Covalent Interactions of Acetaldehyde With the Actin/Microfilament System

Xu, Dongsheng; Jennett, Richard B.; Smith, Scott L.; Sorrell, Michael F.; Tuma, Dean J.

doi:10.1093/oxfordjournals.alcalc.a044914

Cited by 42 publications

(21 citation statements)

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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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“…Kupffer cells tures. [40][41][42][43][44] Data presented herein showed that BSA modified with high or low levels of acetaldehyde are taken up and are the most likely cells other than LECs that may be involved in this process, although others have shown that they degraded by the perfused liver. This action can be competed out with a 100-fold excess of f-Alb, suggesting that the scaven-have little or no scavenger receptors.…”

Section: Aid Hepa 0030mentioning

confidence: 99%

Long-term ethanol administration alters the degradation of acetaldehyde adducts by liver endothelial cells

Thiele¹

1996

Hepatology

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effects of ethanol on liver endothelial cells (LECs). However, Previous reports have shown that long-term ethanolRees et al. 1 have shown recently that the uptake and degradaadministration alters receptor-mediated endocytosis tion of formaldehyde-modified albumin (f-Alb) by the scaven-(RME) of a variety of macromolecules by liver endotheger receptor on LECs is decreased markedly by long-term lial cells (LEC). Acetaldehyde is the major metabolic ethanol consumption. product of ethanol metabolism and has been shown toResearch for the last several years has shown that LECs bind to proteins to form adducts. In this study, the level play an active role in the reticuloendothelial system of the of protein modification by acetaldehyde necessary for liver. Specifically, LECs are involved in clearance from blood the uptake and degradation of acetaldehyde-modified of a variety of substances, including connective tissue compoproteins by LEC was investigated. Bovine serum albunents and several types of modified proteins. 2 In fact, RME min (BSA) acetaldehyde adducts were prepared by incubation of albumin with acetaldehyde at 100 mmol/L for and degradation by LECs are the major mechanisms for 1 hour at 37ЊC, and 1 mmol/L or 0.2 mmol/L for 5 days clearance of circulating hyaluronic acid, denatured collagens, at 37ЊC. In situ liver perfusion in the presence of these the N-terminal propeptide of type III collagen PIIINP, lamiadducts resulted in the degradation of 107 { 10.02 mg, nin, mannosylated glycoproteins, acetylated low-density lipo-69.82 { 5 mg, and 2.5 { 0.42 mg of acetaldehyde-adducted protein (LDL), and f-Alb. Receptors for chemically modified albumin, respectively, during a 4-hour period. These val-proteins, such as acetylated LDL and f-Alb, have been collecues were decreased by 53%, 67%, and nearly 100%, re-tively referred to as scavenger receptors. There has been spectively, in livers from ethanol-fed rats. Additionally, some debate as to whether there is one receptor for acetylated modification of protein with 1 mmol/L of acetaldehyde LDL and f-Alb or whether there is one receptor for each. for different periods of time and/or pH altered the Although macrophages and LECs can clear f-Alb and aceamount of 14 C-acetaldehyde binding, but no signifi-tylated LDL, they are cleared predominantly from the circucant changes in degradation were observed. Finally, lation by LECs. 3,4 Horiuchi et al. have shown that, although an excess of formaldehyde-modified albumin totally acetylated LDL did inhibit binding of f-Alb to sinusoidal endoinhibited the degradation of acetaldehyde adducts, thelial cells, the converse did not occur. 5 Additionally, an suggesting that they use the same receptor. These antibody specific for the f-Alb receptor did not inhibit endocydata show that acetaldehyde-modified proteins may tosis of acetylated LDL. 6 Some investigators maintain that be taken up and degraded by the scavenger receptor there are different receptors for these modified proteins, 7,8 on LEC. This uptake and degradation are dependent ...

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“…913 by various reducing agents such as sodium borohydride, sodium cyanoborohydride, and ascorbate (7,10,22). In animal systems, it has been reported that acetaldehyde readily binds to blood proteins, including serum albumin (7) and hemoglobin (20), as well as to skeletal muscle actin (24). Likewise Mauch et al (12) reported alterations in the catalytic activity of ribonuclease following binding to acetaldehyde.…”

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confidence: 99%

Immunological Detection of Acetaldehyde-Protein Adducts in Ethanol-Treated Carrot Cells

Perata¹,

Vernieri²,

Armellini³

et al. 1992

Plant Physiol.

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Polyclonal antibodies able to recognize protein-acetaldehyde conjugates were produced and characterized. The antibodies react with sodium cyanoborohydride-reduced Schiff's bases between acetaldehyde and a protein, independently of the nature of the macromolecule binding the acetaldehyde moiety. Only conjugates between acetaldehyde or propionaldehyde and a protein are recognized; conjugates obtained with other aldehydes are not reactive. Results conceming the formation of acetaldehyde adducts with carrot (Daucus carota L.) proteins are presented as well as the presence of such conjugates in ethanoltreated carrot cell cultures, a system highly sensitive to the presence of ethanol in the culture medium.

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Covalent Interactions of Acetaldehyde With the Actin/Microfilament System

Cited by 42 publications

References 0 publications

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences

Long-term ethanol administration alters the degradation of acetaldehyde adducts by liver endothelial cells

Immunological Detection of Acetaldehyde-Protein Adducts in Ethanol-Treated Carrot Cells

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