c-Ha-Ras mutants with point mutations in Gln-Val-Val region have reduced inhibitory activity toward cathepsin B.
Protease-inhibitory activity of recombinant Ha-ras gene products (Ras) toward papain and cathepsins B and L was investigated. v-Ha-Ras showed more potent inhibitory activity toward cathepsin B as compared with c-Ha-Ras. We have also investigated protease-inhibitory activity of c-Ha-Ras mutants with point mutations in amino acids between positions 23 and 50. Inhibitory activity of Ras toward papain and cathepsin L was not largely altered among mutants. However, the inhibitory activity toward cathepsin B was significantly impaired by a mutation at position 43, 44, 45 or 48. These results suggest that 43Gln-Val-Val sequence plays an important role at least to inhibit cathepsin B.
Division of Biochemistry, Chiba Cancer Center Research Institute, Japan.
T
T
Hiwasa
J
J
Fujita-Yoshigaki
M
M
Shirouzu
H
H
Koide
T
T
Sawada
S
S
Sakiyama
S
S
Yokoyama
D000595:Amino Acid Sequence; D002401:Cathepsin B / Q000378:metabolism*; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D011905:Genes, ras / Q000235:genetics*; D008969:Molecular Sequence Data; D015689:Oncogene Protein p21(ras) / Q000378:metabolism*; D010206:Papain / Q000378:metabolism*; D017354:Point Mutation
D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056668:Cathepsin L; D010206:Papain; D015689:Oncogene Protein p21(ras)