The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity.
The major excreted protein of transformed mouse cells is an acid activable cysteine protease. In this paper, oxidized insulin B chain is shown to be a substrate for this protease. By isolation and analysis of the insulin B peptides generated by the protease, the bond specificity of this protease was determined. The bonds preferentially cleaved are glu13-ala14, leu17-val18, and tyr26-thr27. No obvious preference for a specific amino acid was found in these studies. The bond specificity of this cysteine protease for oxidized insulin B chain has been compared with that of other proteases, and it is the same as that reported for cathepsin L, suggesting that the major excreted protein and cathepsin L may be the same protein.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000032:analysis*; D002471:Cell Transformation, Neoplastic; D002472:Cell Transformation, Viral; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000378:metabolism; D051379:Mice
D000596:Amino Acids; D007328:Insulin; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; C534278:Ctsl protein, mouse