With new advanced techniques developed by the Copenhagen Center for Glycomics at the University of Copenhagen, it is possible to study cells in greater detail than ever before. The findings described below have just been published in the June 20, 2014 issue of the Journal of Biological Chemistry and may, in the long term, improve the treatment of high cholesterol. Researchers from the Copenhagen Center for Glycomics at the University of Copenhagen have studied an important receptor protein called LDLR (low-density lipoprotein receptor) (see image) using new, ground-breaking techniques. The protein plays an important role in the absorption of the so-called “bad” cholesterol, LDL (low-density lipoprotein). The key to major discoveries within the fields of health and diseases is not just hidden in the human DNA code. The proteins encoded by the genes also play an important role, not least the attached sugar chains which give the proteins an identity and handle important functions in the human organism. Here, the researchers have studied how LDLR is decorated with sugar molecules, so-called glycosylation modifications. "We have not previously had a simple method for studying where glycosylation modifications are located on proteins in the body, because the sugars are very complicated and appear in different combinations. By removing the Cosmc protein, which is necessary for extending the sugar modifications, we have created cells with simplified glycosylations, which we call SimpleCells. The technique has enabled us to see 20 times as many sugar modifications on our proteins as were previously known," says Nis Borbye Pedersen, Ph.D., formerly postdoc at the Copenhagen Center for Glycomics, now postdoc in the Department of Biology, University of Copenhagen.
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