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Transient glucosylation of protein bound nona octa and hepta mannosyldiacetyl glucosamine in calf thyroid cells a possible recognition signal in the processing of glyco proteins


, : Transient glucosylation of protein bound nona octa and hepta mannosyldiacetyl glucosamine in calf thyroid cells a possible recognition signal in the processing of glyco proteins. Journal of Biological Chemistry 258(13): 8260-8265

Calf thyroid slices incubated with [U[uniformly labeled]-14C]glucose synthesized protein-bound Glc3Man9GlcNAc2, Glc2Man9GlcNAC2, Glc1Man9GlcNAc2, Glc1Man8GlcNAc2, and Glc1Man7GlcNAc2. Although label in the glucose residues of the last 3 compounds could be detected within 5 min of incubation, appearance of radioactivity in the mannose residues of the .alpha.-mannosidase-resistant cores of Glc1Man8GlcNAc2 and Glc1Man7GlcNAc2 took more than 30 and 60 min, respectively, to appear after label was detected in the same mannose residues of Glc1Man9GlcNAc2. The glucose residues were removed upon chasing the slices with unlabeled glucose. The last compound to disappear was Glc1Man9GlcNAc2. Calf thyroid microsomes incubated with UDP-[U-14C]Glc synthesized the 5 protein-bound oligosaccharides mentioned above. Although addition of GDP-Man to the incubation mixtures greatly diminished the formation of Glc3Man9GlcNAc2 bound either to dolichol-P-P or to protein, labeling of Glc1Man9GlcNAc2, Glc1Man8GlcNAc2, and Glc1Man7GlcNAc2 was not affected. Addition of kojibiose prevented deglucosylation of protein-bound Glc3Man9GlcNAc2 without affecting the formation of Glc1Man8GlcNAc2 and Glc1Man7GlcNAc2 and only partially diminishing that of Glc1Man9GlcNAc2. Glc1Man8GlcNAc2 and Glc1Man7GlcNAc2 apparently were formed by glucosylation of the unglucosylated species and not by demannosylation of Glc1Man9GlcNAc2 and probably part of the latter compound was formed in the same way.

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