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

Abstract

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.

Alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase activity in the sera of patients with esophageal cancer

“…A lot of enzymes in cancer cells may change their activity. It is commonly accepted that changes of enzyme activity in the neoplastic tissue are reflected by increase of the corresponding enzyme activity in the serum [14,15]. In our last study, we found that alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase are present in esophageal cancer cells.…”

“…For example, in colorectal cancer the total activity of alcohol dehydrogenase and the class I of ADH (the principal class of ADH isoenzymes in the colon) were significantly higher than in healthy colon mucosa [9]. Therefore, the activity of class I alcohol dehydrogenase isoenzymes was significantly elevated in the serum of patients with colorectal cancer [15]. In pancreatic cancer, the activity of class III ADH is significantly higher in Table 3 The activity of ADH isoenzymes and ALDH in the serum of drinkers and non-drinkers with esophageal cancer cancer tissues and the activity of this class is significantly higher in the serum of patients with pancreatic cancer than in the healthy group [20,21].…”

Aldehyde Dehydrogenase Discriminates the CD133 Liver Cancer Stem Cell Populations

“…In particular, ALDH bright cells from human umbilical cord blood and peripheral blood leukemic stem cells have been shown to contain all the nonobese diabetic/SCID engrafting cells in CD34 + cells (18,19). In addition, recent research efforts have shown that ALDH is highly expressed in non -small-cell lung, colon, and pancreatic cancers (20)(21)(22), and that higher ALDH activity levels can be used to better identify the colon CSC population with EpCAM high CD44 + phenotype (6), as well as the glioblastoma (23), retinoblastoma (24), and breast (25) CSC populations. In view of these recent advances, it was both reasonable and logical to speculate that ALDH1A1 or the more general ALDH may possibly play an important role in the better characterization of CD133 + HCC CSCs.…”

The Diagnostic Value of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) Measurement in the Sera of Colorectal Cancer Patients

“…The total ADH activity has been elevated in the sera of patients with colorectal cancer. The increase of total ADH activity was positively correlated with class I ADH and seems to be caused by the release of this isoenzyme from cancer cells [5].…”