[HTML][HTML] Genetically Altered Mice with Different Sialyltransferase Deficiencies Show Tissue-specific Alterations in Sialylation and Sialic Acid 9-O-Acetylation* 210
LT Martin, JD Marth, A Varki, NM Varki - Journal of Biological Chemistry, 2002 - ASBMB
Glycan chains on glycoconjugates traversing the Golgi apparatus are often terminated by
sialic acid residues, which can also be 9-O-acetylated. This process involves competition
between multiple Golgi enzymes. Expression levels of Golgi enzyme mRNAs do not always
correlate with enzyme activity, which in turn cannot accurately predict glycan sequences
found on cell surfaces. Here we examine the cell type-specific expression of terminal
glycans in tissues of normal mice in comparison with animals deficient in ST6Gal-I (transfers …
sialic acid residues, which can also be 9-O-acetylated. This process involves competition
between multiple Golgi enzymes. Expression levels of Golgi enzyme mRNAs do not always
correlate with enzyme activity, which in turn cannot accurately predict glycan sequences
found on cell surfaces. Here we examine the cell type-specific expression of terminal
glycans in tissues of normal mice in comparison with animals deficient in ST6Gal-I (transfers …