n(2)-n(2)-7-trimethylguanosine and Scleroderma--Systemic

n(2)-n(2)-7-trimethylguanosine has been researched along with Scleroderma--Systemic* in 2 studies

Other Studies

2 other study(ies) available for n(2)-n(2)-7-trimethylguanosine and Scleroderma--Systemic

Article	Year
Rare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs. Proceedings of the National Academy of Sciences of the United States of America, 1993, Jul-15, Volume: 90, Issue:14 We have identified a scleroderma serum (Ru) with a previously undescribed specificity to protein components of the U11 small nuclear ribonucleoprotein particle (snRNP), a low-abundance member of the Sm class of U RNPs. The U11 RNP can be specifically immunoprecipitated from sonicated HeLa cells with Ru serum. In nuclear extracts, a fraction of the U11 particle is found complexed to the U12 RNP, an even lower abundance Sm snRNP. In glycerol gradient fractions, Ru serum identifies a 65-kDa protein that cosediments with the U11-U12 complex and is shifted upon targeted degradation of the U12 RNA. The 65-kDa protein therefore appears to be a component of the U11-U12 snRNP complex, whereas another Ru-reactive (140 kDa) protein may be associated with the free U11 RNP. The Ru serum also contains autoantibodies directed against the trimethylguanosine cap of U RNAs. This rare specificity has been described previously in only three other scleroderma patients. Topics: Adult; Antibodies, Antinuclear; Antibody Specificity; Female; Guanosine; Humans; Ribonucleoproteins, Small Nuclear; RNA Caps; RNA, Small Nuclear; Scleroderma, Systemic; Sequence Analysis, RNA	1993
Novel human autoantibodies reactive with 5'-terminal trimethylguanosine cap structures of U small nuclear RNA. Journal of immunology (Baltimore, Md. : 1950), 1992, Aug-01, Volume: 149, Issue:3 A class of RNA-containing particles, U small nuclear/nucleolar ribonucleoprotein particles (U snRNP), are well known to be targets for sera from patients with various autoimmune diseases. In the most cases the protein components carry the antigenic determinants. We have identified serum autoantibodies from three patients with systemic sclerosis that were directed against U1-U5 snRNA by immunoprecipitation of deproteinized 32PO4 labeled HeLa cell total RNA. By competitive radioimmunoprecipitation assays, an experimentally induced anti-2,2,7-trimethylguanosine (TMG) cap structure mAb inhibited the reaction of these antisera. In addition, IgG isolated from the antisera inhibited the anti-TMG mAb reaction to the U snRNA. Furthermore, a structural analog, 7-methylguanosine-triphosphate, competitively inhibited the reaction of the antisera to the U snRNA. Thus we concluded that the TMG cap structure of the U snRNA could be a target for serum autoantibodies. Topics: Autoantibodies; Autoantigens; Binding, Competitive; Guanosine; Humans; Precipitin Tests; RNA Caps; RNA, Small Nuclear; Scleroderma, Systemic	1992

Article

Year

Rare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs.

Proceedings of the National Academy of Sciences of the United States of America, 1993, Jul-15, Volume: 90, Issue:14

We have identified a scleroderma serum (Ru) with a previously undescribed specificity to protein components of the U11 small nuclear ribonucleoprotein particle (snRNP), a low-abundance member of the Sm class of U RNPs. The U11 RNP can be specifically immunoprecipitated from sonicated HeLa cells with Ru serum. In nuclear extracts, a fraction of the U11 particle is found complexed to the U12 RNP, an even lower abundance Sm snRNP. In glycerol gradient fractions, Ru serum identifies a 65-kDa protein that cosediments with the U11-U12 complex and is shifted upon targeted degradation of the U12 RNA. The 65-kDa protein therefore appears to be a component of the U11-U12 snRNP complex, whereas another Ru-reactive (140 kDa) protein may be associated with the free U11 RNP. The Ru serum also contains autoantibodies directed against the trimethylguanosine cap of U RNAs. This rare specificity has been described previously in only three other scleroderma patients.

Topics: Adult; Antibodies, Antinuclear; Antibody Specificity; Female; Guanosine; Humans; Ribonucleoproteins, Small Nuclear; RNA Caps; RNA, Small Nuclear; Scleroderma, Systemic; Sequence Analysis, RNA

1993

Novel human autoantibodies reactive with 5'-terminal trimethylguanosine cap structures of U small nuclear RNA.

Journal of immunology (Baltimore, Md. : 1950), 1992, Aug-01, Volume: 149, Issue:3

A class of RNA-containing particles, U small nuclear/nucleolar ribonucleoprotein particles (U snRNP), are well known to be targets for sera from patients with various autoimmune diseases. In the most cases the protein components carry the antigenic determinants. We have identified serum autoantibodies from three patients with systemic sclerosis that were directed against U1-U5 snRNA by immunoprecipitation of deproteinized 32PO4 labeled HeLa cell total RNA. By competitive radioimmunoprecipitation assays, an experimentally induced anti-2,2,7-trimethylguanosine (TMG) cap structure mAb inhibited the reaction of these antisera. In addition, IgG isolated from the antisera inhibited the anti-TMG mAb reaction to the U snRNA. Furthermore, a structural analog, 7-methylguanosine-triphosphate, competitively inhibited the reaction of the antisera to the U snRNA. Thus we concluded that the TMG cap structure of the U snRNA could be a target for serum autoantibodies.

Topics: Autoantibodies; Autoantigens; Binding, Competitive; Guanosine; Humans; Precipitin Tests; RNA Caps; RNA, Small Nuclear; Scleroderma, Systemic

1992