Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0042961 (volvulus)
 4,305 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ro/SS-A antibodies are found in a number of human autoimmune disorders including Sjogren's syndrome and several systemic lupus erythematosus-related disorders. These heterogeneous autoantibodies are known to recognize several distinct cellular antigens. With synthetic oligonucleotides corresponding to amino acid sequence information we have isolated a full-length cDNA clone which encodes a human Ro ribonucleoprotein autoantigen. The 1,890-base pair clone contains an open reading frame that encodes a 417-amino acid, 48-kD polypeptide that migrates aberrantly at 60 kD by SDS-PAGE. Rabbit antibodies raised against this protein's recently described amino-terminal epitope react with a previously identified 52-kD human Ro protein and immunoprecipitate the human cytoplasmic RNAs. Ultraviolet light cross-linking studies suggest that this Ro protein binds each of the four major human cytoplasmic RNAs. The deduced amino acid sequence is 63% homologous to an Onchocerca volvulus antigen. Southern filter hybridization analysis indicates that this gene is not highly polymorphic and exists as a single copy in the human genome. Chromosomal localization studies place this gene on the short arm of chromosome 19 near the gene encoding the low density lipoprotein receptor.
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PMID:Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen. 233 96

The Ro/SS-A (Ro) autoantigens consist of at least four immunologically distinct proteins which are recognized by autoantibodies typically found in sera from patients with primary Sjogren's syndrome and in subsets of patients with lupus erythematosus. We recently isolated a 1.9-kb human cDNA clone which encodes one of these Ro autoantigens. Synthetic oligonucleotides corresponding to the human Ro sequence were used to amplify the homologous gene from a murine B cell cDNA library using the polymerase chain reaction. The mouse cDNA-encoded amino acid sequence was found to be 94% homologous to the human Ro sequence and is 100% homologous to murine calreticulin, a high affinity calcium-binding protein which resides in the endoplasmic and sarcoplasmic reticulum. The amino acid sequence of rabbit calreticulin is 92% homologous to both murine calreticulin and human Ro. Onchocerca volvulus and Drosophila melanogaster also have molecules that are highly homologous to human Ro. In addition, human Ro has a molecular mass, isoelectric point, and significant amino acid sequence similar to the Aplysia californica snail neuronal protein 407. These homologies suggest that this Ro protein has a very basic cellular function(s) which may in part involve calcium binding.
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PMID:A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia "memory molecule". 236 22