Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-8-28
pubmed:abstractText
Abs to ribosomal P protein have been shown to bind a membrane form of the P0 38-kDa ribosomal phosphoprotein. This study shows that after affinity-purified Abs to ribosomal P proteins bind living HepG2 cells, they then penetrate these live cells and cause cellular dysfunction. Binding and penetration of anti-P Abs is the property of F(ab')2 fragments as well as whole IgG molecules showing that neither binding nor penetration depends on Fc fragments or their cognate receptors. Confocal microscopy shows that internalized Ab concentrates in perinuclear vesicles (presumably lysosomes), but substantial quantities of Ab are also found in the cytosol. This intracellular Ab adversely affects the synthesis of apolipoprotein B resulting in a threefold increase in cellular cholesterol with lipid droplet accumulation as seen in some chronic liver diseases. It also has a profound inhibitory effect on global protein synthesis as measured by [35S]methionine incorporation. These studies therefore describe a model of cellular injury effected by specific Ab to ribosomal "P" protein that may underlie certain forms of autoimmune hepatic diseases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2033-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Autoantibodies to ribosomal P proteins penetrate into live hepatocytes and cause cellular dysfunction in culture.
pubmed:affiliation
Arthritis/Immunology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.