Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-10-1
pubmed:abstractText
Recent studies demonstrate that processing of N-linked glycans plays an important role in the quality control of major histocompatibility complex (MHC) class I transport from the endoplasmic reticulum (ER) to the Golgi complex and beyond. Here, we investigated the importance of oligosaccharide chain length on the association of MHC class I proteins with molecular chaperones and their intracellular transport from the ER to the Golgi. These data show that calnexin interaction with class I proteins having truncated N-glycans was reduced compared to normal class I molecules, whereas the assembly of class I with calreticulin and TAP was unperturbed by N-glycan chain length. Additionally, these results demonstrate that class I proteins containing truncated N-glycans showed decreased detachment from calreticulin and TAP relative to class I proteins bearing typical oligosaccharides. Taken together, these studies show that N-glycan chain length is an important determinant for the quality control of newly synthesized MHC class I proteins in the ER.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
473-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Influence of N-glycan chain length on chaperone association and intracellular transport of major histocompatibility complex class I proteins.
pubmed:affiliation
School of Medicine, East Carolina University, Greenville, North Carolina, 27858-4354, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.