Linked Life Data

19582722

Source:http://linkedlifedata.com/resource/pubmed/id/19582722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2009-7-14
pubmed:abstractText
PTMs, such as glycosylation and phosphorylation of apolipoprotein B100 (apoB), are known to be involved with modulating the metabolism of apoB-containing lipoproteins. Current evidence suggests that intracellular and extracellular PTM of apoB are associated with various disorders such diabetes, dyslipidemia and atherosclerosis. The ability to identify and characterize the specific PTM of apoB correlating to specific pathologies may improve our understanding of the underlying molecular mechanisms regulating apoB metabolism. We have developed an assay to detect PTM and/or conformational changes in apoB isolated from the media of HepG2 cells. Using trypsin digestion in conjunction with 2-DE and Western blotting, a 2-D peptide fragment profile of apoB was established. The 2-D apoB profile was composed of a number of trypsin-generated fragments having a molecular mass between 10 and 188 kDa and a wide spectrum of isoelectric points. The 2-D apoB profile obtained from the media of HepG2 cells treated in the presence of agents (tunicamycin and glucosamine) known to modulate the PTM of apoB was distinct from that of control cells. Identifying changes in the 2-D apoB profile has the potential to not only provide insight into the underlying mechanisms regulating the metabolism of apoB-containing lipoproteins but may also have important implications for the development of novel diagnostic tools and/or future therapeutic agents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1522-2683
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2227-33
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Development of a 2-D apoB peptide profile to detect conformational changes associated with apoB-containing lipoproteins.
pubmed:affiliation
Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't