earticle

영어

Glycosylation, which is susceptible to the biochemical environments, is one of the most important post translational modifications in eukaryotic proteins. Moreover, glycans are involved in many important biochemical events. Especially, sialic acids which are expressed as outer terminal units on all vetebrate are play fundamental roles in cell-to-cell and cell-to-microenvionment interactions. N-acetylneuraminic acid (NeuAc) and N-acetylglycolylneuraminic acid (NeuGc) are predominant sialic acids on most mammalian cells. Unlike other mammalian except chicken, human cannot biosynthesize the NeuGc due to irreversible mutation on gene CMAH encoding CMP-N-acetylneuraminic acid hydroxylase that convert CMP-NeuAc to CMP-NeuGc. When the NeuGc is metabolically incorporated into human tissue from dietary sources (especially red meat), the anti-NeuGc antibodies which leads immune response will be produced and circulated through blood. The evidence showed that the such anti-NeuGc antibodies may cause systemic inflammation and finally can promote tumor progression. Therefore, quantitation of the non-human sialic acid NeuGc in food and therapeutic glycoproteins is of high importance. Here, we introduce analytical methods for rapid and highly sensitive identification and quantitation of NeuGc in food contents containing non-human glycan epitope using LC-MS/MS.