Title : Investigating the Expression of Glycosyltransferase Genes and Glycosylation
Abstract :
- An alternate method for understanding glycosylation is to investigate the Golgi apparatus glycosyltransferases responsible for glycosylating lubricin
- Because the ISOGlyP results suggested less common transferases were necessary for lubricin glycosylation, the expression of ppGalNAc Ts from human primary FLSs isolated from RA and OA patients was investigated
- These types of cell lines are known to produce lubricin ( 1 )
- The relative quantifications of all transcripts were normalized against β-actin expression
- The average (n = 4, except for GALNT8 , where n = 3) expression of the GALNT genes is arranged in descending order of expression in Fig. 4D
- High mRNA expression was observed for GALNT1 , -2, -5, and 15, and lower expression was noted for the GALNT8 , -10, -12, and 16 genes
- The high expression of GALNT1 and -2 was in agreement with the suggestion that these two genes are ubiquitously expressed
- In contrast, GALNT5 and GALNT15 have been shown to display restricted expression profiles, suggesting these isoforms serve unique functions in the tissue where they are expressed (2 1 )
- The high expression of GALNT5 in FLSs indicated a potential role of this gene, and its relevance is increasing, as the expression of this gene has also been shown in chondrocytes (neXtProt)
- The GALNT5 gene was also able to correctly predict 54% of the sites identified via MS (Fig. 4D), which also indicates potential involvement of this gene in lubricin glycosylation
- The data showed that the highest expression was of the GALNT15 gene in the FLS cultures
- The specificity of this enzyme toward mucin-type domains is not currently understood (4 1 ), making its further investigation essential, especially as the gene has been shown to be one of the most expressed genes in chondrocytes and bone (2 1 , 42)
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