Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

AGN-PC-00IQPO 4-hydroxynon-2-enal

Synonyms: AG-A-00102, ACMC-20mo4b, CBiol_001811, CTK0J1367, CTK8E7677, ...

Doorn, J.A. et al., Schmidt, H. et al., Poli, G. et al., Xiao, B. et al., Doorn, J.A. et al., et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Bio1_001075

For quantitative evaluation of lipid peroxidation after perinatal hypoxia in umbilical arterial cord blood samples from 109 healthy, acidotic, and asphyctic neonates with a gestational age ranging from 26 to 41 wk, the levels of aldehydic lipid peroxidation products malondialdehyde (MDA) and 4-hydroxynon-2-enal (HNE) were measured [1].

High impact information on Bio1_001075

We find that histidine residues in proteins are major targets for reaction with the lipid peroxidation product 4-hydroxynon-2-enal (HNE) [2].
Furthermore, these findings reveal that CR catalyzes hydride transfer selectively to the ketone but also to the aldehyde and C=C of 4ONE, resulting in 4HNE, 1HNO, and 4ONA, respectively [3].
The time course for CR-mediated, NADPH-dependent 4ONE reduction and appearance of 4HNE and 1HNO was determined using HPLC, demonstrating 4HNE to be a major product and 1HNO and 4ONA to be minor products [3].
mGSTA4-4, a murine glutathione S-transferase (GST) exhibiting high activity in conjugating the lipid peroxidation product 4-hydroxynon-2-enal (4-HNE) with glutathione (GSH), was crystallized in complex with the GSH conjugate of 4-HNE (GS-Hna) [4].
Separation of the individual non-polar hydrazones in each zone by h.p.l.c. demonstrated that zone I prepared from microsomal fraction or hepatocytes incubated with CCl4 or ADP-iron contained mainly 4-hydroxyhex-2-enal, 4-hydroxynon-2-enal and 4-hydroxynona-2,5-dienal [5].

Associations of Bio1_001075 with other chemical compounds

Previous studies found the lipid peroxidation product 4-hydroxynon-2-enal (4HNE) to be both a substrate and an inhibitor of mitochondrial aldehyde dehydrogenase (ALDH2) [6].

References

Increased levels of lipid peroxidation products malondialdehyde and 4-hydroxynonenal after perinatal hypoxia. Schmidt, H., Grune, T., Müller, R., Siems, W.G., Wauer, R.R. Pediatr. Res. (1996) [Pubmed]
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Uchida, K., Stadtman, E.R. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal. Doorn, J.A., Maser, E., Blum, A., Claffey, D.J., Petersen, D.R. Biochemistry (2004) [Pubmed]
Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface. Xiao, B., Singh, S.P., Nanduri, B., Awasthi, Y.C., Zimniak, P., Ji, X. Biochemistry (1999) [Pubmed]
Separation and characterization of the aldehydic products of lipid peroxidation stimulated by carbon tetrachloride or ADP-iron in isolated rat hepatocytes and rat liver microsomal suspensions. Poli, G., Dianzani, M.U., Cheeseman, K.H., Slater, T.F., Lang, J., Esterbauer, H. Biochem. J. (1985) [Pubmed]
Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal. Doorn, J.A., Hurley, T.D., Petersen, D.R. Chem. Res. Toxicol. (2006) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.