The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in breast cancer

Jelski, Wojciech; Chrostek, Lech; Szmitkowski, Maciej; Markiewicz, W.

doi:10.1007/s10238-006-0101-z

Cited by 35 publications

(30 citation statements)

References 49 publications

(29 reference statements)

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“…ADH activity seems to be elevated in the cancer cells from patients with gastrointestinal tumors compared with the corresponding normal cells [Jelski et al, 2004[Jelski et al, , 2007. At the same time in breast cancer cells the ADH activity is as low as in healthy counterparts [Jelski et al, 2006]. This indicates the heterogeneity of ADH activity in respect of the origin of tumor cells.…”

Section: Discussionmentioning

confidence: 89%

Expression and activity of alcohol and aldehyde dehydrogenases in melanoma cells and in melanocytes

Amann¹,

Hofmann²,

Freudenberger³

et al. 2012

J of Cellular Biochemistry

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Disturbances in vitamin A metabolism are an important attribute of some cancer cells. Most evidence point that these disturbances lead to decreasing of the retinoic acid concentration in tumor cells. Up to now, in benign and malignant skin cells the features of vitamin A metabolism with its participating enzymes are not entirely understood. Alcohol and aldehyde dehydrogenases (ALDH) are involved in the retinol metabolism, oxidizing retinol, and retinal in retinoic acid or reducing retinal in retinol. In this work we investigated the expression and enzymatic activity of alcohol and ALDH in melanoma cells compared to their benign counterparts. We demonstrated that melanoma cell lines and melanocytes despite similar pattern of the enzyme expression, show different general ALDH activity. Retinal, the substrate of ALDH, could stimulate the ALDH activity through up-regulation of retinaldehyde dehydrogenase 1 and aldehyde dehydrogenase 6. Furthermore, we found that retinoids regulate alcohol dehydrogenase activity, probably via effects on alcohol dehydrogenase expression at the post-transcriptional level. We suggest that melanoma cells in contrast to melanocytes should favor the retinal reduction over its oxidation. The decreasing cellular amount of the precursor molecules of retinoic acid could result in a changed gene regulation in melanoma cells.

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Section: Discussionmentioning

confidence: 89%

Expression and activity of alcohol and aldehyde dehydrogenases in melanoma cells and in melanocytes

Amann¹,

Hofmann²,

Freudenberger³

et al. 2012

J of Cellular Biochemistry

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“…Aldehyde dehydrogenase activity was measured using the fluorogenic method based on the oxidation of 6-methoxy-2-naphtaldehyde to the fluorescent 6-methoxy-2 naphtoate [5,7]. The fluorescence was read at an excitation wavelength of 310 and an emission wavelength of 360 nm on a Shimadzu RF-5301 spectrofluorophotometer (Shimadzu Europa GmbH, Duisburg, Germany).…”

Section: Determination Of Total Aldh Activitymentioning

confidence: 99%

The diagnostic value of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) measurement in the sera of gastric cancer patients

et al. 2010

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Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in gastric cancer cells (GC). Moreover, the activity of total ADH and class IV isoenzymes is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is probably reflected in the sera and could thus be helpful for diagnostics of gastric cancer. The aim of this study was to investigate a potential role of ADH and ALDH as tumor markers for gastric cancer. We defined diagnostic sensitivity, specificity, predictive value for positive and negative results, and receiver-operating characteristics (ROC) curve for tested enzymes. Serum samples were taken from 168 patients with gastric cancer before treatment and from 168 control subjects. Total ADH activity and class III and IV isoenzymes were measured by photometric but ALDH activity and ADH I and II by the fluorometric method, with class-specific fluorogenic substrates. There was significant increase in the activity of ADH IV isoenzyme and ADH total in the sera of gastric cancer patients compared to the control. The diagnostic sensitivity for ADH IV was 73%, specificity 79%, positive and negative predictive values were 81 and 72% respectively. Area under ROC curve for ADH IV was 0.67. The results suggest a potential role for ADH IV as marker of gastric cancer.

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“…We Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with colorectal cancer hypothesised that the changed activities of these enzymes in cancer cells were reflected in the serum and perhaps could thus be helpful for diagnosing colorectal cancer. But it is necessary to remember that isoenzymes of ADH and ALDH are present in large quantities in the liver, and also occur in the different organs such as gastrointestinal tract, lungs, kidneys and breast [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with colorectal cancer

et al. 2007

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Various isoenzymes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) exist in human colorectal mucosa. In our last experiments we have shown that ADH and ALDH are present also in colorectal cancer cells. Moreover the activities of total ADH and class I isoenzymes were significantly higher in cancer tissue than healthy mucosa. This may suggest that these changes may be reflected by enzyme activity in the serum. Therefore, we have measured the activity of total ADH, and classes I-IV of this enzyme and ALDH in the sera of patients suffering from this cancer. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline (NDMA) as a substrate and ALDH activity by the fluorometric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I and II isoenzymes we employed fluorometric methods, with class-specific fluorogenic substrates. The activity of class III ADH was measured by the photometric method with formaldehyde and class IV with m-nitrobenzaldehyde as a substrate. Serum samples were taken for routine biochemical investigations from 52 patients with colorectal carcinoma before treatment. A statistically significant increase of class I ADH isoenzymes was found. Therefore the total ADH activity was also significantly increased. The total ALDH and the activity of other tested ADH isoenzymes were unchanged. We also observed the increasing tendency of ADH I activity in accordance with the advance of disease. The activity of class I ADH isoenzymes was elevated in the serum of patients with colorectal cancer. This activity was derived from colorectal cancer cells and probably from severely damaged liver by metastatic disease.

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The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in breast cancer

Cited by 35 publications

References 49 publications

Expression and activity of alcohol and aldehyde dehydrogenases in melanoma cells and in melanocytes

Expression and activity of alcohol and aldehyde dehydrogenases in melanoma cells and in melanocytes

The diagnostic value of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) measurement in the sera of gastric cancer patients

Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with colorectal cancer

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