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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1989-1-24
pubmed:abstractText
We have recently described the occurrence of integral membrane glycoproteins in rat liver smooth and rough endoplasmic reticulum with O-N-acetylglucosamine facing the cytosolic and luminal sides of the membrane (Abeijon, C., and Hirschberg, C. B. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 1010-1014). We now report that integral membrane glycoproteins with cytosolic facing O-N-acetylglucosamine also occur in membranes of rat liver Golgi apparatus. This was determined following incubation of vesicles from the Golgi apparatus, which were sealed and of the same membrane topographical orientation as in vivo, with UDP-[14C]galactose and saturating amounts of bovine milk galactosyltransferase. This enzyme does not enter the lumen of the vesicles and specifically catalyzes the addition of galactose, in a beta 1-4 linkage, to terminal N-acetylglucosamine. Under these conditions, galactose was transferred to a glycoprotein of molecular mass of 92 kDa. This protein was insoluble in sodium carbonate, pH 11.5, conditions under which integral membrane proteins remain membrane bound and was insensitive to treatment with peptide:N-glycosidase F. beta Elimination and chromatography showed that radiolabeled galactose was part of a disaccharide which was characterized as Gal beta 1-4GlcNAcitol. This glycoprotein is specific of the Golgi apparatus membrane. Intrinsic membrane glycoproteins with this unusual carbohydrate membrane orientation thus occur in the endoplasmic reticulum and Golgi apparatus of rat liver.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19778-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
An intrinsic membrane glycoprotein of the golgi apparatus with O-linked N-acetylglucosamine facing the cytosol.
pubmed:affiliation
Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01655.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.