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Proteoglycan metabolism in normal and inflammatory human macrophages
L Uhlin-Hansen, T Wik, L Kjellen, E Berg, F Forsdahl and SO Kolset
Department of Biochemistry, University of Tromso, Norway.
To study proteoglycan metabolism in inflammatory macrophages, primary
cultures of human macrophages were cultured in the absence and presence of
bacterial lipopolysaccharide (LPS). When exposed to [35S]sulfate, the cells
incorporated the label almost exclusively into chondroitin sulfate
proteoglycan (CSPG), which was recovered from the culture medium and the
cell layer. Cells stimulated with LPS secreted approximately three times
more [35]CSPG into the culture medium than control cells. Furthermore, cell
adhesion was also found to promote proteoglycan secretion; when nonadherent
monocytic cells were induced to adhere, the release of proteoglycan
increased two times. The increased secretion seen in LPS-stimulated
macrophages was partly due to increased biosynthesis, but was mostly due to
increased sorting of CSPG to the secretory pathway. Only about 20% of the
CSPG synthesized in unstimulated cells was secreted, whereas the
corresponding figure in LPS-treated cells was 35%. In both cell types, the
remaining [35S]CSPG was degraded, probably in the lysosomes. The
degradation was a two-step process. First, the [35S]CSPG was rapidly
cleaved to yield free glycosaminoglycan (GAG) chains (t1/2 = 15 to 30
minutes). Secondly, the GAG chains were completely depolymerized (t1/2 = 2
to 3 hours). Neither resting nor LPS-stimulated cells sorted CSPG to
intracellular storage, as is evident in many hematopoietic cells. The
LPS-treated cells synthesized [35S]CSPG of smaller molecular size than did
control cells, with GAG chains of approximate molecular mass of 12 kD
versus 16 kD in control cells. No difference was seen in the disaccharide
composition of the GAG chains; both LPS-stimulated and unstimulated cells
expressed a mixture of 80% to 90% chondroitin 4-sulfate and 10% to 20%
chondroitin 4,6-disulfate. N-terminal sequence and Northern blot analysis
indicate that the core protein of the CSPG secreted by human macrophages is
serglycin.
Volume 82,
Issue 9,
pp. 2880-2889,
11/01/1993
Copyright © 1993 by The American Society of Hematology
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