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13 February 2013

Discovering the behaviour of cell surface proteins

A new paper advances scientific understanding of the structure and function of glycoproteins, in particular the number and positioning of sugars.



The researchers verified their observation of a correlation between the number of sugars on a glycoprotein and its function in five animal species — worms, flies, fish, mice and humans. This led to their realization that the correlation has been conserved through evolution.

To obtain the number of N-Glycans on proteins, the researchers used proteomics — a combination of mass spectrometry (MS) and high-performance liquid chromatography (HPLC). In less than an hour, high-throughput technique identifies the exact place where N-Glycans attach on hundreds of glycoproteins.



Sun says this deeper understanding of the correlation between sugars’ positioning on glycoproteins and the proteins’ functions will benefit medical researchers and the pharmaceutical industry.

“As membrane proteins, glycoproteins are biologically important. They mediate cells’ communication to their environment, thus governing a plethora of cellular processes and functions, including growth, development, immunity and aging. Understanding how membrane proteins adapt to better protect themselves will help us design better, less toxic drugs to treat diseases.”

The paper, N-glycoproteome of E14.Tg2a Mouse Embryonic Stem Cells, appears in PLoS ONE.

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