Impairment of histone H1 DNA binding by adduct formation with acetaldehyde

Niemelä, Onni; Mannermaa, Riitta-Maaria; Oikarinen, Jouko

doi:10.1016/0024-3205(90)90155-k

Cited by 18 publications

(8 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AcH has been reported to be bound to substances in vivo to form adducts (Stevens et al, 1981;Niemela et al, 1990;Lumeng et al, 1982;Brenner and Chojkier, 1987). When adduct antibody measurements were determined by the ELISA method using rabbit LDL, which we have established (Nagata et al, 1998), anti-LDL-adduct antibody levels in the alcoholic hepatitis group were shown to be significantly higher than those in the healthy group and other liver injury groups.…”

Section: Discussionmentioning

confidence: 99%

Relationship Between Serum Levels of Anti‐Low‐Density Lipoprotein‐Acetaldehyde‐Adduct Antibody and Aldehyde Dehydrogenase 2 Heterozygotes in Patients With Alcoholic Liver Injury

Nagata

Watanabe

Tsuda

et al. 1999

Alcoholism Clin & Exp Res

View full text Add to dashboard Cite

We prepared low-density lipoprotein (LDL)-acetaldehyde-adduct (hereafter abbreviated as LDL-adduct) and anti-LDL-adduct antibody by using Watanabe hyperlipidemic rabbits, and determined values of serum anti-LDL-adduct antibody levels by the ELISA method in healthy adults and patients with alcoholic liver injury. In the nondrinking group in healthy adults, values of anti-LDL-adduct antibody levels were 25 +/- 13 microg/ml, and there was no significant difference between moderate drinkers without diseases and the nondrinking group in healthy adults. Values of anti-LDL-adduct antibody in alcoholic disease groups, 17 +/- 9 microg/ml for the patients with the fatty liver group, 21 +/- 14 microg/ml for the hepatic fibrosis group, 70 +/- 21 microg/ml for the alcoholic hepatitis group, 41 +/- 50 microg/ml for the alcoholic cirrhosis group, and 19 +/- 18 microg/ml for the alcoholic pancreatitis group. Examinations of aldehyde dehydrogenase 2 (ALDH2) genetic variations by the polymerase chain reaction-single-strand conformation polymorphism (PCR-SSCP) method in the healthy group and the liver injury group revealed a tendency for patients with ALDH2(1)/2(2) in the liver injury group to have relatively mild liver lesions. When comparing anti-LDL-adduct antibody levels between ALDH2 genetic variations, those for the patients with ALDH2(1)/2(2) (36 +/- 40 microg/ml) were significantly higher than those for patients with ALDH2(1)/2(2) (11 +/- 5 microg/ml). Results of the present study suggest that genetic variation may influence the progression of liver injury.

show abstract

Section: Discussionmentioning

confidence: 99%

Relationship Between Serum Levels of Anti‐Low‐Density Lipoprotein‐Acetaldehyde‐Adduct Antibody and Aldehyde Dehydrogenase 2 Heterozygotes in Patients With Alcoholic Liver Injury

Nagata

Watanabe

Tsuda

et al. 1999

Alcoholism Clin & Exp Res

View full text Add to dashboard Cite

show abstract

“…DNA malfunction represented by AcHprovoked collagen gene expression has been observed in human fibroblasts (Brenner and Chojkier, 1987) and in hepatic stellate cells (Casini et al, 1991;Chen and Davis, 2000;Pares et al, 1994;Tsukamoto, 1993; see also review by Greenwel, 1999). AcH also has been observed to bind with histone H1, which may be a regulator of the ␣2(I) collagen promoter (Niemelä et al, 1990). Curiously, AcH has been found to suppress the activation of the transcription factor nuclear factor (NF)-B in isolated lipopolysaccharide-stimulated Kupffer cells (Jokelainen et al, 1998) and to promote the activation in HepG2 cells (Roman et al, 2000).…”

Section: Chronic Pathological Effects Of Alcohol Drinkingmentioning

confidence: 93%

The Role of Acetaldehyde in the Actions of Alcohol (Update 2000)

Eriksson

2001

Alcoholism Clin & Exp Res

226

116

View full text Add to dashboard Cite

Background: Recent advances in the field of acetaldehyde (AcH) research have raised the need for a comprehensive review on the role of AcH in the actions of alcohol. This update is an attempt to summarize the available AcH research.Methods: The descriptive part of this article covers not only recent research but also the development of the field. Special emphasis is placed on mechanistic analyses, new hypotheses, and conclusions.Results: Elevated AcH during alcohol intoxication causes alcohol sensitivity, which involves vasodilation associated with increased skin temperature, subjective feelings of hotness and facial flushing, increased heart and respiration rate, lowered blood pressure, sensation of dry mouth or throat associated with bronchoconstriction and allergy reactions, nausea and headache, and also reinforcing reactions like euphoria. These effects seem to involve catecholamine, opiate peptide, prostaglandin, histamine, and/or kinin mechanisms. The contribution of AcH to the pathological consequences of chronic alcohol intake is well established for different forms of cancer in the digestive tract and the upper airways. AcH seems to play a role in the etiology of liver cirrhosis. AcH may have a role in other pathological developments, which include brain damage, cardiomyopathy, pancreatitis, and fetal alcohol syndrome. AcH creates both unpleasant aversive reactions that protect against excessive alcohol drinking and euphoric sensations that may reinforce alcohol drinking. The protective effect of AcH may be used in future treatments that involve gene therapy with or without liver transplantation.Conclusions: AcH plays a role in most of the actions of alcohol. The individual variability in these AcH-mediated actions will depend on the genetic polymorphism, not only for the alcohol and AcHmetabolizing enzymes but also for the target sites for AcH actions. The subtle balance between aversive and reinforcing, protecting and promoting factors will determine the overall behavioral and pathological developments.

show abstract

“…The nuclear extracts from myofibroblastlike cells previously exposed to 200 pmol/L acetaldehyde showed a marked increase in NF-I protein ( It appears that several proteins present in 3T3 cells, and in myofibroblastlike cells, are bound t o the NF-I oligo but are not shifted by the NF-I antibody used in the EMSA. The most likely reason for this finding is that NF-I represents a family of site-specific DNA-binding proteins,28 and that multiple forms of NF-I are found in various differentiated cell typesz9 These multiple species are generated by several mechanisms, including expression of distinct but related gene^,^"^^ as well as by differential splicing of the messenger RNAs of these genes.31 13 Furthermore, it is known that posttranslational modification events, including covalent modification by g~lycosylation"~ and pho~phorylation,~~ result in phenotypical differences in the mature polypeptides. The antibody used in these experiments was made against purified NF-I from HeLa cells,23 and isoforms present in the extract may not be recognized by this antibody.…”

Section: Ne P I C a Kdamentioning

confidence: 99%

Effects of acetaldehyde on nuclear protein binding to the nuclear factor I consensus sequence in the α2(I) collagen promoter

et al. 1995

View full text Add to dashboard Cite

Acetaldehyde has been shown to increase collagen production in cultured rat myofibroblastlike cells and to activate the mouse alpha 2(I) collagen promoter in transfected NIH 3T3 cells. Nuclear factor I (NF-I), a CCAAT binding transcription factor, is known to bind and activate the alpha 1(I) and alpha 2(I) collagen genes. Activation of the alpha 2(I) collagen promoter was not observed when the NF-I binding site of the promoter was deleted. In this study, we determined if acetaldehyde influences the binding of NF-I to the alpha 2(I) collagen promoter. Nuclear proteins extracted from NIH 3T3 cells, or myofibroblastlike cells, 36 hours after the addition of acetaldehyde (200 mumol/L) in serum-free media showed increased binding to the consensus sequence of the NF-I binding site by DNase I protection analysis and by electrophoretic mobility shift assay (EMSA) as compared with control nuclear extracts that were not exposed to acetaldehyde. Furthermore, nuclear proteins extracted from myofibroblastlike cells that had been previously exposed to acetaldehyde had a marked increase in NF-I protein, as shown by Western blot with NF-I antibodies. Antisera to NF-I resulted in a slow migrating DNA-protein-antibody complex (supershift) on EMSA. However, the NF-I antibody did not supershift all the DNA-protein complexes, and the supershift band was not increased with nuclear proteins from acetaldehyde-treated cells despite the increased binding of these nuclear protein preparations to the NF-I oligo. Therefore, nuclear proteins, in addition to NF-I, bind to the NF-I consensus sequence and may have their binding altered by acetaldehyde.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Impairment of histone H1 DNA binding by adduct formation with acetaldehyde

Cited by 18 publications

References 41 publications

Relationship Between Serum Levels of Anti‐Low‐Density Lipoprotein‐Acetaldehyde‐Adduct Antibody and Aldehyde Dehydrogenase 2 Heterozygotes in Patients With Alcoholic Liver Injury

Relationship Between Serum Levels of Anti‐Low‐Density Lipoprotein‐Acetaldehyde‐Adduct Antibody and Aldehyde Dehydrogenase 2 Heterozygotes in Patients With Alcoholic Liver Injury

The Role of Acetaldehyde in the Actions of Alcohol (Update 2000)

Effects of acetaldehyde on nuclear protein binding to the nuclear factor I consensus sequence in the α2(I) collagen promoter

Contact Info

Product

Resources

About