Glycosylation of the alpha and beta tubulin by sialyloligosaccharides.
To examine whether alpha and beta tubulin are glycoproteins, we used a pyridylamino labeling method and a monoclonal antibody, SG3-1, raised against NeuAcalpha2-3Gal structure. Alpha and beta tubulin from both pig brain and HeLa cells were positive for the SG3-1 antibody by immunoblot assay. Sialidase treatment reduced the reactivity of the SG3-1 antibody to alpha and beta tubulin molecules. N-linked oligosaccharide analysis also showed that alpha and beta tubulin are glycosylated. Moreover, immunofluorescence analysis showed that the filamentous structure recognized by the SG3-1 antibody was overlapped with microtubules, especially in the vicinity of the nucleus. These results indicate that alpha and beta tubulin are glycosylated with sialyloligosaccharides.
Hino
Mizuki
M
Department of Biological Science, Graduate School of Science, Hiroshima University, Hiroshima, Japan.
Kijima-Suda
Isao
I
Nagai
Yoshitaka
Y
Hosoya
Hiroshi
H
D000818:Animals; D000911:Antibodies, Monoclonal; D001921:Brain; D006031:Glycosylation; D006367:HeLa Cells; D006801:Humans; D015151:Immunoblotting; D009844:Oligosaccharides / Q000737:chemistry / Q000494:pharmacology*; D013552:Swine; D014404:Tubulin / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D009844:Oligosaccharides; D014404:Tubulin; C016735:sialooligosaccharides