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."