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Tissue difference of protein sialylation in transgenic mice harboring Galβ1,3GalNAc α2,3‐sialyltranseferase II (ST3Gal II) transgenes

During our research on sialic acid metabolism, we found dilated cardiomyopathy‐like symptoms with 100 % incidence in homozygous mice of a transgenic mouse line harboring the Galβ1,3GalNAc α2,3‐sialyltransferase type II (ST3Gal II) transgenes. In this study, we performed lectin blot analysis to compare glycoprotein sialylation in heart and skeletal muscle tissues between wild and transgenic (Tg) mice. Proteins extracted from heart and femoral muscle tissues were separated by SDS‐electrophoresis using BLOT‐EX Precast Gels (Elchrom Scientific). After transfer to PVDF membranes, we analyzed protein reactivity to peanut agglutinin (PNA, HONEN), which binds to ST3Gal II substrates, but not to sialylated products. While a protein (~100 kDa) lost PNA‐reactivity in Tg hearts, some proteins (e.g., ~60 kDa and ~30 kDa) gained PNA‐reactivity in Tg femoral muscles. Thus, ST3Gal II transgenes increased sialylated protein species in hearts, but decreased protein species in femoral muscles. These results suggest that the sialylation system in hearts is different from that in skeletal muscles and that this difference might be related to the etiology of the symptoms in Tg mice.