Mammalian Liver Alcohol Dehydrogenases

Pietruszko, Regina

doi:10.1007/978-1-4684-7529-6_1

Cited by 32 publications

(10 citation statements)

References 107 publications

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“…To get insights into the function of the cysteines of p12, OEVs were solubilized and incubated with a zinc-coated affinity matrix ( Figure 5A). We did not observe any bound p12 (lane 4) but alcohol dehydrogenase (ALDH) known to bind zinc (Pietruszko, 1975;bottom panel, lanes 4 and 7). In parallel, facilitating a zincreleasing assay zinc could be detected bound to ALDH (F), but not to p12 (E).…”

Section: The Cysteines Within the Loop Region Seem To Stabilize The Smentioning

confidence: 89%

Toc12, a Novel Subunit of the Intermembrane Space Preprotein Translocon of Chloroplasts

Becker¹,

Hritz

Vogel

et al. 2004

MBoC

109

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Translocation of proteins across membranes is essential for the biogenesis of each cell and is achieved by proteinaceous complexes. We analyzed the translocation complex of the intermembrane space from chloroplasts and identified a 12-kDa protein associated with the Toc machinery. Toc12 is an outer envelope protein exposing a soluble domain into the intermembrane space. Toc12 contains a J-domain and stimulates the ATPase activity of DnaK. The conformational stability and the ability to stimulate Hsp70 are dependent on a disulfide bridge within the loop region of the J-domain, suggesting a redox-regulated activation of the chaperone. Toc12 is associated with Toc64 and Tic22. Its J-domain recruits the Hsp70 of outer envelope membrane to the intermembrane space translocon and facilitates its interaction to the preprotein.

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Section: The Cysteines Within the Loop Region Seem To Stabilize The Smentioning

confidence: 89%

Toc12, a Novel Subunit of the Intermembrane Space Preprotein Translocon of Chloroplasts

Becker¹,

Hritz

Vogel

et al. 2004

MBoC

109

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“…1.1.1.1) is the most important enzyme in the oxidation of ethanol to acetaldehyde (18). In mammals, ADH activity has been found to be present principally in the liver, although small quantities have been detected in the small intestine, lung, kidney, stomach, and retina (32). It has been proposed that liver ADH accounts for 75-80% of the in vivo ethanol metabolism (16,20).…”

mentioning

confidence: 99%

“…It has been proposed that liver ADH accounts for 75-80% of the in vivo ethanol metabolism (16,20). However, although the amount of ADH in the liver is appreciable, its physiological role is uncertain (32).…”

mentioning

confidence: 99%

Ultracytochemical Study of Alcohol Dehydrogenase Activity in Normal Mouse Hepatic Cells

Watabiki

1979

Acta Histochem. Cytochem

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“…The enzymes that catalyze these two oxidations are alcohol dehydrogenase (ADH), located in the cytoplasm, catalase in the peroxisomes, the microsomal ethanol oxidizing system (MEOS) in the endoplasmic reticulum (Lieber, 1985), and aldehyde dehydrogenase (ALDH) which is located in the soluble and insoluble fractions of hepatocytes (Crow et al, 1974;Harada, 2001). Although ADH catalyzes the rate-limiting step in the ethanol metabolism (Plapp et al, 1984;Vidal et al, 1990), its physiological role is uncertain (Pietruszko, 1975). However, the serum activity of this enzyme is a specific reflexion of hepatocellular necrosis (Mezey et al, 1968;Skursk et al, 1979) because the highest ADH activities have been found in the liver (Skursk et al, 1979), and the reduction of ADH activity is proportional to the severity of liver disease (Pan et al, 1989;Vidal et al, 1989); that being so, the appearance of this enzyme in serum can indicate liver disease with comparatively good selectivity (Skursk et al, 1979).…”

Section: Introductionmentioning

confidence: 99%

Effects of high taurocholate load on activities of hepatic alcohol metabolizing enzymes

Kim

Shin²

2002

Exp Mol Med

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Membrane-associated cytotoxicity induced by hydrophobic bile salts is a major contributing factor leading to liver diseases. Administration of ursodeoxycholate reduces serum liver enzymes in chronic liver diseases but the nature of this effect is still unclear. Using alcohol metabolising enzymes as cellular markers, the hepatotoxic properties of hydrophobic bile salts and the putative hepatoprotective effect of ursodeoxycholate was examined. Two animal models of biliary retention, bile duct obstruction and choledochocaval fistula was used to investigate the effect of taurocholate on the hepatic alcohol metabolizing enzymes: cytosolic alcohol dehydrogenase, microsomal ethanol oxidizing system, catalase and aldehyde dehydrogenase before and after the infusion of taurocholic acid or tauroursodeoxycholic acid for two days period. Bile duct obstruction was found to be similar to or slightly exceeds choledochocaval fistula in the degree of retention. Following the taurocholic acid infusion, the serum alcohol dehydrogenase activity as well as microsomal ethanol oxidizing system and aldehyde dehydrogenase were greatly increased but the level of cytosolic alcohol dehydrogenase and catalase activities was found to be lower in either or both models in comparison with the control animals. However, the tauroursodeoxycholic acid infusion did not induce any significant changes in the levels of all the alcohol metabolizing enzyme activities in either or both models. These findings suggest that hydrophobic taurocholic acid (7α α α α) affects the plasmalemma to allow leakage of cytosolic alcohol dehydrogenase into the blood circulation, stimulates the biosynthesis of microsomal ethanol oxidizing system and aldehyde dehydrogenase, and suppresses the biosynthesis of alcohol dehydrogenase and catalase. But in contrast, the hydrophilic tauroursodeoxycholic acid (7β β β β) provided hepatoprotective effect.

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Mammalian Liver Alcohol Dehydrogenases

Cited by 32 publications

References 107 publications

Toc12, a Novel Subunit of the Intermembrane Space Preprotein Translocon of Chloroplasts

Toc12, a Novel Subunit of the Intermembrane Space Preprotein Translocon of Chloroplasts

Ultracytochemical Study of Alcohol Dehydrogenase Activity in Normal Mouse Hepatic Cells

Effects of high taurocholate load on activities of hepatic alcohol metabolizing enzymes

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