Biochemical and mitogenic properties of Tamm-Horsfall urinary glycoprotein.
Thirty separate preparations of human Tamm-Horsfall urinary glycoprotein (THP) prepared from pooled urine of normal individuals were assessed for the capacity to stimulate in vitro blast transformation with normal human peripheral blood lymphocytes. Detailed studies were performed on some of these preparations by various biochemical, ultrastructural and in vitro techniques. Heterogeneity amongst the sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) profiles of several electrophoresis (2D-IEP). Gas liquid chromatographic analysis (GLC) revealed significant amounts of glucose in two of these samples. Ultrastructural studies using direct staining or platinum carbon shadowed specimens confirmed the fibrillar polymeric nature of soluble THP in vitro studies with human peripheral blood lymphocyte populations showed THP to have mitogenic properties towards B cells associated with the production of intracytoplasmic immunoglobulin. THP also stimulated the migration of mouse peritoneal exudate macrophages in a micro macrophages migration assay.
D002464:Cell Migration Inhibition; D002849:Chromatography, Gas; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D008213:Lymphocyte Activation / Q000187:drug effects*; D008264:Macrophages / Q000276:immunology; D008854:Microscopy, Electron; D009088:Mucoproteins / Q000032:analysis / Q000494:pharmacology / Q000652:urine*; D058949:Uromodulin
D009088:Mucoproteins; C548612:UMOD protein, human; C548613:Umod protein, mouse; D058949:Uromodulin