Title : Detection of novel carbohydrate binding activity of
interleukin-1
Abstract :
- 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) 1beta 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-1beta and suppress its cytokine activity
- IL-1beta 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-1beta
- Removal of either the sulfate residue or the N-acetylgalactosamine residue from the oligosaccharides abolished both the proliferation-inhibition and IL-1beta binding activities
- Since IL-1beta 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-1beta toward oligosaccharides in fraction AR was considered to be highly specific
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. interleukin-1, , interleukin-1, novel carbohydrate binding activity, -
- 1. glycoprotein, , THGP, -, -
- 1. glycoprotein, , Tamm-Horsfall glycoprotein, -, -
- 1. liberated, , THGP, the oligosaccharide fraction, -
- 11. chains, , -, the N-acetylgalactosamine residue, residue in
- 11. has, , thyroid-stimulating hormone, the N-acetylgalactosamine residue, -
- 11. residue, , -, its N-linked sugar chains, residue in
- 11. residue, , -, the N-acetylgalactosamine residue, residue in
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):