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Aldehyde Dehydrogenase

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Regina Pietruszko – One of the best experts on this subject based on the ideXlab platform.

Ming-kai Chern – One of the best experts on this subject based on the ideXlab platform.

  • Betaine Aldehyde Dehydrogenase from rat liver mitochondrial matrix.
    Chemico-Biological Interactions, 2001
    Co-Authors: Regina Pietruszko, Ming-kai Chern
    Abstract:

    An NAD-linked Aldehyde Dehydrogenase which in addition to aliphatic and aromatic Aldehydes, metabolizes aminoAldehydes and betaine Aldehyde, has been purified to homogeneity from male Sprague-Dawley rat liver mitochondria. The properties of the rat mitochondrial enzyme are similar to those of a rat liver cytoplasmic betaine Aldehyde dehydrognase and the human cytoplasmic E3 isozyme. The primary structure. of four tryptic peptides were also similar; only one difference in primary structure was observed. The close similarity of properties of the cytoplasmic with the mitochondrial form suggest that the cytoplasmic and mitochondrial betaine Aldehyde Dehydrogenase may be coded for by the same nuclear gene. Investigation of the mitochondrial form by isoelectric focusing resulted in visualization of multiple forms, different from those seen in the cytoplasm suggesting that the enzyme may be processed in the mitochondria.

  • Evidence for mitochondrial localization of betaine Aldehyde Dehydrogenase in rat liver: purification, characterization, and comparison with human cytoplasmic E3 isozyme.
    Biochemistry and cell biology = Biochimie et biologie cellulaire, 1999
    Co-Authors: Ming-kai Chern, Regina Pietruszko
    Abstract:

    Betaine Aldehyde Dehydrogenase has been purified to homogeneity from rat liver mitochondria. The properties of betaine Aldehyde Dehydrogenase were similar to those of human cytoplasmic E3 isozyme in substrate specificity and kinetic constants for substrates. The primary structure of four tryptic peptides was also similar; only two substitutions, at most, per peptide were observed. Thus, betaine Aldehyde Dehydrogenase is not a specific enzyme, as formerly believed; activity with betaine Aldehyde is a property of Aldehyde Dehydrogenase (EC 1.2.1.3), which has broad substrate specificity. Up to the present time the enzyme was thought to be cytoplasmic in mammals. This report establishes, for the first time, mitochondrial subcellular localization for Aldehyde Dehydrogenase, which dehydrogenates betaine Aldehyde, and its colocalization with choline Dehydrogenase. Betaine Aldehyde dehydrogenation is an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mam…

  • Human Aldehyde Dehydrogenase E3 isozyme is a betaine Aldehyde Dehydrogenase.
    Biochemical and biophysical research communications, 1995
    Co-Authors: Ming-kai Chern, Regina Pietruszko
    Abstract:

    The E3 isozyme of human Aldehyde Dehydrogenase (EC 1.2.1.3), with broad substrate specificity, which also catalyzes dehydrogenation of 4-aminobutyrAldehyde, was purified and sequenced recently (1,3). It has been shown during this investigation to have betaine Aldehyde Dehydrogenase activity. Betaine Aldehyde and 4-aminobutyrAldehyde activities copurified on six chromatographic columns. Molecular properties of the homogeneous product were identical with those of E3 isozyme. Activity with betaine Aldehyde was considerably higher than that with 4-aminobutyrAldehyde, the best known substrate. Thus, human E3 isozyme and betaine Aldehyde Dehydrogenase (EC 1.2.1.8) are the same enzyme.

Hans Jörnvall – One of the best experts on this subject based on the ideXlab platform.

Christine Beedham – One of the best experts on this subject based on the ideXlab platform.

D. Sasse – One of the best experts on this subject based on the ideXlab platform.

  • Spatial distribution of human liver Aldehyde Dehydrogenase isoenzymes.
    Histochemistry and cell biology, 1999
    Co-Authors: I. P. Maly, Valérie Crotet, D. Sasse
    Abstract:

    To elucidate the pattern of lesions in the liver pareparenchyma after ethanol ingestion, the quantitative distribution profiles of both the cytosolic and the mitochondrial Aldehyde Dehydrogenase isoenzyme activities were determined by the use of ultrathin-layer electrophoresis. It was found that in human liver pareparenchyma, both isoforms of Aldehyde Dehydrogenase are almost homogeneously represented in the liver acinus. These quantitative data are supported by the results of an improved histochemical technique. Moreover, sex differences were not detected either in activity or in the distribution pattern. Consequently, it can be assumed that it is not the activity of total Aldehyde Dehydrogenase or its isoforms which is responsible for the higher susceptibility of the perivenous zone to alcohol-dependent damage.

  • The intramucosal distribution of gastric alcohol Dehydrogenase and Aldehyde Dehydrogenase activity in rats.
    Histochemistry, 1992
    Co-Authors: I. P. Maly, M. Arnold, K. Krieger, M. Zalewska, D. Sasse
    Abstract:

    Using qualitative and microquantitative histochemical techniques, alcohol Dehydrogenase and Aldehyde Dehydrogenase activity was studied in the gastric mucomucosa of male and female rats. Alcohol Dehydrogenase was demonstrated by staining reactions with maximum activity in surface and neck cells and with clearly weaker activity also in parietal cells. Aldehyde Dehydrogenase could be detected in surface and neck cells, and also to a comparable degree in the parietal cells. Quantitative analyses of microdissected samples yielded high values for alcohol Dehydrogenase activity exclusively in the superficial part of the gastric mucomucosa, whereas low-K m Aldehyde Dehydrogenase activity showed a decreasing gradient from the surface to the deeper parts of the mucosa. Sex differences could not be confirmed.