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Chemical Compound Review:

GS-HNE (2S)-2-amino-4-[[(1S)-1...

Synonyms: AC1NUTSY, CHEMBL2074757, CHEBI:32711

Sharma, R. et al., Enoiu, M. et al., Yang, Y. et al., Cheng, J.Z. et al., Sharma, R. et al., et al.

Ramana, Reddy, Tammali, Srivastava,

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Disease relevance of GS-HNE

Cells exposed to mild oxidative stress show a rapid and transient induction of RLIP76 resulting in an increased efflux of GS-HNE and acquire resistance to oxidative stress mediated toxicity and apoptosis [1].

High impact information on GS-HNE

The protective effect of stress pre-conditioning against apoptosis was abrogated by coating the cells with anti-RLIP76 IgG, which inhibited the efflux of GS-HNE from cells, indicating that the cells acquired resistance to apoptosis by metabolizing and excluding 4-HNE at a higher rate [2].
Furthermore, inhibition of AR prevents cell death caused by HNE and GS-HNE, but not GS-DHN [3].
Anti-RLIP76 IgG inhibited approximately 65% of the transport of GS-HNE and DNP-SG, indicating that most of the transport was mediated by RLIP76 [4].
The kinetics of adenosine triphosphate (ATP)-dependent uptake of GS-HNE and dinitrophenyl S-glutathione (DNP-SG) by these IOVs and inhibition of GS-HNE uptake by anti-RLIP76 IgG was studied [4].
RESULTS: The results showed the presence of RLIP76 in plasma membranes of HLE B-3 cells and that it mediated ATP-dependent transport of GS-HNE as well as of DNP-SG [4].

Biological context of GS-HNE

These studies demonstrate that RLIP76 mediates active transport of GS-HNE, and are consistent with our previous work showing that RLIP76-mediated efflux of GS-HNE regulates the intracellular concentration of 4-HNE and thereby affects 4-HNE mediated signaling [5].

Anatomical context of GS-HNE

Furthermore, the GGT-dependent metabolism of GS-HNE in the V79 GGT cell line was associated with a considerable increase of cytotoxicity as compared to a control cell line which does not express GGT (V79 Cl) [6].

Associations of GS-HNE with other chemical compounds

METHODS: HLE B-3 cells were treated with [(3)H] 4-HNE and efflux of its GSH conjugate, [(3)H] GS-HNE, into the medium was quantitated and characterized by HPLC and mass spectrometry [4].

Gene context of GS-HNE

Using mass spectrometry analysis we identified for the first time cysteinylglycine-HNE (CysGly-HNE) as the GGT metabolite of GS-HNE [6].
The intracellular concentrations of 4-HNE are regulated through a coordinated action of GSTs (GSTA4-4 and hGST5.8) which conjugate 4-HNE to GSH to form the conjugate (GS-HNE) and the transporter 76 kDa Ral-binding GTPase activating protein (RLIP76), which catalyze ATP-dependent transport of GS-HNE [7].

References

Transport functions and physiological significance of 76 kDa Ral-binding GTPase activating protein (RLIP76). Awasthi, S., Sharma, R., Yang, Y., Singhal, S.S., Pikula, S., Bandorowicz-Pikula, J., Singh, S.V., Zimniak, P., Awasthi, Y.C. Acta Biochim. Pol. (2002) [Pubmed]
Accelerated metabolism and exclusion of 4-hydroxynonenal through induction of RLIP76 and hGST5.8 is an early adaptive response of cells to heat and oxidative stress. Cheng, J.Z., Sharma, R., Yang, Y., Singhal, S.S., Sharma, A., Saini, M.K., Singh, S.V., Zimniak, P., Awasthi, S., Awasthi, Y.C. J. Biol. Chem. (2001) [Pubmed]
Aldose reductase mediates endotoxin-induced production of nitric oxide and cytotoxicity in murine macrophages. Ramana, K.V., Reddy, A.B., Tammali, R., Srivastava, S.K. Free Radic. Biol. Med. (2007) [Pubmed]
Mechanisms and physiological significance of the transport of the glutathione conjugate of 4-hydroxynonenal in human lens epithelial cells. Sharma, R., Yang, Y., Sharma, A., Dwivedi, S., Popov, V.L., Boor, P.J., Singhal, S.S., Awasthi, S., Awasthi, Y.C. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
Functional reconstitution of Ral-binding GTPase activating protein, RLIP76, in proteoliposomes catalyzing ATP-dependent transport of glutathione conjugate of 4-hydroxynonenal. Sharma, R., Sharma, A., Yang, Y., Awasthi, S., Singhal, S.S., Zimniak, P., Awasthi, Y.C. Acta Biochim. Pol. (2002) [Pubmed]
gamma-Glutamyltranspeptidase-dependent metabolism of 4-hydroxynonenal-glutathione conjugate. Enoiu, M., Herber, R., Wennig, R., Marson, C., Bodaud, H., Leroy, P., Mitrea, N., Siest, G., Wellman, M. Arch. Biochem. Biophys. (2002) [Pubmed]
Lipid peroxidation and cell cycle signaling: 4-hydroxynonenal, a key molecule in stress mediated signaling. Yang, Y., Sharma, R., Sharma, A., Awasthi, S., Awasthi, Y.C. Acta Biochim. Pol. (2003) [Pubmed]

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