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Abstract:

An assay for UDP-Glc:glycoprotein glucosyltransferase was developed. Incubation of rat liver microsomes with UDP-[14C]Glc led to the formation of hot trichloroacetic acid insoluble material identified as protein-linked Glc1Man7-9GlcNAc2. Addition of 8 M urea-denatured thyroglobulin to the incubation mixtures stimulated up to 10-12-fold the formation of the same compounds but only in the presence of detergents. Native thyroglobulin was ineffective. Several experiments indicated that the stimulation was due to the transfer of glucose residues from UDP-Glc to high-mannose oligosaccharides in urea-denatured thyroglobulin and that this transfer reaction did not involve dolichol mono- or diphosphate derivatives as intermediates. The glycoprotein glucosylating activity was mainly located in the endoplasmic reticulum and could glucosylate glycopeptides derived from the digestion of thyroglobulin with an unspecific protease. Glucosylation of oligosaccharides in those glycopeptides occurred, however, at a rate at least 2 orders of magnitude slower than that of the same compounds in urea-denatured thyroglobulin. Tryptic digestion of urea-denatured thyroglobulin did not affect its glucosylation rate. The structure of Glc1Man9GlcNAc2 linked to urea-denatured thyroglobulin was identical with that of Glc1Man9GlcNAc2-P-P-dolichol. The assay of UDP-Glc:glycoprotein glucosyltransferase allowed detection of the activity in microsomal membranes in which endogenous acceptors appeared to be absent or almost absent, such as those derived from mung bean, Mucor rouxii, Crithidia fasciculata, and Trypanosoma cruzi cells. These results provide evidence for the transfer of glucose residues directly from UDP-Glc to high-mannose oligosaccharides in glycoproteins in the endoplasmic reticulum of mammalian, plant, fungal, and protozoan cells and indicate that the previously characterized glucosidase II probably is responsible for the processing of glucosylated glycoproteins. © 1989, American Chemical Society. All rights reserved.

Registro:

Documento: Artículo
Título:Glucosylation of Glycoproteins by Mammalian, Plant, Fungal, and Trypanosomatid Protozoa Microsomal Membranes
Autor:Trombetta, S.E.; Bosch, M.; Parodi, A.J.
Filiación:Instituto de Investigations Bioquímicas “Fundación Campomar”, IIB-FCEN-UBA, IIBBA-CONICET, Antonio Machado 151, 1405 Buenos Aires, Argentina
Palabras clave:glycoprotein; mannose; radioisotope; alpha glucosidase ab; animal cell; fungus; glycogen(starch) synthase; glycosylation; liver microsome; mammal; microsome membrane; nonhuman; plant; priority journal; protozoon; Acetylglucosaminidase; Animal; Crithidia; Glucose; Glucosyltransferases; Glycoproteins; Glycosylation; Male; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; Microsomes; Microsomes, Liver; Mucor; Peptide Hydrolases; Plants; Protein Denaturation; Rats; Saccharomyces cerevisiae; Streptomyces griseus; Subcellular Fractions; Support, Non-U.S. Gov't; Transferases; Trypanosoma cruzi
Año:1989
Volumen:28
Número:20
Página de inicio:8108
Página de fin:8116
DOI: http://dx.doi.org/10.1021/bi00446a022
Título revista:Biochemistry
Título revista abreviado:Biochemistry
ISSN:00062960
CAS:mannose, 31103-86-3, 3458-28-4; Acetylglucosaminidase, EC 3.2.1.30; dolichyl-diphosphooligosaccharide - protein glycotransferase, EC 2.4.1.119; Glucose, 50-99-7; Glucosyltransferases, EC 2.4.1.-; Glycoproteins; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, EC 3.2.1.96; Peptide Hydrolases, EC 3.4; Transferases, EC 2.
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v28_n20_p8108_Trombetta

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Citas:

---------- APA ----------
Trombetta, S.E., Bosch, M. & Parodi, A.J. (1989) . Glucosylation of Glycoproteins by Mammalian, Plant, Fungal, and Trypanosomatid Protozoa Microsomal Membranes. Biochemistry, 28(20), 8108-8116.
http://dx.doi.org/10.1021/bi00446a022
---------- CHICAGO ----------
Trombetta, S.E., Bosch, M., Parodi, A.J. "Glucosylation of Glycoproteins by Mammalian, Plant, Fungal, and Trypanosomatid Protozoa Microsomal Membranes" . Biochemistry 28, no. 20 (1989) : 8108-8116.
http://dx.doi.org/10.1021/bi00446a022
---------- MLA ----------
Trombetta, S.E., Bosch, M., Parodi, A.J. "Glucosylation of Glycoproteins by Mammalian, Plant, Fungal, and Trypanosomatid Protozoa Microsomal Membranes" . Biochemistry, vol. 28, no. 20, 1989, pp. 8108-8116.
http://dx.doi.org/10.1021/bi00446a022
---------- VANCOUVER ----------
Trombetta, S.E., Bosch, M., Parodi, A.J. Glucosylation of Glycoproteins by Mammalian, Plant, Fungal, and Trypanosomatid Protozoa Microsomal Membranes. Biochemistry. 1989;28(20):8108-8116.
http://dx.doi.org/10.1021/bi00446a022