Matches in SemOpenAlex for { <https://semopenalex.org/work/W2565087697> ?p ?o ?g. }
Showing items 1 to 74 of
74
with 100 items per page.
- W2565087697 abstract "Apolipoprotein B-100 (apoB) is the central protein component of very low density lipoproteins (VLDL) and is subject to endoplasmic reticulum-associated degradation (ERAD). Hepatic assembly of VLDL particles is monitored by the cellular quality control machinery, which determines whether a properly formed lipoprotein is secreted or the inadequately lipidated apoB protein is degraded. Changes in lipid supply, ER folding capacity or ERAD pathway function can alter VLDL output from HepG2 cells. Bag6 is a cytosolic protein that has a role in the bilayer integration of proteins and is also implicated in maintaining the solubility of proteasome substrates that contain exposed hydrophobic regions. Notably, Bag6 has been observed to interact with the ERAD components gp78 and p97, which are known to facilitate apoB degradation. The goal of this study was to evaluate the role of cytosolic Bag6 in apoB metabolism in HepG2 cells. When MG132 was used to inhibit proteasomal degradation of apoB, Bag6 was co-immunoprecipitated with apoB as determined by functional proteomics and immunoblot analysis. Conversely, if VLDL assembly was enhanced by treatment of the cells with the MEK/ERK inhibitor U0126, both the Bag6-apoB and p97-apoB associations were no longer detectable. Metabolic labelling studies indicated that siRNA knockdown of Bag6 did not alter the initial rate of apoB biosynthesis, but decreased the secretion of newly synthesized apoB. The decrease in apoB secretion with Bag6 knockdown could not be reversed by U0126. In addition, Bag6 knockdown decreased the effectiveness of MG132 as an inhibitor of cellular apoB degradation even though ubiquitination of apoB appeared to be unaffected. These observations suggest that Bag6 may be a component of the ERAD pathway that modulates VLDL assembly. Reduction of Bag6 partially decreases both secretion and MG132-inhibitable degradation of apoB, suggesting that another mechanism is also involved in apoB degradation. We hypothesize that the “holdase” function of Bag6 may temporarily stabilize exposed hydrophobic domains of apoB prior to its progression to assembly or degradation." @default.
- W2565087697 created "2017-01-06" @default.
- W2565087697 creator A5027914982 @default.
- W2565087697 creator A5090810310 @default.
- W2565087697 date "2012-05-01" @default.
- W2565087697 modified "2023-09-23" @default.
- W2565087697 title "Abstract 164: The Chaperone Holdase Bag6 Modulates the Intracellular Fate of Newly Synthesized ApoB100" @default.
- W2565087697 doi "https://doi.org/10.1161/atvb.32.suppl_1.a164" @default.
- W2565087697 hasPublicationYear "2012" @default.
- W2565087697 type Work @default.
- W2565087697 sameAs 2565087697 @default.
- W2565087697 citedByCount "0" @default.
- W2565087697 crossrefType "journal-article" @default.
- W2565087697 hasAuthorship W2565087697A5027914982 @default.
- W2565087697 hasAuthorship W2565087697A5090810310 @default.
- W2565087697 hasConcept C104317684 @default.
- W2565087697 hasConcept C139447449 @default.
- W2565087697 hasConcept C158617107 @default.
- W2565087697 hasConcept C158619295 @default.
- W2565087697 hasConcept C173396325 @default.
- W2565087697 hasConcept C181199279 @default.
- W2565087697 hasConcept C185592680 @default.
- W2565087697 hasConcept C190283241 @default.
- W2565087697 hasConcept C25602115 @default.
- W2565087697 hasConcept C27740335 @default.
- W2565087697 hasConcept C2778163477 @default.
- W2565087697 hasConcept C2780072125 @default.
- W2565087697 hasConcept C2992195973 @default.
- W2565087697 hasConcept C49039625 @default.
- W2565087697 hasConcept C55493867 @default.
- W2565087697 hasConcept C62746215 @default.
- W2565087697 hasConcept C8243546 @default.
- W2565087697 hasConcept C86803240 @default.
- W2565087697 hasConcept C95444343 @default.
- W2565087697 hasConcept C98539663 @default.
- W2565087697 hasConceptScore W2565087697C104317684 @default.
- W2565087697 hasConceptScore W2565087697C139447449 @default.
- W2565087697 hasConceptScore W2565087697C158617107 @default.
- W2565087697 hasConceptScore W2565087697C158619295 @default.
- W2565087697 hasConceptScore W2565087697C173396325 @default.
- W2565087697 hasConceptScore W2565087697C181199279 @default.
- W2565087697 hasConceptScore W2565087697C185592680 @default.
- W2565087697 hasConceptScore W2565087697C190283241 @default.
- W2565087697 hasConceptScore W2565087697C25602115 @default.
- W2565087697 hasConceptScore W2565087697C27740335 @default.
- W2565087697 hasConceptScore W2565087697C2778163477 @default.
- W2565087697 hasConceptScore W2565087697C2780072125 @default.
- W2565087697 hasConceptScore W2565087697C2992195973 @default.
- W2565087697 hasConceptScore W2565087697C49039625 @default.
- W2565087697 hasConceptScore W2565087697C55493867 @default.
- W2565087697 hasConceptScore W2565087697C62746215 @default.
- W2565087697 hasConceptScore W2565087697C8243546 @default.
- W2565087697 hasConceptScore W2565087697C86803240 @default.
- W2565087697 hasConceptScore W2565087697C95444343 @default.
- W2565087697 hasConceptScore W2565087697C98539663 @default.
- W2565087697 hasIssue "suppl_1" @default.
- W2565087697 hasLocation W25650876971 @default.
- W2565087697 hasOpenAccess W2565087697 @default.
- W2565087697 hasPrimaryLocation W25650876971 @default.
- W2565087697 hasRelatedWork W2027988379 @default.
- W2565087697 hasRelatedWork W2068067496 @default.
- W2565087697 hasRelatedWork W2097963351 @default.
- W2565087697 hasRelatedWork W2139653729 @default.
- W2565087697 hasRelatedWork W2145161673 @default.
- W2565087697 hasRelatedWork W2391179902 @default.
- W2565087697 hasRelatedWork W2565087697 @default.
- W2565087697 hasRelatedWork W2799789464 @default.
- W2565087697 hasRelatedWork W2897243648 @default.
- W2565087697 hasRelatedWork W37241425 @default.
- W2565087697 hasVolume "32" @default.
- W2565087697 isParatext "false" @default.
- W2565087697 isRetracted "false" @default.
- W2565087697 magId "2565087697" @default.
- W2565087697 workType "article" @default.