Altered glycosaminoglycan production by HL-60 cells treated with 4-
methylumbelliferyl-beta-D-xyloside
SD Luikart, JL Sackrison and CV Thomas
Glycosaminoglycans, mainly chondroitin 4-sulfate, are located in the
primary granules of human myeloid cells. These polyanionic carbohydrates
are believed to play an important role in leukocyte maturation and
function. To study the effect of altered chondroitin sulfate metabolism on
human promyelocytic leukemia cells, we have treated HL-60 cells with
4-methylumbelliferyl-beta-D-xyloside. beta-D- Xylosides initiate the
synthesis of free chondroitin sulfate chains. Cytochemical studies of
treated cells demonstrated a marked increase in cytoplasmic granules
stained with cationic dyes. This was confirmed by radiolabeled precursor
incorporation studies that demonstrated a 344% increase in 35S-sulfate
uptake into glycosaminoglycans associated with the cells and a 39% increase
in incorporation into glycosaminoglycans released into the media.
Chromatographic analyses of these glycosaminoglycans from treated cells
demonstrated that the newly formed chondroitin sulfate chains were not
attached to protein core and were of shorter length, but of greater charge
density than chondroitin sulfate produced by control cells. Thus,
beta-D-xyloside appears to alter the protein linkage, chain length, and
sulfation of chondroitin sulfate produced by HL-60 cells, and these changes
are morphologically evident. These biochemically altered cells may provide
important information concerning the role of these macromolecules in
myeloid development.
Volume 66,
Issue 4,
pp. 866-872,
10/01/1985
Copyright © 1985 by The American Society of Hematology
