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PubMed1982

Metabolic interactions of aldehyde dehydrogenase with therapeutic and toxic agents.

The specific physiological roles of ALDH have not been determined. In this overview, we have identified malondialdehyde as one potential endogenous toxic aldehyde that is oxidized by ALDH. Undoubtedly, there are other cytotoxic aldehydes which occur in several different tissues that are detoxified by this same system of enzymes. Intuitively, the role of aldehyde dehydrogenases in the detoxification of xenobiotic aldehydes should also receive additional consideration and attention. An interesting feature of specific studies described in this overview is that a single aldehydic substrate, like malondialdehyde, may be a substrate for one ALDH isozyme and a potent inhibitor of ALDH present in another cellular compartment. Assuming that the ALDH susceptible to this inhibition performs other important physiological or biochemical functions, a potentiating effect would occur. Thus, the efficient metabolism of potentially cytotoxic aldehydes may be a protective mechanism against a number of different organ system pathologies. Another striking feature of ALDH is its sensitivity to in vitro and in vivo inhibition by a number of chemically and pharmacologically diverse agents. This characteristic suggests that ALDH may be a target enzyme for inhibition by several therapeutically important drugs or their metabolites. As a result, the perturbation of ALDH by specific therapeutic agents suggests a potential role of this enzyme in a number of different drug-induced toxicities.

Alcohol Oxidoreductases↗
PubMed1978

Resolution of the initial phase controversy in the thiamine-polyphenol reaction.

The kinetics of interactions between thiamine and seven polyphenols were followed by two types of thiochrome assays. The assays on the reaction mixture showed the extremely rapid initial phase whereas those on the eluate of the mixture previously treated by the Decalso column did not. The former assay methods also produced higher estimates of thiamine modification than the latter over the period of 3 hours of reaction. Arguments are given to show the probable non-existence of the observed extremely rapid initial phase. Reinterpretation of some past results are also presented.

Caffeic Acids↗
PubMed1976

Electrophoretic pattern of red blood cell catechol-o-methyltransferase in schizophrenia and manic-depressive illness.

Human red blood cell (RBC) catechol-O-methyltransferase (COMT) was analyzed by polyacrylamide gel electrophoresis (PAGE). One major enzyme band (B) is observed after electrophoresis. In addition, a minor band (A) of COMT activity comprising no more than 25% of the total activity, is also detectable. The rate of migration during electrophoresis of both bands of RBC COMT was the same in manic depressive, schizophrenic, and normal individuals. These results did not reveal genetic variations in the COMT molecule among these three groups. Furthermore, when total RBC COMT was measured there were no statistically significant differences between schizophrenic, manic-depressive, and control individuals.

Bipolar Disorder↗