Degradation of a cAMP-binding protein is inhibited by human c-Ha-ras gene products.
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.
Hiwasa
T
T
Sakiyama
S
S
Noguchi
S
S
Ha
J M
JM
Miyazawa
T
T
Yokoyama
S
S
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002373:Cyclic AMP Receptor Protein; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D051379:Mice; D009857:Oncogenes; D011480:Protease Inhibitors; D011518:Proto-Oncogene Proteins / Q000494:pharmacology*; D016283:Proto-Oncogene Proteins p21(ras); D014357:Trypsin / Q000378:metabolism
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D011480:Protease Inhibitors; D011518:Proto-Oncogene Proteins; D010450:Endopeptidases; D014357:Trypsin; D003546:Cysteine Endopeptidases; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)