ADP-RIBOSYLATION OF RHO-PROTEINS IS INHIBITED BY MELITTIN, MAST-CELL DEGRANULATING PEPTIDE AND COMPOUND-48/80
ADP-RIBOSYLATION OF RHO-PROTEINS IS INHIBITED BY MELITTIN, MAST-CELL DEGRANULATING PEPTIDE AND COMPOUND-48/80
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DOI：
10.1016/0922-4106(92)90086-b
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发表时间：
1992-05-12
期刊：
影响因子：
--
通讯作者：
AKTORIES, K
中科院分区：
文献类型：
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作者：
KOCH, G;HABERMANN, B;AKTORIES, K
两亲性试剂蜂毒素、肥大细胞脱颗粒肽和化合物48/80抑制肉毒梭菌外酶C3对小GTP结合蛋白Rho的ADP-核糖化。化合物48/80、肥大细胞脱颗粒肽、蜂毒素分别在8和25mU·g/ml、10和45mU·m~(-1)、15和50mU·m~(-1)时，对ADP-核糖化的抑制分别为90%和50%。此外，这些化合物还通过增加GDP/GTP交换增加了Rho蛋白的稳态GTP水解率和GTP结合的缔合和解离速率。数据表明，被测试的两亲性试剂与Rho蛋白家族的小GTP结合蛋白相互作用。
The amphiphilic agents melittin, mast cell degranulating peptide and compound 48/80 inhibit the ADP-ribosylation of the small GTP-binding proteins rho by Clostridium botulinum exoenzyme C3. Half-maximal and maximal inhibition (> 90%) of ADP-ribosylation occurred at about 8 and 25-mu-g/ml for compound 48/80, at 10 and 45-mu-M for mast cell degranulating peptide and at 15 and 50-mu-M for melittin, respectively. In addition, these compounds increase the steady state GTP hydrolysis and the association and dissociation rate of GTP-binding of rho proteins through an increase of GDP/GTP exchange. The data suggest that the amphiphilic agents tested interact with small GTP-binding proteins of the rho protein family.