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

Abstract

The principal enzymes catalyzing the conversion of ethanol to acetate are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). The activities of these enzymes are elevated in the serum during the course of alcoholism or cirrhosis. In previous investigations we have found elevated levels of ADH, ALDH, and class I ADH activity in liver cancer cells. It can suggest that these changes may be reflected by enzyme activity in the serum. In this work, the activity of ADH isoenzymes, and ALDH in the sera of patients with liver cancer was measured. Serum samples were taken from 64 patients (28 drinkers, 36 nondrinkers), with liver cancer. 25 patients had primary and 39 metastatic liver tumors. Total ADH activity was measured by photometric method with p-nitrosodimethylaniline (NDMA) as a substrate and ALDH activity by the fluorimetric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I and II isoenzymes we employed the fluorimetric 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. A statistically significant increase of class I ADH isoenzymes was found in the sera of cancer patients. The median activity of this class isoenzyme in the total cancer group increased about 51% (2.94 mU/L) in the comparison to the control level (1.43 mU/L). The activity of the class I ADH isoenzyme was significantly higher in the sera of patients with metastatic tumors than with primary cancers. The activity of this class in the sera of drinkers and group of moderate drinkers was significantly higher in comparison to the control group and higher in the sera of heavy drinkers when compared with moderate drinking patients. The total ADH activity was significantly higher (44%) among patients with cancer than healthy ones. The activity of class I ADH isoenzymes was elevated only in the serum of patients with metastatic liver cancer. This increase of activity seems to be caused by the enzyme released from liver cancer cells and primary tumors originating in other organs.

Proteomic Analysis of Differentially Expressed Proteins in Peripheral Cholangiocarcinoma

“…Many of these proteins were involved in cellular metabolism while a number were cytoskeletal proteins. Several of these proteins have also been reported to be differentially expressed in either hepatocellular carcinoma or other tumor types, for example alcohol dehydrogenase and aldehyde dehydrogenase [12], carbamyl phosphate synthase [13], selenium binding protein 1 and DNA helicase RuvB-like protein 2 ( [14][15][16]). …”

Microarray data analysis reveals differentially expressed genes in prolactinoma

“…ALDH are a group of enzymes catalyzing the oxidation of acetaldehyde and transforming it into acetate [27]. Abnormal activity of ALDH is implicated in a variety of cancers such as lung, colorectal and breast cancer [28][29][30].This study indicated ALDH is involved in prolactinoma as well, and might be a possible biomarker for this disease. Besides, SNARE interactions in vesicular transport was "partially" enriched in protein complex 2, which was also associated with hormone secretion [31].…”

Human Aldehyde Dehydrogenase (ALDH) in Cirrhotic and Hepatocellular Carcinoma Patients Related to Hepatitis C Virus

“…and need to be detoxified, as reviewed by Marchitti et al [16] . In addition to their important function in aldehyde detoxification, ALDHs perform other functions including ester hydrolysis, serving as binding proteins for various molecules (e.g., androgen and cholesterol) and potentially function as antioxidants by NAD(P) H production, ultra violet light absorption and/or hydroxyl radical scavenging [16,20,21] . Alcohol dehydrogenase and Aldehyde dehydrogenase which are most abundant in the liver, are the main enzymes involved in ethanol and acetaldehyde metabolism.…”