Inhibiting formation of a branched sugar molecule

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Inhibiting formation of a branched sugar molecule

Postby MSUK » Fri Oct 04, 2013 7:52 am

Inhibiting formation of a branched sugar molecule could lead to new treatments for MS

Multiple sclerosis is a debilitating condition that involves the degeneration of myelin—the fatty tissue that insulates nerve fibers and helps them to conduct impulses. This process, called demyelination, can lead to deficits in sensation, movement and thought processes, depending on exactly which nerve fibers are affected. Replacing lost myelin is a promising approach for treating multiple sclerosis and related diseases, but the mechanisms underlying demyelination and remyelination remain poorly understood...... Read More -
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Re: Inhibiting formation of a branched sugar molecule

Postby Annesse » Fri Oct 04, 2013 10:14 am

I think this would be associated with a lack of DNase1.

Here is a quote from the information MSUK posted.

"Taniguchi and his colleagues genetically engineered a strain of mice carrying mutations in the gene encoding an enzyme called N-acetylglucosaminyltransferase-IX (GnT-IX), which catalyzes the branching of O-mannosyl glycan sugars on proteins in the brain. Using these mice, the researchers found that GnT-IX acts on a specific brain protein called receptor protein tyrosine phosphatase ? (RPTP?), which has previously been shown to play a critical role in demyelination."

In the following study the researchers concluded that N-acetylglucosaminyltransferase IX is regulated by histone modifications and that their report demonstrates a molecular mechanism at the "chromatin" level that underlies tissue-specific glycan expression.

J Biol Chem. 2011 Sep 9;286(36):31875-84. doi: 10.1074/jbc.M111.251173. Epub 2011 Jul 19.
Brain-specific expression of N-acetylglucosaminyltransferase IX (GnT-IX) is regulated by epigenetic histone modifications.
Kizuka Y, Kitazume S, Yoshida M, Taniguchi N.

"Here we investigated the expression mechanism of a brain-specific glycosyltransferase, GnT-IX (N-acetylglucosaminyltransferase IX, also designated as GnT-Vb), which synthesizes branched O-mannose glycan. Using an epigenetic approach, we revealed that the genomic region around the transcriptional start site of the GnT-IX gene was highly associated with active chromatin histone marks in a neural cell-specific manner, indicating that brain-specific GnT-IX expression is under control of an epigenetic "histone code"... This is the first report demonstrating a molecular mechanism at the chromatin level underlying tissue-specific glycan expression."

In the following study the researchers concluded that the relationship between DNase 1 and histone modifications is part of the complex regulatory process responsible for maintaining chromatin structure.

Nucleic Acids Res. 2011 Sep 1;39(17):7428-43. doi: 10.1093/nar/gkr443. Epub 2011 Jun 17.
Genome-wide analysis of the relationships between DNaseI HS, histone modifications and gene expression reveals distinct modes of chromatin domains.
Shu W, Chen H, Bo X, Wang S.

"Our findings uncovered a complex regulatory process involving by DNaseI HS sites and histone modifications, and suggest that these dynamic elements may be responsible for maintaining chromatin structure and integrity of the human genome."
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