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Transforming growth factor (TGF) activity in human urine: Synergism between TFG‐beta and urogastrone
Author(s) -
Twardzik Daniel R.,
Sherwin Stephen A.
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240280407
Subject(s) - urine , transforming growth factor , receptor , medicine , endocrinology , growth factor , peptide , epidermal growth factor , biological activity , chemistry , transforming growth factor beta , beta (programming language) , biology , biochemistry , computer science , in vitro , programming language
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 nonneoplastic 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.