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UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothane.
Chem Res Toxicol. 1997 Jan; 10(1):59-63.CR

Abstract

Halothane causes an idiosyncratic hepatitis that is thought to result, in part, from immune reactions against one or more lumenal endoplasmic reticulum (ER) proteins that have been covalently modified by the trifluoroacetyl chloride metabolite of halothane. In this study, we have identified a 170 kDa protein target of halothane in the liver of rats. The 170 kDa protein was first detected when proteins in lysates of hepatocytes from halothane-treated rats were immunoprecipitated with antisera against several resident ER proteins. This 170 kDa protein was found to be associated with other protein targets of halothane, including protein disulfide isomerase, a protein disulfide isomerase isoform, a 59 kDa carboxylesterase, and 78 kDa glucose-regulated protein. Immunoblotting with antiserum directed against the trifluoroacetylated hapten indicated that the 170 kDa protein was trifluoroacetylated. Based upon its subcellular localization, molecular mass, N-terminal amino acid sequence, and antigenicity, the trifluoroacetylated 170 kDa protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGGT), a lumenal ER protein that is thought to have a role in the folding of N-linked glycoproteins. Moreover, treatment of rats with halothane caused a 44% decrease in the activity of liver microsomal UGGT, and at least 36% of the change in the activity of the enzyme could be due to a decrease in the level of the protein. The results suggest that the function of UGGT in folding of N-linked glycoproteins may be affected by other resident ER proteins or xenobiotics such as halothane.

Authors+Show Affiliations

Molecular and Cellular Toxicology Section, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-1760, USA. Hamid_Amouzadeh@nih.govNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9074803

Citation

Amouzadeh, H R., et al. "UDP-glucose:glycoprotein Glucosyltransferase Associates With Endoplasmic Reticulum Chaperones and Its Activity Is Decreased in Vivo By the Inhalation Anesthetic Halothane." Chemical Research in Toxicology, vol. 10, no. 1, 1997, pp. 59-63.
Amouzadeh HR, Bourdi M, Martin JL, et al. UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothane. Chem Res Toxicol. 1997;10(1):59-63.
Amouzadeh, H. R., Bourdi, M., Martin, J. L., Martin, B. M., & Pohl, L. R. (1997). UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothane. Chemical Research in Toxicology, 10(1), 59-63.
Amouzadeh HR, et al. UDP-glucose:glycoprotein Glucosyltransferase Associates With Endoplasmic Reticulum Chaperones and Its Activity Is Decreased in Vivo By the Inhalation Anesthetic Halothane. Chem Res Toxicol. 1997;10(1):59-63. PubMed PMID: 9074803.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothane. AU - Amouzadeh,H R, AU - Bourdi,M, AU - Martin,J L, AU - Martin,B M, AU - Pohl,L R, PY - 1997/1/1/pubmed PY - 1997/1/1/medline PY - 1997/1/1/entrez SP - 59 EP - 63 JF - Chemical research in toxicology JO - Chem. Res. Toxicol. VL - 10 IS - 1 N2 - Halothane causes an idiosyncratic hepatitis that is thought to result, in part, from immune reactions against one or more lumenal endoplasmic reticulum (ER) proteins that have been covalently modified by the trifluoroacetyl chloride metabolite of halothane. In this study, we have identified a 170 kDa protein target of halothane in the liver of rats. The 170 kDa protein was first detected when proteins in lysates of hepatocytes from halothane-treated rats were immunoprecipitated with antisera against several resident ER proteins. This 170 kDa protein was found to be associated with other protein targets of halothane, including protein disulfide isomerase, a protein disulfide isomerase isoform, a 59 kDa carboxylesterase, and 78 kDa glucose-regulated protein. Immunoblotting with antiserum directed against the trifluoroacetylated hapten indicated that the 170 kDa protein was trifluoroacetylated. Based upon its subcellular localization, molecular mass, N-terminal amino acid sequence, and antigenicity, the trifluoroacetylated 170 kDa protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGGT), a lumenal ER protein that is thought to have a role in the folding of N-linked glycoproteins. Moreover, treatment of rats with halothane caused a 44% decrease in the activity of liver microsomal UGGT, and at least 36% of the change in the activity of the enzyme could be due to a decrease in the level of the protein. The results suggest that the function of UGGT in folding of N-linked glycoproteins may be affected by other resident ER proteins or xenobiotics such as halothane. SN - 0893-228X UR - https://www.unboundmedicine.com/medline/citation/9074803/UDP_glucose:glycoprotein_glucosyltransferase_associates_with_endoplasmic_reticulum_chaperones_and_its_activity_is_decreased_in_vivo_by_the_inhalation_anesthetic_halothane_ L2 - https://dx.doi.org/10.1021/tx9601364 DB - PRIME DP - Unbound Medicine ER -