Sandbox 181: Difference between revisions

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Heredity deficiency of GSH reductase is rare<ref name="Kamerbeek">PMID: 17185460 </ref>. A deficiency is most often due a genetic mutation and in two related case studies a deletion of the Asp385-Arg478 segment was found <ref name="Kamerbeek"/>. This shorted the protein to 43.8 kDA and once expressed, was likely degraded due to misfolding, leading to a deficiency of GSH reductase<ref name="Kamerbeek"/>. The symptoms and consequences in these genetically related cases were favism and cataracts<ref name="Kamerbeek"/>. The formation of cataracts in theses patients was likely due to UV-induced oxidative damage to the lens of the eye<ref name="Kamerbeek"/>.

~~Elevated~~ GSH ~~levels (ie~~. a ~~more reducing environment) stimulates cellular proliferation~~ <ref>~~PMID: 16978905~~ </~~ref~~>.

A second mutation in the GSH reductase gene truncated GSH reductase at Trp287 by changing the TGG codon for Trp287 into a premature TGA stop codon <ref name="Kamerbeek"/>. The folding-initiating helix 11 of residues 439 to 454 is then missing causing the improper folding and an inactive enzyme <ref name="Kamerbeek"/>. Additionally, Gly330 is exchanged for a GCG codon for alanine <ref name="Kamerbeek"/>. The exchange of glycine to alanine affects catalysis and stability of GSH reductase by disrupting the proper FAD binding necessitating the presence of higher concentrations of FAD to saturate the apoenzyme <ref name="Kamerbeek"/>.

Sandbox 181: Difference between revisions

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Revision as of 18:47, 26 March 2010 view source Josina Rhebergen (talk \| contribs) 62 edits No edit summary ← Older edit		Revision as of 18:58, 26 March 2010 view source Josina Rhebergen (talk \| contribs) 62 edits No edit summary Newer edit →
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	Heredity deficiency of GSH reductase is rare<ref name="Kamerbeek">PMID: 17185460 </ref>. A deficiency is most often due a genetic mutation and in two related case studies a deletion of the Asp385-Arg478 segment was found <ref name="Kamerbeek"/>. This shorted the protein to 43.8 kDA and once expressed, was likely degraded due to misfolding, leading to a deficiency of GSH reductase<ref name="Kamerbeek"/>. The symptoms and consequences in these genetically related cases were favism and cataracts<ref name="Kamerbeek"/>. The formation of cataracts in theses patients was likely due to UV-induced oxidative damage to the lens of the eye<ref name="Kamerbeek"/>.		Heredity deficiency of GSH reductase is rare<ref name="Kamerbeek">PMID: 17185460 </ref>. A deficiency is most often due a genetic mutation and in two related case studies a deletion of the Asp385-Arg478 segment was found <ref name="Kamerbeek"/>. This shorted the protein to 43.8 kDA and once expressed, was likely degraded due to misfolding, leading to a deficiency of GSH reductase<ref name="Kamerbeek"/>. The symptoms and consequences in these genetically related cases were favism and cataracts<ref name="Kamerbeek"/>. The formation of cataracts in theses patients was likely due to UV-induced oxidative damage to the lens of the eye<ref name="Kamerbeek"/>.

	~~Elevated~~ GSH ~~levels (ie~~. a ~~more reducing environment) stimulates cellular proliferation~~ <ref>~~PMID: 16978905~~ </~~ref~~>.		A second mutation in the GSH reductase gene truncated GSH reductase at Trp287 by changing the TGG codon for Trp287 into a premature TGA stop codon <ref name="Kamerbeek"/>. The folding-initiating helix 11 of residues 439 to 454 is then missing causing the improper folding and an inactive enzyme <ref name="Kamerbeek"/>. Additionally, Gly330 is exchanged for a GCG codon for alanine <ref name="Kamerbeek"/>. The exchange of glycine to alanine affects catalysis and stability of GSH reductase by disrupting the proper FAD binding necessitating the presence of higher concentrations of FAD to saturate the apoenzyme <ref name="Kamerbeek"/>.