Myeloglycan, a Series of E-Selectin-Binding Polylactosaminolipids Found in Normal Human Leukocytes and Myelocytic Leukemia HL60 Cells

Autor: Stroud, M.R., Handa, K., Ito, K., Salyan, M.E.K., Fang, H., Levery, S.B., Hakamori, S., Reinhold, B.B., Reinhold, V.N.
Zdroj: Biochemical and Biophysical Research Communications; April 1995, Vol. 209 Issue: 3 p777-787, 11p
Abstrakt: Sialosyl-LeX(SLeX) is assumed to be the binding epitope of E- and P-selectin in normal human neutrophils and myelocytic leukemia HL60 cells. Glycosphingolipid (GSL) fractions from large quantities of normal human neutrophils and HL60 cell extract did not contain SLeXGSLs having 6-10 sugar residues, as commonly found in solid tumor cells and tissues. Instead, the binding target of E-selectin was revealed to be a series of long-chain, unbranched polylactosamine GSLs with terminally sialylated, internally α1→3 polyfucosylated structureas the major component, or having SLeXat the terminus and internally polyfucosylated structure as a minor component. These GSLs are hereby collectively termed "myeloglycan." Regardless of the site of fucosylation, all myeloglycans cross-react strongly with "anti-SLeX" monoclonal antibodies such as CSLEX, FH6, SNH3, and SNH4.
Databáze: Supplemental Index
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