Source:http://linkedlifedata.com/resource/pubmed/id/12710947
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2003-4-24
|
pubmed:abstractText |
Aggresome formation in cells involves the failure of the ubiquitin-proteasome pathway to dispose of proteins destined for degradation by the 26S proteasome. UBB(+1) is present in Mallory bodies in alcoholic liver disease and in aggresomes formed in Alzheimer's desease. The present investigation focuses on the role that UBB(+1) plays in cytokeratin aggresome formation in Mallory bodies (MBs) in vitro. Immunoprecipitation with a monoclonal antibody to cytokeratin-8 (CK-8) was used. The immunoprecipitate was incubated for 24 h in the presence of different constituents involved in aggresome formation including ubiquitin, UBB(+1), the proteasome inhibitor PS341, an ATP generating energy source, a deubiquitinating enzyme inhibitor, a purified proteasome fraction, and an E(1-3) conjugating enzyme fraction. MB-like protein aggregates formed in the presence of ubiquitin, plus UBB(+1) or PS341. These aggregates stained positively for CK-8. UBB(+1), and a proteasome subunit Tbp7, as demonstrated on Western blots. A second approach was used to form MBs in vitro in cultured hepatocytes transfected with UBB(+1) protein using Chariot. The cells were double stained using CK-8 and ubiquitin antibodies. The two proteins colocalized in MB-like aggregates. The results support the possibility that aggresome formation is a complex multifactor process, which is favored by inhibition of the proteasome and by the presence of UBB(+1).
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP dependent 26S protease,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Keratins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0014-4800
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
74
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
160-7
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:12710947-Adenosine Triphosphate,
pubmed-meshheading:12710947-Animals,
pubmed-meshheading:12710947-Cells, Cultured,
pubmed-meshheading:12710947-DNA-Binding Proteins,
pubmed-meshheading:12710947-Hepatocytes,
pubmed-meshheading:12710947-Immunohistochemistry,
pubmed-meshheading:12710947-Inclusion Bodies,
pubmed-meshheading:12710947-Keratins,
pubmed-meshheading:12710947-Male,
pubmed-meshheading:12710947-Mice,
pubmed-meshheading:12710947-Mice, Inbred C3H,
pubmed-meshheading:12710947-Mutation,
pubmed-meshheading:12710947-Peptide Hydrolases,
pubmed-meshheading:12710947-Proteasome Endopeptidase Complex,
pubmed-meshheading:12710947-Transcription Factors,
pubmed-meshheading:12710947-Ubiquitin
|
pubmed:year |
2003
|
pubmed:articleTitle |
The mechanism of cytokeratin aggresome formation: the role of mutant ubiquitin (UBB+1).
|
pubmed:affiliation |
Department of Pathology, Harbor-UCLA Medical Center, Torrance, CA 90509, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|