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Native cytokines do not bind to uromodulin (Tamm‐Horsfall glycoprotein)
Author(s) -
Moonen Peter,
Gaffner Raymond,
Wingfield Paul
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81446-7
Subject(s) - tamm–horsfall protein , chemistry , tumor necrosis factor alpha , recombinant dna , glycoprotein , size exclusion chromatography , plasma protein binding , biophysics , chromatography , biochemistry , biology , immunology , urine , gene , enzyme
Uromodulin bound with high affinity to human tumour necrosis factor (TNF) coated on microtitre plates. This interaction was not competitively inhibited by native TNF in solution. No interaction was observed between immobilized uromodulin and TNF in the liquid phase unless conditions were chosen which denatured the latter protein. Recombinant interleukin‐1α adsorbed on microtitre plates also interacted with uromodulin. However, gel filtration experiments demonstrated no interaction between the proteins in the liquid phase. These and additional results indicate that uromodulin interacts with denatured cytokines, but not with native, soluble cytokines.