Linked Life Data

8599890

Source:http://linkedlifedata.com/resource/pubmed/id/8599890

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-4-30
pubmed:abstractText
Autoantibodies against centromere proteins are commonly found in the serum of patients with scleroderma and other systemic autoimmune diseases. The reactivity of anticentromere autoantibodies (ACA) from 78 patients was investigated by ELISA using two kinds of a 15-amino-acid peptide corresponding to the N- and C-termini of CENP-A, one of the target molecules of ACA. The N-terminal peptide (residues 3-17) was recognized by 85% of ACA, while the C- terminal peptide (residues 126-140) was not. The ELISA result for the N-terminal peptide correlated with the immunoreactivity of CENP-A observed in immunoblotting. Moreover, the binding between autoantibodies and CENP-A was inhibited by the N-terminal peptide in 98.5% of anti-CENP-A- positive sera in immunoblotting. The sequence of peptide, PRRRSRKPEAPRRRS, is highly charged and has two repeats of PRRRS. These results indicate that the N-terminal-charged region forms a major epitope of CENP-A. This area may be involved in the induction of specific autoantibodies against centromere in autoimmune patients.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0090-1229
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A charged segment mainly composed of basic amino acids forms an autoepitope of CENP-A.
pubmed:affiliation
Department of Dermatology, Nagoya University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't