Linked Life Data

11823543

Source:http://linkedlifedata.com/resource/pubmed/id/11823543

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-2-1
pubmed:abstractText
Autoantibodies directed against spliceosomal proteins are a common and specific feature of systemic lupus erythematosus. These autoantibodies target a collection of proteins, including Sm B, B', D1, D2, and D3. We define the common antigenic targets of Sm D2 and D3 and examine their role in spliceosomal autoimmunity. Our results define nine major common epitopes, five on Sm D2 and four on Sm D3. These epitopes have significantly higher (more basic) isoelectric points than do nonantigenic regions. In fact, this association is of sufficient power to make isoelectric point an excellent predictor of spliceosomal antigenicity. The crystallographic structure of Sm D2 and D3 is now partially described. The anti-Sm D2 and D3 antigenic targets are located on the surface of the respective three-dimensional complexed proteins, thereby suggesting that these epitopes are accessible in the native configuration. All but one of these nine epitopes conspicuously avoid the specific regions involved in intermolecular interactions within the spliceosomal complex. One of the D3 epitopes (RGRGRGMGR) has significant sequence homology with a major antigenic region of Sm D1 (containing a carboxyl-terminal glycine-arginine repeat), and anti-D3 Abs cross-react with this epitope of Sm D1. These results demonstrate that spliceosomal targets of autoimmunity are accessible on native structure surfaces and that cross-reactive epitopes, as well as structural associations of various spliceosomal Ags, may be involved in the induction of autoimmunity in systemic lupus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
168
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2054-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11823543-Adolescent, pubmed-meshheading:11823543-Adult, pubmed-meshheading:11823543-Amino Acid Sequence, pubmed-meshheading:11823543-Amino Acids, Basic, pubmed-meshheading:11823543-Autoantibodies, pubmed-meshheading:11823543-Autoantigens, pubmed-meshheading:11823543-Binding, Competitive, pubmed-meshheading:11823543-Crystallography, X-Ray, pubmed-meshheading:11823543-Epitope Mapping, pubmed-meshheading:11823543-Epitopes, B-Lymphocyte, pubmed-meshheading:11823543-Female, pubmed-meshheading:11823543-Humans, pubmed-meshheading:11823543-Isoelectric Point, pubmed-meshheading:11823543-Lupus Erythematosus, Systemic, pubmed-meshheading:11823543-Macromolecular Substances, pubmed-meshheading:11823543-Male, pubmed-meshheading:11823543-Models, Molecular, pubmed-meshheading:11823543-Molecular Sequence Data, pubmed-meshheading:11823543-Ribonucleoproteins, Small Nuclear, pubmed-meshheading:11823543-Spliceosomes
pubmed:year
2002
pubmed:articleTitle
Anti-sm autoantibodies in systemic lupus target highly basic surface structures of complexed spliceosomal autoantigens.
pubmed:affiliation
Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't