TY - JOUR
T1 - Evidence for a novel function of E-selectin in neutrophil recruitment unrelated to leukocyte rolling
AU - Ramos, C. L.
AU - Kunkel, E. J.
AU - Jung, U.
AU - Norton, C. R.
AU - McIntyre, K. W.
AU - Gillooly, K. M.
AU - Lawrence, M. B.
AU - Vestweber, D.
AU - Wolitzky, B. A.
AU - Ley, K.
PY - 1996
Y1 - 1996
N2 - The functional effects of three monoclonal antibodies (mAbs) raised against murine E-selectin, 9A9, 10E6 and IOE9.6, on neutrophil recruitment, leukocyte rolling and circulating leukocyte concentrations in vivo, as well as adhesion of myeloid cells to E-selectin transfectants and recombinant E-selectin-IgG fusion protein in vitro were investigated. MAbs 9A9 and 10E6 map to the lectin and EGF-like domains of murine E-selectin, while mAb 10E9.6 binds to the consensus repeat region. IOE9.6 blocked neutrophil recruitment to peritonitis induced by injection of thioglycollate into Balb/c mice by more than 90%, while 9A9 and 10E6 showed only partial effects (<50% inhibition). Neither 9A9 nor IOE9.6 alone blocked leukocyte rolling in TNF-o treated venules of Balb/c mice, but 9A9 almost completely inhibited leukocyte rolling when combined with the function-blocking murine P-selectin mAb, RB40.34. In contrast, 10E9.6 had no effect on leukocyte rolling in RB40.34-treated Balb/c or C57BL/6 mice. 10E9.6 did not affect adhesion of myeloid cells to Eselectin transfectants nor attachment, rolling and detachment of myeloid cells to murine E-selectin-IgG fusion protein. However, adhesion was completely blocked in the same assays by 9A9. Taken together, these results indicate that E-selectin serves a function, other than rolling, that may be critically important for neutropohil recruitment to inflammatory sites in Balb/c mice. Supported in part by NIH HL54136 and HL07284.
AB - The functional effects of three monoclonal antibodies (mAbs) raised against murine E-selectin, 9A9, 10E6 and IOE9.6, on neutrophil recruitment, leukocyte rolling and circulating leukocyte concentrations in vivo, as well as adhesion of myeloid cells to E-selectin transfectants and recombinant E-selectin-IgG fusion protein in vitro were investigated. MAbs 9A9 and 10E6 map to the lectin and EGF-like domains of murine E-selectin, while mAb 10E9.6 binds to the consensus repeat region. IOE9.6 blocked neutrophil recruitment to peritonitis induced by injection of thioglycollate into Balb/c mice by more than 90%, while 9A9 and 10E6 showed only partial effects (<50% inhibition). Neither 9A9 nor IOE9.6 alone blocked leukocyte rolling in TNF-o treated venules of Balb/c mice, but 9A9 almost completely inhibited leukocyte rolling when combined with the function-blocking murine P-selectin mAb, RB40.34. In contrast, 10E9.6 had no effect on leukocyte rolling in RB40.34-treated Balb/c or C57BL/6 mice. 10E9.6 did not affect adhesion of myeloid cells to Eselectin transfectants nor attachment, rolling and detachment of myeloid cells to murine E-selectin-IgG fusion protein. However, adhesion was completely blocked in the same assays by 9A9. Taken together, these results indicate that E-selectin serves a function, other than rolling, that may be critically important for neutropohil recruitment to inflammatory sites in Balb/c mice. Supported in part by NIH HL54136 and HL07284.
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M3 - Article
AN - SCOPUS:33749173028
SN - 0892-6638
VL - 10
SP - A610
JO - FASEB Journal
JF - FASEB Journal
IS - 3
ER -