mature T cells. Here we show
that ART2.2 is shed from the cell surface in enzymatically active form
upon activation of T cells. Shedding of ART2.2 resembles that of
L-selectin (CD62L) in dose response, kinetics of release, and
sensitivity to the metalloprotease inhibitor Immunex Compound 3,
suggesting that ART2.2, like CD62L, is cleaved by TNF-
-converting
enzyme or by another metalloprotease. ART2.2 shed from activated T
cells migrates slightly faster in SDS-PAGE analyses than does ART2.2
released upon cleavage of the GPI anchor. This indicates that shedding
of ART2.2 is mediated by proteolytic cleavage close to its membrane
anchor. Shed ART2.2 is enzymatically active and ADP-ribosylates several
substrates in vitro. Thus, shedding of ART2.2 releases a potential
intercellular regulator. Finally, using a new FACS assay for monitoring
ADP-ribosylation of cell surface proteins, we demonstrate that shedding
of ART2.2 correlates with a reduced sensitivity of T cell surface
proteins to ADP-ribosylation. Our findings suggest that by shedding
ART2.2 the activated T cell not only releases a potential intercellular
regulator but also may alter its responsiveness to immune regulation by
ART2.2-mediated ADP-ribosylation of cell surface
proteins.
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