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J Biol Chem, Vol. 274, Issue 7, 4459-4466, February 12, 1999
From the Department of Biochemistry, Institute of Medical Science,
University of Tokyo, 4-6-1 Shirokane-dai,
Minato-ku, Tokyo 108-0071, Japan
Tamm-Horsfall glycoprotein (THGP) and the
oligosaccharide fraction liberated from THGP by hydrazinolysis
inhibited tetanus toxoid-induced T cell proliferation. Intact THGP
showed approximately 100-fold more inhibitory activity than the
free oligosaccharides. After fractionating the oligosaccharides by
anion-exchange column chromatography, the inhibitory activity could be
detected in a sialidase-resistant acidic oligosaccharide fraction
(fraction AR). The inhibitory activity of fraction AR was not observed
when the fraction was added to the T cell culture medium 24 h
after the addition of tetanus toxoid. Increased concentration of
interleukin (IL) 1
and decreased concentration of IL-2 were observed
in the T cell culture medium after the addition of fraction AR. The
oligosaccharides in fraction AR also inhibited the growth of an
IL-1-dependent cell line, D10-G4. These results strongly
suggested that the oligosaccharides in fraction AR bind to IL-1
and
suppress its cytokine activity. IL-1
actually bound to the fraction
AR immobilized on an amino-bonded thin layer plate. Fractionation of
the oligosaccharides indicated that only oligosaccharides containing an
N-acetylgalactosamine residue and a sulfate residue bound
specifically to IL-1
. Removal of either the sulfate residue or the
N-acetylgalactosamine residue from the oligosaccharides
abolished both the proliferation-inhibition and IL-1
binding
activities. Since IL-1
did not bind to thyroid-stimulating hormone,
which has the sulfate group at C-4 of the
N-acetylgalactosamine residue in its N-linked
sugar chains, the binding of IL-1
toward oligosaccharides in
fraction AR was considered to be highly specific.
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