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Characterization and partial purification of human epithelial transforming growth factor
D J Dunnington1, R G Scott, M A Anzano
1Department of Cell Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406-2799.
Journal of Cellular Biochemistry
|December 1, 1990
Summary
A novel human transforming growth factor-epsilon (h-TGFe) stimulates cancer cell growth. This epithelial cell-derived factor shows stability and unique properties, suggesting a new role in cell proliferation.
Area of Science:
- * Molecular and Cell Biology
- * Cancer Research
- * Biochemistry
Background:
- * Cancer cell lines are crucial models for studying tumor growth.
- * Growth factors play a significant role in regulating cell proliferation and tissue development.
- * Identifying novel growth factors can lead to new therapeutic targets for cancer.
Purpose of the Study:
- * To partially purify and characterize a novel polypeptide growth factor from human adrenocortical carcinoma cells (SW13).
- * To investigate the biological activity and properties of the purified growth factor, designated h-TGFe.
- * To determine the potential origin and prevalence of h-TGFe in human tissues and cell lines.
Main Methods:
- * Partial purification of h-TGFe from SW13 cell conditioned medium using a four-step chromatographic procedure.
- * Characterization of h-TGFe stability through exposure to low pH, urea, dithiothreitol, and sodium dodecyl sulfate.
- * Determination of molecular weight via size exclusion chromatography and binding properties using heparin and cation exchangers.
- * Analysis of elution profiles from C18 reverse-phase chromatography.
Main Results:
- * A polypeptide growth factor, h-TGFe, was partially purified from SW13 cells, stimulating anchorage-independent growth.
- * Similar growth-stimulating activity was detected in human milk and media from other epithelial cell lines.
- * h-TGFe demonstrated stability to low pH and 8M urea, but sensitivity to dithiothreitol and SDS.
- * The factor exhibited a molecular weight of 59 kDa, strong cation exchange binding, and eluted at 15-30% acetonitrile on reverse-phase chromatography.
- * h-TGFe did not bind to heparin or stimulate endothelial cell growth.
Conclusions:
- * h-TGFe is a novel growth factor produced by SW13 cells and potentially many other epithelial cells and tissues.
- * The unique biochemical properties of h-TGFe suggest it may play a distinct role in epithelial cell biology and cancer.
- * Further research into h-TGFe could elucidate its function in normal and malignant epithelial tissues.