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...
Guardado en:
| Autores principales: | , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00219258_v258_n13_p8260_Parodi |
| Aporte de: |
| id |
todo:paper_00219258_v258_n13_p8260_Parodi |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_00219258_v258_n13_p8260_Parodi2023-10-03T14:22:54Z Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins Parodi, A.J. Mendelzon, D.H. Lederkremer, G.Z. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Parodi, A.J. Mendelzon, D.H. Lederkremer, G.Z. 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. |
| format |
JOUR |
| author |
Parodi, A.J. Mendelzon, D.H. Lederkremer, G.Z. |
| author_facet |
Parodi, A.J. Mendelzon, D.H. Lederkremer, G.Z. |
| author_sort |
Parodi, A.J. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00219258_v258_n13_p8260_Parodi |
| work_keys_str_mv |
AT parodiaj transientglucosylationofproteinboundman9glcnac2man8glcnac2andman7glcnac2incalfthyroidcellsapossiblerecognitionsignalintheprocessingofglycoproteins AT mendelzondh transientglucosylationofproteinboundman9glcnac2man8glcnac2andman7glcnac2incalfthyroidcellsapossiblerecognitionsignalintheprocessingofglycoproteins AT lederkremergz transientglucosylationofproteinboundman9glcnac2man8glcnac2andman7glcnac2incalfthyroidcellsapossiblerecognitionsignalintheprocessingofglycoproteins |
| _version_ |
1807317331203850240 |