Acetaldehyde adducts with hemoglobin.

Stevens, Victor J.; Fantl, Wendy J.; Newman, Connie B.; Sims, Richard V.; Cerami, Anthony; Peterson, Charles M.

doi:10.1172/jci110043

Cited by 310 publications

(108 citation statements)

References 25 publications

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“…Many proteins can be modified by acetaldehyde, including tubulin, actin, calmodulin, hemoglobin, hepatic enzymes and plasma proteins [31,50,51,57,84,112]. In general, acetaldehyde is thought to form stable adducts with the e-amino group of lysine residues [93,95,97].…”

Section: Ethanol-induced Tubulin Modificationsmentioning

confidence: 99%

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

2009

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Alcoholic liver disease is a major biomedical health concern in the United States. Despite considerable research efforts aimed at understanding the progression of the disease, the specific mechanisms leading to alcohol-induced damage remain elusive. Numerous proteins are known to have alcohol-induced alterations in their dynamics. Defining these defects in protein trafficking is an active area of research. In general, two trafficking pathways are affected: transport of newly synthesized secretory or membrane glycoproteins from the Golgi to the basolateral membrane and clathrin-mediated endocytosis from the sinusoidal surface. Both impaired secretion and internalization require ethanol metabolism and are likely mediated by acetaldehyde. Although the mechanisms by which ethanol exposure impairs protein trafficking are not fully understood, recent work implicates alcohol-induced modifications on tubulin or components of the clathrin machinery as potential mediators. Furthermore, the physiological ramifications of impaired protein trafficking are not fully understood. In this review, we will list and discuss the proteins whose trafficking patterns are known to be impaired by ethanol exposure. We will then describe what is known about the possible mechanisms leading to impaired protein trafficking and how disrupted protein trafficking alters liver function and may explain clinical features of the alcoholic patient.

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Section: Ethanol-induced Tubulin Modificationsmentioning

confidence: 99%

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

2009

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“…29 Examples inold of bound native Apo A-I was observed for concentrations above 5 mg/100 mL, but no saturation was ob-clude hepatic proteins, hemoglobin, erythrocyte membrane proteins, and enzymes. 16,18,20,30 The relevance of served for acetaldehyde-modified Apo A-I in the range of concentrations tested.…”

Section: Binding Assay Of Apo A-i and Acetaldehyde-modified Apomentioning

confidence: 99%

“…Ethylation of the most thoroughly studied. [16][17][18][19][20][21] More recently, apoli-Apo A-I was performed in tightly capped microtubes. 22 Acetaldehyde was conjugated to Apo A-I using the procedure de-poproteins have also been shown to form an acetaldescribed by Palinski et al 24 Solid NaBH 3 CN (final concentrahyde adduct.…”

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confidence: 99%

Binding of apolipoprotein A-I and acetaldehyde-modified apolipoprotein A-I to liver extracellular matrix

et al. 1996

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Apolipoprotein A-I (Apo A-I), a protein producedApolipoprotein A-I (Apo A-I), a 28-kd protein, is synmainly by hepatocytes, is decreased in the sera of alco-thesized mainly by hepatocytes. It is the major protein holic patients with liver fibrosis and cirrhosis. To ex-of the high-density lipoproteins. These particles are inplain this decrease, we investigated possible interac-volved in the reverse transport of cholesterol, a process tions between liver extracellular matrix (ECM) and Apo that promotes cholesterol efflux from cells to the liver. 1 A-I. Using a solid-phase binding assay, we evaluated the Apo A-I is a marker of atheromatous disease, and its binding of Apo A-I to the different liver matrix compo-decrease in serum is correlated with a higher risk of The mechanisms of serum Apo A-I decrease in liver urable. Apo A-I bound also to ECM in vivo because Apo fibrosis are unknown, but it has been shown that serum A-I was detected by immunofluorescence on fibrous Apo A-I measurement alone 4 or in correlation with septa in liver biopsy specimens of alcoholic patients. Be-other biological data such as prothrombin time and gcause a negative correlation between Apo A-I and liver glutamyl transferase (PGA score) 5 can serve as a fibrosis is amplified in alcoholic patients, we investi-marker of liver fibrosis and cirrhosis in alcoholic pa- argument is that lipoproteins can be extracted from vessels only in association with constituents of the ECM. 8 The ECM is a multimolecular complex that forms a network between cells, and expansion of the ECM is Abbreviations: Apo A-I, apolipoprotein A-I; ECM, extracellular matrix; the hallmark of fibrosis. In the liver, the matrix is made SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis; FN, up of proteins, glycoconjugates, and carbohydrate polyfibronectin; C, collagen; Ig, immunoglobulin; BSA, bovine serum albumin; mers. 9 Because of its multiple components and their EDTA, ethylenediaminetetraacetic where they are stored. [13][14][15] Copyright ᭧ 1996 by the American Association for the Study of Liver Acetaldehyde, the first oxidative metabolite of ethaDiseases.

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“…This reaction forms malondialdehyde-deoxyguanosine adducts, which are found in pathologists who are occupationally exposed to formaldehyde (Bono et al , 2010). Moreover, AA has been demonstrated to form adducts in reactions involving a number of proteins, such as albumin (Donohue et al , 1983) and haemoglobin (Stevens et al , 1981), and also with DNA: the resulting DNA adduct in humans is a Schiff base N 2 -ethylidene-2'-deoxyguanosine (N 2 -ethylidene-dG) adduct (Vaca et al , 1995).…”

Section: Introductionmentioning

confidence: 99%

Immune response to acetaldehyde-human serum albumin adduct among healthy subjects related to alcohol intake

Romanazzi

Schilirò

Carraro

et al. 2013

Environmental Toxicology and Pharmacology

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Acetaldehyde adducts with hemoglobin.

Cited by 310 publications

References 25 publications

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

Binding of apolipoprotein A-I and acetaldehyde-modified apolipoprotein A-I to liver extracellular matrix

Immune response to acetaldehyde-human serum albumin adduct among healthy subjects related to alcohol intake

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