Degradation of a cAMP-binding protein is inhibited by human c-Ha-ras gene products |
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| Authors: | T Hiwasa S Sakiyama S Noguchi J M Ha T Miyazawa S Yokoyama |
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| Institution: | 1. Department of Chemistry, Purdue University, West Lafayette, Indiana, USA;2. Department of Biological Sciences, College of Basic and Applied Sciences, Mountain Top University, Ogun state, Nigeria;3. Daniel and Fola Biotechnology Foundation, Makoko, Lagos state, Nigeria |
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| Abstract: | Incubation of the particulate fraction of cell extract prepared from NIH3T3 mouse fibroblasts resulted in preferential proteolytic degradation of a cAMP-binding protein. The proteolysis was inhibited by human c-Ha-ras gene products produced by Escherichia coli. The proteolysis was observed at pH 6 to 7, and inhibited by antipain and leupeptin. These results suggest that cAMP-binding proteins might be cleaved by thiol proteinases. In fact, c-Ha-ras gene products were proved to inhibit the cathepsin B-like activity present in the particulate fraction. |
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