Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.

Class II molecules of the major histocompatibility complex (MHC) are composed of two polymorphic glycoprotein chains (alpha and beta), that associate in the ER with a third, non-polymorphic glycoprotein known as the invariant chain (Ii). We have examined the relationship between the intracellular tr...

Ful tanımlama

Detaylı Bibliyografya
Asıl Yazarlar: Bonnerot, C, Marks, MS, Cosson, P, Robertson, E, Bikoff, E, Germain, R, Bonifacino, J
Materyal Türü: Journal article
Dil:English
Baskı/Yayın Bilgisi: 1994
_version_ 1826283343850766336
author Bonnerot, C
Marks, MS
Cosson, P
Robertson, E
Bikoff, E
Germain, R
Bonifacino, J
author_facet Bonnerot, C
Marks, MS
Cosson, P
Robertson, E
Bikoff, E
Germain, R
Bonifacino, J
author_sort Bonnerot, C
collection OXFORD
description Class II molecules of the major histocompatibility complex (MHC) are composed of two polymorphic glycoprotein chains (alpha and beta), that associate in the ER with a third, non-polymorphic glycoprotein known as the invariant chain (Ii). We have examined the relationship between the intracellular transport and physico-chemical characteristics of various combinations of murine alpha, beta and Ii chains. Biochemical and morphological analyses of transfected fibroblasts expressing class II MHC chains show that both unassembled alpha and beta chains, as well as a large fraction of alpha+beta complexes synthesized in the absence of Ii chain, are retained in the ER in association with the immunoglobulin heavy chain binding protein, BiP. Analyses by sedimentation velocity on sucrose gradients show that most incompletely assembled class II MHC species exist as high molecular weight aggregates in both transfected fibroblasts and spleen cells from mice carrying a disruption of the Ii chain gene. This is in contrast to the sedimentation properties of alpha beta Ii complexes from normal mice, which migrate as discrete, stoichiometric complexes of M(r) approximately 200,000-300,000. These observations suggest that assembly with the Ii chain prevents accumulation of aggregated alpha and beta chains in the ER, which might relate to the known ability of the Ii chain to promote exit of class II MHC molecules from the ER.
first_indexed 2024-03-07T00:57:29Z
format Journal article
id oxford-uuid:8894394f-b50e-4fd1-a701-d0ae8a59953f
institution University of Oxford
language English
last_indexed 2024-03-07T00:57:29Z
publishDate 1994
record_format dspace
spelling oxford-uuid:8894394f-b50e-4fd1-a701-d0ae8a59953f2022-03-26T22:18:18ZAssociation with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8894394f-b50e-4fd1-a701-d0ae8a59953fEnglishSymplectic Elements at Oxford1994Bonnerot, CMarks, MSCosson, PRobertson, EBikoff, EGermain, RBonifacino, JClass II molecules of the major histocompatibility complex (MHC) are composed of two polymorphic glycoprotein chains (alpha and beta), that associate in the ER with a third, non-polymorphic glycoprotein known as the invariant chain (Ii). We have examined the relationship between the intracellular transport and physico-chemical characteristics of various combinations of murine alpha, beta and Ii chains. Biochemical and morphological analyses of transfected fibroblasts expressing class II MHC chains show that both unassembled alpha and beta chains, as well as a large fraction of alpha+beta complexes synthesized in the absence of Ii chain, are retained in the ER in association with the immunoglobulin heavy chain binding protein, BiP. Analyses by sedimentation velocity on sucrose gradients show that most incompletely assembled class II MHC species exist as high molecular weight aggregates in both transfected fibroblasts and spleen cells from mice carrying a disruption of the Ii chain gene. This is in contrast to the sedimentation properties of alpha beta Ii complexes from normal mice, which migrate as discrete, stoichiometric complexes of M(r) approximately 200,000-300,000. These observations suggest that assembly with the Ii chain prevents accumulation of aggregated alpha and beta chains in the ER, which might relate to the known ability of the Ii chain to promote exit of class II MHC molecules from the ER.
spellingShingle Bonnerot, C
Marks, MS
Cosson, P
Robertson, E
Bikoff, E
Germain, R
Bonifacino, J
Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title_full Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title_fullStr Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title_full_unstemmed Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title_short Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
title_sort association with bip and aggregation of class ii mhc molecules synthesized in the absence of invariant chain
work_keys_str_mv AT bonnerotc associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT marksms associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT cossonp associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT robertsone associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT bikoffe associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT germainr associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain
AT bonifacinoj associationwithbipandaggregationofclassiimhcmoleculessynthesizedintheabsenceofinvariantchain