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Blood, Vol. 95 No. 2 (January 15), 2000:
pp. 602-609
Soluble VCAM-1 binding to  4 integrins is cell-type specific and
activation dependent and is disrupted during apoptosis in T cells
David M. Rose,
Pina M. Cardarelli,
Ronald R. Cobb, and
Mark H. Ginsberg
From the Department of Vascular Biology, The Scripps Research
Institute, La Jolla, and Tanabe Research Laboratories, San Diego, CA.
Soluble vascular cell adhesion molecule-1 (sVCAM-1) is generated
during inflammation and can alter lymphocyte functions. The authors
report that the binding of sVCAM-1 to  4 integrin-bearing cells is a
dynamically regulated, active cellular process. Binding of recombinant
sVCAM-1 to 4 integrins on peripheral blood mononuclear cells was
cell-type specific. Circulating CD16+ NK cells constitutively bound sVCAM-1 with high affinity, whereas a subpopulation of
T-lymphocytes, primarily CD45RO+ (memory), bound sVCAM-1 only after
phorbol ester stimulation. sVCAM-1 binding to homogenous stable cell
lines was also cell-type specific, and required active cellular
processes because it was blocked by the inhibition of ATP synthesis and by Fas-induced apoptosis. Indeed, the loss of high-affinity VCAM-1 binding was an early event in apoptosis. Furthermore, an
H-Ras/Raf-initiated signaling pathway also suppressed sVCAM-1 binding
to 4 1 integrins. Collectively, these results showed that the
capacity of 4 integrins to bind VCAM-1 is actively regulated and
that this regulation may control 4 integrin-dependent cellular functions.
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