Transforming growth factor (TGF) activity in human urine: synergism between TGF-beta and urogastrone.
Human urine contains an acid and heat stable peptide with an apparent molecular weight of 8,000-10,000 that, in the presence of urogastrone (EGF), induces the anchorage-independent growth of nontransformed cells in semisolid media. This nonmitogenic growth-modulating activity does not compete with EGF for binding to EGF membrane receptor sites and can be resolved from EGF by high-performance liquid chromatography. The urine-derived growth factor has been purified more than 10,000-fold and shares many biochemical properties with and is functionally related to the B class of TGFs isolated from transformed cells and non-neoplastic tissues. The low molecular weight anchorage-independent growth-stimulating activity universally present in human urine is a result of the synergistic interaction of this urine-derived TGF-beta and urogastrone.
D000818:Animals; D001667:Binding, Competitive; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003114:Colony-Forming Units Assay; D004815:Epidermal Growth Factor / Q000502:physiology / Q000652:urine*; D066246:ErbB Receptors; D005260:Female; D006801:Humans; D008297:Male; D051379:Mice; D010455:Peptides / Q000502:physiology / Q000652:urine*; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism; D015291:Transforming Growth Factors
D010455:Peptides; D011956:Receptors, Cell Surface; D004815:Epidermal Growth Factor; D015291:Transforming Growth Factors; D066246:ErbB Receptors