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Blood, 15 May 2001, Vol. 97, No. 10, pp. 3251-3258
PHAGOCYTES
Phosphoinositide 3-kinase modulation of  3-integrin
represents an endogenous "braking" mechanism during neutrophil
transmatrix migration
Walter J. Bruyninckx,
Katrina M. Comerford,
Donald W. Lawrence, and
Sean P. Colgan
From the Center for Experimental Therapeutics and
Reperfusion Injury, Brigham and Women's Hospital, Harvard Medical
School, Boston, Massachusetts, and the Department of Biology, Hanover
College, Indiana.
During episodes of inflammation, neutrophils (polymorphonuclear
leukocytes [PMNs]) encounter subendothelial matrix substrates that
may require additional signaling pathways as directives for movement
through the extracellular space. Using an in vitro endothelial and
epithelial model, inhibitors of phosphoinositide 3-kinase (PI3K) were
observed to promote chemoattractant-stimulated migration by as much as
8 ± 0.3-fold. Subsequent studies indicated that PMNs respond
in a similar manner to RGD-containing matrix substrates and that
PMN-matrix interactions are potently inhibited by antibodies directed
against  3- but not 1-integrin antibodies,
and that PI3K inhibitors block 3-integrin dependence.
Biochemical analysis of intracellular 3-integrin
uncoupling by PI3K inhibitors revealed diminished
3-integrin tyrosine phosphorylation and decreased association with p72syk. Similarly, the p72syk
inhibitor piceatannol promoted PMN transmatrix migration, whereas HIV-tat peptide-facilitated loading of peptides corresponding to the
3-integrin cytoplasmic tail identified the functional tyrosine residues for this activity. These data indicate that PI3K-regulated 3-integrin represents a natural
"braking" mechanism for PMNs during transit through the
extracellular matrix.
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