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Blood, Vol. 94 No. 4 (August 15), 1999:
pp. 1313-1318
A Critical Role for N-ethylmaleimide-Sensitive Fusion Protein
(NSF) in Platelet Granule Secretion
János Polgár and
Guy L. Reed
From the Harvard School of Public Health, Cardiovascular Biology
Laboratory, Boston, MA.
The molecular mechanisms that regulate membrane targeting/fusion
during platelet granule secretion are not yet understood. N-ethylmaleimide-sensitive fusion protein (NSF), soluble NSF
attachment proteins (SNAPs), and SNAREs (SNAP receptors) are elements
of a conserved molecular machinery for membrane targeting/fusion that
have been detected in platelets. We examined whether NSF, an ATPase
that has been shown to play a critical role in membrane targeting/fusion in many cell types, is necessary for platelet granule
secretion. Peptides that mimic NSF sequence motifs inhibited both
 -granule and dense-granule secretion in permeabilized human platelets. This inhibitory effect was sequence-specific, because neither proteinase K-digested peptides nor peptides containing similar
amino acids in a scrambled sequence inhibited platelet secretion. The
peptides that inhibited platelet granule secretion also inhibited the
human recombinant -SNAP-stimulated ATPase activity of recombinant
NSF. It was also found that anti-NSF antibodies, which inhibited
recombinant -SNAP-stimulated ATPase activity of NSF, inhibited
platelet granule secretion in permeabilized cells. The inhibition by
anti-NSF antibodies was abolished by the addition of recombinant NSF.
These data provide the first functional evidence that NSF plays an
important role in platelet granule secretion.
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