| First Author | Chen X | Year | 2022 |
| Journal | J Physiol Biochem | Volume | 78 |
| Issue | 1 | Pages | 73-83 |
| PubMed ID | 34462883 | Mgi Jnum | J:341294 |
| Mgi Id | MGI:7431340 | Doi | 10.1007/s13105-021-00840-x |
| Citation | Chen X, et al. (2022) Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression. J Physiol Biochem 78(1):73-83 |
| abstractText | Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, alpha2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1(-/-) mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, alpha2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1(-/-) mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that alpha2,6-sialyltransferase gene expression decreased significantly in Cav-1(-/-) mouse organ tissues, but alpha2,3- and alpha2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the beta-galactoside alpha2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1(-/-) mice organ tissues, which was consistent with the alpha2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1(-/-) mice. These results provide for the first time the N-glycans profile of Cav-1(-/-) mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. |
