Reaction of acetaldehyde with human erythrocyte membrane proteins

Gaines, Katherine C.; Salhany, James M.; Tuma, Dean J.; Sorrell, Michael F.

doi:10.1016/0014-5793(77)80065-3

Cited by 125 publications

(26 citation statements)

References 24 publications

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“…Acetaldehyde has been shown to crosslink erythrocyte membrane proteins (24), to brown with albumin (25), and in this report to react with hemoglobin by adduct formation. At least as many adducts are recovered in the plasma proteins as in hemoglobin when whole blood is reacted with [14C]acetaldehyde (not shown).…”

Section: Resultssupporting

confidence: 55%

“…The accumulation of adducts would appear to explain the fact that alcoholics in this study had elevated minor hemoglobins but below normal levels of hemoglobin A,, by specific radioimmunoassay. Gel chromatography and electrophoresis revealed no evidence for cross-linked hemoglobin after reaction with 0.3 mM acetaldehyde but crosslinked hemoglobin has been reported at higher concentrations of acetaldehyde (24). As minor hemoglobin levels are being clinically employed as a means of diagnosing and monitoring diabetes mellitus, the alcohol consumption habits of patients should also be considered.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Acetaldehyde adducts with hemoglobin.

Stevens¹,

Fantl²,

Newman³

et al. 1981

J. Clin. Invest.

310

104

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Section: Resultssupporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Acetaldehyde adducts with hemoglobin.

Stevens¹,

Fantl²,

Newman³

et al. 1981

J. Clin. Invest.

310

104

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“…Alternatively, the aldehyde may crosslink the membrane in the sickled state in such a way as to preclude formation of biconcave disks. Crosslinking of proteins with monofunctional aldehydes has been observed previously (27) and, in fact, high concentrations of acetaldehyde have been shown to produce erythrocytes with stiffened membranes (28,29). However, the degree of cross-linking of HbS by glyceraldehyde (less than 3%) and the amount of cross-linking in the membrane would appear to be too small to account for the morphological changes in sickle erythrocytes as well as for the increase in the minimum gelling concentration of deoxyhemoglobin S. Further studies with aldehydes that inhibit sickling but do not lead to cross-linking may help resolve these questions on the mechanism of action of glyceraldehyde.…”

Section: Discussionmentioning

confidence: 59%

Effects of Glyceraldehyde on the Structural and Functional Properties of Sickle Erythrocytes

Nigen¹,

Manning²

1978

J. Clin. Invest.

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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%

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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Reaction of acetaldehyde with human erythrocyte membrane proteins

Cited by 125 publications

References 24 publications

Acetaldehyde adducts with hemoglobin.

Acetaldehyde adducts with hemoglobin.

Effects of Glyceraldehyde on the Structural and Functional Properties of Sickle Erythrocytes

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

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