Transforming growth factor-␣ (TGF-␣) is synthesized as a membrane-bound precursor protein, pro-TGF-␣, that is converted to a soluble form by 2 endoproteolytic cleavages. Several factors have been implicated in the regulation of the second rate-limiting step, including protein kinase C (PKC). Earlier
Differential role of transforming growth factor-α in two human colon-carcinoma cell lines
✍ Scribed by Linda F. Watkins; Alan E. Levine
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- French
- Weight
- 702 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
✦ Synopsis
Antibodies to epidermal-growth-factor receptor (EGF) and transforming growth factor-a (TGVa) were used to determine the role of endogenous TGF-a in the growth of 2 human colon-carcinoma cell lines. Both the GEO and HCT I 16 coloncarcinoma cell lines secrete similar levels of TGF-a and have similar numbers of low-affinity binding sites for EGF. However, the HCT l 16 cells lack the high-affinity EGF binding site present on the CEO cells. The anti-EGF receptor antibodies effectively blocked the binding of Iz51-EGF to the CEO and HCT I 16 cell lines. Growth of the GEO cell line was inhibited 5040% by the anti-EGF receptor and anti-TGF-a antibodies. When the same antibodies, in sufficient amounts to block binding of TGF-a to the cells, were added to the HCT I 16 cell line, no effect on growth was seen. These results suggest that while the CEO cell line utilizes TGF-a in an autocrine manner, the TGF-a secreted by the HCT I 16 cells apparently does not play a role in the growth of these cells.
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