CHARACTERIZATION OF ALDEHYDE DEHYDROGENASE FROM HTC RAT HEPATOMA-CELLS

CHARACTERIZATION OF ALDEHYDE DEHYDROGENASE FROM HTC RAT HEPATOMA-CELLS
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DOI:
10.1016/0304-4165(85)90137-0
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发表时间:
1985-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
通讯作者:
WINTERS, AL
WINTERS, AL
中科院分区:
其他
文献类型:
--
作者:
LINDAHL, R;BAGGETT, DW;WINTERS, AL

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我们建议发展大鼠肝癌细胞系作为研究肝癌发生过程中醛脱氢酶活性变化的调控的体外模型。从HTC大鼠肝癌细胞中一步纯化的醛脱氢酶与从大鼠肝细胞癌中分离的醛脱氢酶相同。HTC醛脱氢酶是由54-kDa亚基组成的110 kDa二聚体,优选NADP+作为辅酶,并且优先氧化苯甲醛,如芳香醛而不是苯乙醛。HTC醛脱氢酶的底物和辅酶特异性、双硫仑的作用、pH曲线和等电点也与肿瘤醛脱氢酶的这些相同性质相同。在免疫扩散中,这两种同工酶被抗HTC醛脱氢酶抗体完全识别。已经确定HTC醛脱氢酶与肝细胞癌中发现的醛脱氢酶非常相似(如果不相同的话),简化了用于检查体内和体外肿瘤醛脱氢酶活性调节的分子探针的开发。
We have proposed developing rat hepatoma cell lines as an in vitro model for studying the regulation of changes in aldehyde dehydrogenase activity occurring during hepatocarcinogenesis. Aldehyde dehydrogenase purified in a single step from HTC rat hepatoma cells is identical to the aldehyde dehydrogenase isolated from rat hepatocellular carcinomas. HTC aldehyde dehydrogenase is a 110 kDa dimer composend of 54-kDa subunits, prefers NADP+ as coenzyme, and preferentially oxidizes benzaldehyde like aromatic aldehydes but not phenylacetaldehyde. The substrate and coenzyme specificity, effects of disulfiram, pH profile and isoelectric point of HTC aldehyde dehydrogenase are also identical to these same properties of the tumor aldehyde dehydrogenase. In immunodiffusions, both isozymes are recognized with complete identity by anti-HTC aldehyde dehydrogenase antibodies. Having established that HTC aldehyde dehydrogenase is very similar, if not identical, to the aldehyde dehydrogenase found in hepatocellular carcinomas, simplifies the development of molecular probes for examination of the regulation of tumor aldehyde dehydrogenase activity in vivo and in vitro.