[HTML][HTML] Involvement of a metalloprotease in the shedding of human neutrophil FcγRIIIB

PJ Middelhoven, A Ager, D Roos, AJ Verhoeven - FEBS letters, 1997 - Elsevier
PJ Middelhoven, A Ager, D Roos, AJ Verhoeven
FEBS letters, 1997Elsevier
FcγRIIIb is a glycosylphosphatidylinositol (GPI)-anchored, low-affinity IgG receptor,
expressed exclusively on human neutrophils. Upon activation or apoptosis of neutrophils,
FcγRIIIb is shed from the cell surface, but the enzyme (s) responsible for this process is (are)
still unknown. Recently, metalloproteases have been suggested to mediate the shedding of
cell surface proteins such as l-selectin and TNF-α. Using hydroxamic acid-based inhibitors
of this class of proteases (BB-3103, Ro31-9790), we have observed a clear inhibitory effect …
FcγRIIIb is a glycosylphosphatidylinositol(GPI)-anchored, low-affinity IgG receptor, expressed exclusively on human neutrophils. Upon activation or apoptosis of neutrophils, FcγRIIIb is shed from the cell surface, but the enzyme(s) responsible for this process is (are) still unknown. Recently, metalloproteases have been suggested to mediate the shedding of cell surface proteins such as l-selectin and TNF-α. Using hydroxamic acid-based inhibitors of this class of proteases (BB-3103, Ro31-9790), we have observed a clear inhibitory effect on FcγRIIIb shedding after PMA stimulation of neutrophils or induction of apoptosis. These inhibitors did not affect PMA-induced degranulation or superoxide generation.
Elsevier