Rabbit Anti-Human AASS Polyclonal Antibody

The presence or absence of acetyl groups in oligosaccharides greatly affects the biological activities of glycoproteins. Consequently, in studies on glycoproteins, sensitive and accurate methods are required for the analysis of acetylated amino sugars (AASs) are required. We report here our newly developed method for the determination of four AASs [N-acetyl-d-glucosamine (GlcNAc), N-acetyl-d-galactosamine (GalNAc), N-acetyl neuraminic acid (Neu5Ac), N-glycolyl neuraminic acid (Neu5Gc)]. This method is based on the optimization of the release of AASs from Potentilla anserina L. glycoprotein and involves modification of experimental design and the use of high-performance liquid chromatography coupled with UV detection and mass spectrometry identification. Using our optimized conditions of derivatization and separation, we successfully detected these four AAS derivatives with good precision and accuracy. This is the first report of determination of the four AASs simultaneously on the basis of its release study. The newly developed method exhibits a high potential for the analysis of AASs from various bio-samples and provides a sensitive method for further study of the relationship between AAS composition and their bioactivities in glycoprotein.

Amino acid catabolism is frequently executed in mitochondria; however, it is largely unknown how aberrant amino acid metabolism affects mitochondria. Here we report the requirement for mitochondrial saccharopine degradation in mitochondrial homeostasis and animal development. In Caenorhbditis elegans, mutations in the saccharopine dehydrogenase (SDH) domain of the bi-functional enzyme alpha-aminoadipic semialdehyde synthase AASS-1 greatly elevate the lysine catabolic intermediate saccharopine, which causes mitochondrial damage by disrupting mitochondrial dynamics, leading to reduced adult animal growth. In mice, failure of mitochondrial saccharopine oxidation causes lethal mitochondrial damage in the liver, leading to postnatal developmental retardation and death. Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans. Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. Our study provides mechanistic and therapeutic insights for understanding and treating hyperlysinemia II (saccharopinuria), an aminoacidopathy with severe developmental defects.