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The Journal of Immunology, Vol 156, Issue 9 3093-3097, Copyright © 1996 by American Association of Immunologists

CUTTING EDGE

Hydroxamate-based metalloprotease inhibitor blocks shedding of L- selectin adhesion molecule from leukocytes: functional consequences for neutrophil aggregation

TA Bennett, EB Lynam, LA Sklar and S Rogelj
Department of Pathology, Cancer Research and Treatment Center, University of New Mexico School of Medicine, Albuquerque 87131, USA.

L-selectin is an adhesion molecule that mediates the recruitment of neutrophils to inflammatory sites and initiates the migration of lymphocytes into the peripheral lymph nodes. In response to cell activation, L-selectin is shed from the cell surface, and altered levels of functional soluble L-selectin are detected in the plasma of patients suffering from numerous inflammatory diseases as well as AIDS. The mechanism that regulates L-selectin shedding is poorly understood. Here we show that a hydroxamate-based metalloprotease inhibitor, N-(D,L- [2-(hydroxyaminocarbonyl)- methyl]-4-methylpentano)-L-3-(tert-butyl)- alanyl-L-alanine, 2-aminoethyl amide, which blocks leukocyte TNF, TNF receptor, and IL-6 receptor release, also inhibits L-selectin shedding from neutrophils, eosinophils, and lymphocytes. Moreover, we show that such inhibition of L-selectin shedding profoundly affects neutrophil aggregation and permits reaggregation in the presence of a heterologous stimulus.


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