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*
Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;
Oncology Drug Discovery, Bristol-Myers Squibb, Princeton, NJ 08543;
The Maxwell Finland Laboratory for Infectious Diseases, Boston University School of Medicine, Boston, MA 02118; and
§
Department of Pathology, Brigham and Women’s Hospital, Boston, MA 02115
Taxol, a potent antitumor agent that binds ß-tubulin and promotes
microtubule assembly, results in mitotic arrest at the G2/M
phase of the cell cycle. More recently, Taxol was shown to be a potent
LPS mimetic in murine, but not in human macrophages, stimulating
signaling pathways and gene expression indistinguishably from LPS.
Although structurally unrelated to LPS, Taxol’s LPS-mimetic activities
are blocked by inactive structural analogues of LPS, indicating that
despite the species-restricted effects of Taxol, LPS and Taxol share a
common receptor/signaling complex that might be important in
LPS-induced human diseases. To identify components of the putatively
shared Taxol/LPS receptor, a novel, photoactivatable Taxol analogue was
employed to identify unique Taxol-binding proteins in murine macrophage
membranes. Seven major Taxol-binding proteins, ranging from 
50 to
200 kDa, were detected. Although photoactivatable Taxol analogue failed
to bind to CD14, the prominent Taxol-binding protein was identified as
CD18, the 96-kDa common component of the ß2 integrin
family. This finding was supported by the concomitant failure of
macrophage membranes from Mac-1 knockout mice to express immunoreactive
CD18 and the major Taxol-binding protein. In addition, Taxol-induced
IL-12 p40 mRNA was markedly reduced in Mac-1 knockout macrophages and
anti-Mac-1 Ab blocked secretion of IL-12 p70 in Taxol- and
LPS-stimulated macrophages. Since CD18 has been described as a
participant in LPS-induced binding and signal transduction, these data
support the hypothesis that the interaction of murine CD18 with Taxol
is involved in its proinflammatory activity.
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