A pattern of protein modifications specific to the brain is driven by the tissue-specific regulation of multiple enzymes Figure 1: In the brain, epigenetic factors can increase expression of the enzyme GnT-IX to produce a specific glycosylation pattern (left), or block GnT-IX expression to prevent the same glycosylation process (right). © 2014 Yasuhiko Kizuka, RIKEN–Max Planck Joint Research Center for Systems Chemical Biology Many human proteins are modified by the attachment of short sugar chains called glycans. The patterns of attachment, or glycosylations, are known to be specific to organs, tissues and cell types, but the mechanisms regulating these patterns have been unclear. Naoyuki Taniguchi, Yasuhiko Kizuka and colleagues from the RIKEN–Max Planck Joint Research Center for Systems Chemical Biology have now clarified one such mechanism in the brain1. Glycosylation is mediated by glycosyltransferase enzymes. The researchers studied one of these enzymes called N-acetylglucosaminyltransferase-IX (GnT-IX), which is expressed only in the brain and is involved in demyelination—degradation of the insulation around neurons that helps them to conduct electrical signals. Understanding the regulation of GnT-IX expression could help in developing better knowledge of diseases such as multiple sclerosis. As Kizuka explains, a closer look at the process regulating GnT-IX expression could also
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