Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins

Calf thyroid slices incubated with [U-14C]glucose synthesized protein-bound Glc3Man9GlcNAc2, Glc2-Man9GlcNac2, Glc1Man9GlcNAc2, Glc1Man8GlcNac2, and Glc1Man7GlcNAc2. Although label in the glucose residues of the last three compounds could be detected within 5 min of incubation, appearance of radioac...

Descripción completa

Guardado en:

Detalles Bibliográficos
Publicado:	1983
Materias:	glycoprotein radioisotope animal cell cattle endocrine system microsome nonhuman thyroid gland Animal Carbohydrate Sequence Carbon Radioisotopes Cattle Glucose Glycoproteins In Vitro Oligosaccharides Structure-Activity Relationship Support, Non-U.S. Gov't Thyroid Gland
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v258_n13_p8260_Parodi http://hdl.handle.net/20.500.12110/paper_00219258_v258_n13_p8260_Parodi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00219258_v258_n13_p8260_Parodi
record_format	dspace
spelling	paper:paper_00219258_v258_n13_p8260_Parodi2023-06-08T14:43:15Z Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins glycoprotein radioisotope animal cell cattle endocrine system microsome nonhuman thyroid gland Animal Carbohydrate Sequence Carbon Radioisotopes Cattle Glucose Glycoproteins In Vitro Oligosaccharides Structure-Activity Relationship Support, Non-U.S. Gov't Thyroid Gland Calf thyroid slices incubated with [U-14C]glucose synthesized protein-bound Glc3Man9GlcNAc2, Glc2-Man9GlcNac2, Glc1Man9GlcNAc2, Glc1Man8GlcNac2, and Glc1Man7GlcNAc2. Although label in the glucose residues of the last three compounds could be detected within 5 min of incubation, appearance of radioactivity in the mannose residues of the α-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 five protein-bound oligosaccharides mentioned above. Although addition to 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. These results indicate that Glc1Man8GlcNAc2 and Glc1Man7GlcNAc2 were formed by glucosylation of the unglucosylated species and not be demannosylation of Glc1Man9GlcNAc2 and that probably part of the latter compound was formed in the same way. 1983 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v258_n13_p8260_Parodi http://hdl.handle.net/20.500.12110/paper_00219258_v258_n13_p8260_Parodi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	glycoprotein radioisotope animal cell cattle endocrine system microsome nonhuman thyroid gland Animal Carbohydrate Sequence Carbon Radioisotopes Cattle Glucose Glycoproteins In Vitro Oligosaccharides Structure-Activity Relationship Support, Non-U.S. Gov't Thyroid Gland
spellingShingle	glycoprotein radioisotope animal cell cattle endocrine system microsome nonhuman thyroid gland Animal Carbohydrate Sequence Carbon Radioisotopes Cattle Glucose Glycoproteins In Vitro Oligosaccharides Structure-Activity Relationship Support, Non-U.S. Gov't Thyroid Gland Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
topic_facet	glycoprotein radioisotope animal cell cattle endocrine system microsome nonhuman thyroid gland Animal Carbohydrate Sequence Carbon Radioisotopes Cattle Glucose Glycoproteins In Vitro Oligosaccharides Structure-Activity Relationship Support, Non-U.S. Gov't Thyroid Gland
description	Calf thyroid slices incubated with [U-14C]glucose synthesized protein-bound Glc3Man9GlcNAc2, Glc2-Man9GlcNac2, Glc1Man9GlcNAc2, Glc1Man8GlcNac2, and Glc1Man7GlcNAc2. Although label in the glucose residues of the last three compounds could be detected within 5 min of incubation, appearance of radioactivity in the mannose residues of the α-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 five protein-bound oligosaccharides mentioned above. Although addition to 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. These results indicate that Glc1Man8GlcNAc2 and Glc1Man7GlcNAc2 were formed by glucosylation of the unglucosylated species and not be demannosylation of Glc1Man9GlcNAc2 and that probably part of the latter compound was formed in the same way.
title	Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
title_short	Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
title_full	Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
title_fullStr	Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
title_full_unstemmed	Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
title_sort	transient glucosylation of protein-bound man9glcnac2, man8glcnac2, and man7glcnac2 in calf thyroid cells. a possible recognition signal in the processing of glycoproteins
publishDate	1983
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v258_n13_p8260_Parodi http://hdl.handle.net/20.500.12110/paper_00219258_v258_n13_p8260_Parodi
_version_	1768543880221818880

Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins

Ejemplares similares