Purification and immunochemical characterization of aldehyde dehydrogenase from 2-acetylaminofluoreneinduced rat hepatomas

Lindahl, Ronald; Feinstein, Robert N.

doi:10.1016/0005-2744(76)90184-4

Cited by 50 publications

(23 citation statements)

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“…It is also noteworthy, since tumor ALDH functions as a multimer (dimer) with relatively large (M, 50,000) subunits, that the pTALDH cDNA encodes a functional ALDH that possesses many properties of tumor ALDH (Table 1) (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). Like authentic tumor ALDH, the pTALDH-encoded polypeptide prefers aromatic aldehydes as substrate and NADP+ as coenzyme.…”

Section: Resultsmentioning

confidence: 99%

“…The tumor ALDH isozyme has a Mr of 110,000 and is composed of two apparently identical subunits. While the tumor ALDH isozyme shares identical subunit size (Mr. 54,000) with the normal liver ALDH isozymes, it is a distinctly different enzymatic species based on electrophoretic mobility, isoelectric point, sensitivity to inhibitors, substrate and coenzyme preference, and immunologic crossactivity (1,4,(12)(13)(14)(15).…”

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confidence: 99%

“…The tumor ALDH isozyme has been purified from a variety of sources and its properties have been described (1,13,14). The tumor ALDH isozyme has a Mr of 110,000 and is composed of two apparently identical subunits.…”

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confidence: 99%

“…This phenotype is characterized by an increase in total ALDH activity due to the appearance of a cytosolic isozyme undetectable in normal rat liver. This isozyme preferentially oxidizes aromatic aldehyde substrates using NADP+ as coenzyme and differs from normal liver ALDH isozymes in a number of physical and functional properties (1,4,12,13).…”

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confidence: 99%

“…Previous work has shown that a tumor-associated aldehyde dehydrogenase (tumor ALDH) can be induced by a number of different chemical carcinogens during rat hepatocarcinogenesis (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). This phenotype is characterized by an increase in total ALDH activity due to the appearance of a cytosolic isozyme undetectable in normal rat liver.…”

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confidence: 99%

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Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase.

Jones

Brennan

Hempel

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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To study the mechanism(s) controlling expression of the tumor-associated aldehyde dehydrogenase (tumor ALDH), which appears during rat hepatocarcinogenesis, cDNAs encoding this isozyme were cloned and identified with an antibody probe. Poly(A)-containing RNA from HTC rat hepatoma cells, which have been shown to possess high levels of tumor ALDH, was used as template to synthesize double-stranded cDNA. The cDNA was methylated to protect internal sites. Two different synthetic DNA linkers were added sequentially to the cDNA to insure correct orientation for expression from the lac promoter of pUC8. A library of 100,000 independent members carrying inserts >1 kilobase was obtained. From this library, two apparently identical tumor ALDH clones, differing only in size, were identified with an indirect immunological probe. The larger of the cDNA clones identified, pTALDH, was chosen for further study. Interestingly, since tumor ALDH is a dimeric enzyme, pTALDH directs synthesis of a functional tumor ALDH in the bacterial cell. The cDNA sequence has been confirmed by comparison to the amino acid sequence of tumor ALDH purified from HTC cells.

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Section: Resultsmentioning

confidence: 99%

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Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase.

Jones

Brennan

Hempel

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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Comparative subcellular distribution of benzaldehyde and acetaldehyde dehydrogenase activities in two hepatoma cell lines and in normal hepatocytes

Ferro

Muzio

Bassi

et al. 1991

Cell Biochemistry & Function

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The NAD- and NADP-dependent aldehyde dehydrogenase (ALDH) activities were evaluated in two rat hepatoma cell lines, namely the well-differentiated MH1C1 line and the less differentiated HTC line. Each activity was determined in parallel in isolated rat hepatocytes, for comparison. The aliphatic aldehyde acetaldehyde (ACA) and the aromatic aldehyde benzaldehyde (BA) were used as substrates. With the first substrate the ALDH activities found in the crude cytoplasmic extracts were lower in hepatoma cells than in normal hepatocytes, especially when measured with NADP as coenzyme (ACA/NADP). Otherwise, with benzaldehyde as substrate the NAD-dependent enzyme activity (BA/NAD) was increased about 9-fold in HTC cells over hepatocytes and decreased in MH1C1 cells, while the NADP-dependent (BA/NADP) activity was increased 38- and 2.5-fold in HTC and MH1C1 cell lines, respectively. Studies on the subcellular distribution of these enzyme activities showed that the activity measured with acetaldehyde and NAD (ACA/NAD) was almost equally distributed between the cytosol and the subcellular particles in the three cell populations, but the ACA/NADP activity was shifted towards the cytosolic compartment in hepatomas, especially in HTC cells. The BA/NAD and BA/NADP ALDH activities found in the organelles of hepatoma cells were markedly reduced in comparison with hepatocytes, in favour of the cytosol. The most striking difference between the normal and the transformed cells was the 94-fold increase over hepatocytes of the BA/NADP activity, found in the cytosolic fractions of HTC cells. MH1C1 cells showed a less pronounced (7.5-fold) enhancement of this tumour-associated specific activity.(ABSTRACT TRUNCATED AT 250 WORDS)

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Drug‐metabolizing enzymes in liver, olfactory, and respiratory epithelium of cattle

Longo¹,

Mazzaccaro²,

Naldi³

et al. 1991

J. Biochem. Toxicol.

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The drug-metabolizing enzymes of olfactory and respiratory epithelium of cattle were determined. The data of nasal tissues were compared to those of bovine liver. Both oxidative and nonoxidative enzyme activities were investigated. Many compounds including testosterone were used as substrates for the P450-dependent monooxygenase activities. The results demonstrated that the P450 content and all the activities assayed including reduced nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome P450 reductase were much higher in the olfactory than in the respiratory mucosa and for some activities (hexamethyl-phosphoramide and dimethylnitrosamine N-demethylase, aniline hydroxylase, and ethoxycoumarin O-deethylase) the values in the olfactory tissue were even markedly higher than those of liver. Also the activities of some nonoxidative enzymes such as glutathione S-transferase, uridine 5'-diphosphate (UDP)-glucuronyl-transferase, and epoxide hydrolase were higher in the olfactory than in the respiratory mucosa but lower than in liver. The results taken together suggest that the olfactory and respiratory epithelium of cattle, which contain in addition to a wide array of nonoxidative enzymes multiple forms of P450, can be useful and easily available tissues to study the biotransformation processes of odorants.

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Purification and immunochemical characterization of aldehyde dehydrogenase from 2-acetylaminofluoreneinduced rat hepatomas

Cited by 50 publications

References 8 publications

Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase.

Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase.

Comparative subcellular distribution of benzaldehyde and acetaldehyde dehydrogenase activities in two hepatoma cell lines and in normal hepatocytes

Drug‐metabolizing enzymes in liver, olfactory, and respiratory epithelium of cattle

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