Linked Life Data

11251884

Source:http://linkedlifedata.com/resource/pubmed/id/11251884

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-3-19
pubmed:abstractText
Anti-Ro (or SSA) is found in the sera of patients with autoimmune rheumatic illnesses. All patients with anti-Ro defined by precipitation bind a 60 000 Da antigen (60 kDa Ro), whereas some patients also bind a 52 000 Da molecule (52 kDa Ro). In general, antibody binding is directed against native 60 kDa Ro and denatured 52 kDa Ro. The mechanism by which anti-52 kDa Ro arises in the setting of anti-60 kDa Ro is unknown. Conflicting data exist as to the existence of a physical interaction between the two proteins in cells and as to cross-reacting antibodies. Antibodies were affinity purified from a peptide within the leucine zipper region of 52 kDa Ro. These purified antibodies binding the 197-207 peptide from 52 kDa Ro (anti-52LZ) bound native 60 kDa Ro as well as denatured 52 kDa Ro. In addition, anti-52LZ also bound up to four regions from the sequence of 60 kDa Ro and a single conformational epitope of 60 kDa Ro. Thus, these primary sites represent components of the tertiary epitope. We hypothesized that if this was the case, these peptides making up a tertiary epitope would show molecular interaction. In fact, peptides from 60 kDa Ro have a molecular interaction with the 52 kDa Ro peptide as well as full-length 52 kDa Ro when assessed by surface plasmon resonance. The leucine-zipper region peptide from 52 kDa Ro bound three of the four peptides from 60 kDa Ro. These data suggest that these two molecular species, 60 and 52 kDa Ro, form a conformational epitope. This relationship may explain why anti-52 kDa Ro is found in association with anti-60 kDa Ro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0300-9475
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
268-76
pubmed:dateRevised
2007-5-11
pubmed:meshHeading
pubmed-meshheading:11251884-Amino Acid Sequence, pubmed-meshheading:11251884-Autoantibodies, pubmed-meshheading:11251884-Autoantigens, pubmed-meshheading:11251884-Binding Sites, pubmed-meshheading:11251884-Chromatography, Affinity, pubmed-meshheading:11251884-Cross Reactions, pubmed-meshheading:11251884-Epitopes, pubmed-meshheading:11251884-Humans, pubmed-meshheading:11251884-Leucine Zippers, pubmed-meshheading:11251884-Lupus Erythematosus, Systemic, pubmed-meshheading:11251884-Molecular Weight, pubmed-meshheading:11251884-Protein Conformation, pubmed-meshheading:11251884-Protein Denaturation, pubmed-meshheading:11251884-Protein Structure, Tertiary, pubmed-meshheading:11251884-RNA, Small Cytoplasmic, pubmed-meshheading:11251884-Ribonucleoproteins, pubmed-meshheading:11251884-Surface Plasmon Resonance
pubmed:year
2001
pubmed:articleTitle
Autoantibody to the leucine zipper region of 52 kDa Ro/SSA binds native 60 kDa Ro/SSA: identification of a tertiary epitope with components from 60 kDa Ro/SSA and 52 kDa Ro/SSA.
pubmed:affiliation
Arthritis and Immunology Program, Oklahoma Medical Research Foundation, University of Oklahoma Health Sciences Center, 825 NE 13th Street, Oklahoma City, OK 73104, USA.
pubmed:publicationType
Journal Article, In Vitro