C-HA-RAS MUTANTS WITH POINT MUTATIONS IN GLN-VAL-VAL REGION HAVE REDUCED INHIBITORY ACTIVITY TOWARD CATHEPSIN-B

被引:19
作者
HIWASA, T [1 ]
FUJITAYOSHIGAKI, J [1 ]
SHIROUZU, M [1 ]
KOIDE, H [1 ]
SAWADA, T [1 ]
SAKIYAMA, S [1 ]
YOKOYAMA, S [1 ]
机构
[1] UNIV TOKYO,FAC SCI,DEPT BIOPHYS & BIOCHEM,BUNKYO KU,TOKYO 113,JAPAN
关键词
C-HA-RAS; ONCOGENE PRODUCT; PROTEASE INHIBITOR; CATHEPSIN;
D O I
10.1016/0304-3835(93)90169-A
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
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.
引用
收藏
页码:161 / 165
页数:5
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