Autoantibodies to the U2 small nuclear ribonucleoprotein in a patient with scleroderma-polymyositis overlap syndrome.

Mimori, Tsuneyo; Hinterberger, M.; Pettersson, Ingvar; Steitz, Joan A.

doi:10.1016/s0021-9258(17)43698-2

Cited by 166 publications

(8 citation statements)

References 45 publications

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“…2 illustrates the results obtained in immunoblotting experiments with the antisera listed in Table II. The Sm monoclonal and the anti-Sm serum react with snRNP polypeptides B/B' and D (lanes 1 and 2) in accordance with previously published results (20,25). The three anti-RNP sera react with different combinations of the U 1-associated snRNP polypeptides: CL with a 68K protein (lane 3), RE with B/B' and faintly with C (lane 4), and AL with A (lane 5) (20,25).…”

Section: Specificity Of the Antiserasupporting

confidence: 91%

“…The Sm monoclonal and the anti-Sm serum react with snRNP polypeptides B/B' and D (lanes 1 and 2) in accordance with previously published results (20,25). The three anti-RNP sera react with different combinations of the U 1-associated snRNP polypeptides: CL with a 68K protein (lane 3), RE with B/B' and faintly with C (lane 4), and AL with A (lane 5) (20,25). The La antiserum (lane 6) identifies a 50K polypeptide (6, 7) which penetrates the nitrocellulose and thus stains more strongly on the backside of the sheet.…”

Section: Specificity Of the Antiserasupporting

confidence: 91%

“…The amount loaded corresponds to 1 × 10 6 cells/mm slot width. After separation, the peptides were transferred to Trans-Blot nitrocellulose sheets (Bio-Rad Laboratories, Richmond, CA) by electroblotting for 2 h at 225 mA in a buffer containing 25 mM Tris, 192 mM gtycine, 0.1% SDS, and 25% methanol (20,36).…”

Section: Deteetion Of Peptide Antigens By Immunoblottingmentioning

confidence: 99%

“…The 68K, A, and C proteins are specific for U 1 RNA-containing particles. At least one U2-specific polypeptide, A', has been found (13,20). Proteins uniquely associated with the other particles have not been reproducibly demonstrated.…”

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confidence: 98%

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Intranuclear localization of snRNP antigens.

Nyman¹,

Hallman²,

Hadlaczky³

et al. 1986

The Journal of Cell Biology

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144

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Abstract.Anti-Sm antibodies recognize a group of small, nuclear RNA-protein complexes (snRNPs) containing U 1, U2, U4, U5, and U6 snRNAs. Anti-RNP antibodies only react with U I snRNA-containing complexes.The intranuclear distribution of snRNP particles was studied by double immunofluorescence staining of human fibroblasts. Mouse monoclonal anti-Sm antibodies and polyclonal patient sera reacting with different peptides in the snRNP complexes were used. The immunofluorescence patterns obtained with fluorescein isothiocyanate-conjugated anti-mouse Ig and tetramethylrhodamine isothiocyanate-conjugated anti-human Ig second antibodies were examined using computer analysis of digitized images. With this approach the similarity of different patterns could be visualized and estimated with mathematical methods. It was found that human anti-Sm serum as well as three different anti-RNP sera produced speckled patterns overlapping with the anti-Sm monoclonal pattern. Thus, Sm antigenic intranuclear domains also reacted with anti-RNP antibodies, suggesting a high degree of co-localization of the antigenic structures. A partial overlap was found between speckles detected by mouse anti-Sm antibodies and a human La-antiserum. No significant co-localization occurred between speckles detected by mouse anti-Sm antibodies and speckles detected by human antisera reacting with Scl-70 and centromeric antigens.As the U 1 snRNP complex is believed to play a role in the splicing of RNA polymerase II transcripts, it appears that the speckles detected by Sm and RNP antibodies may be regions of hnRNA synthesis and m.RNA processing. Although no function has been demonstrated for the U2, U4, U5, and U6 snRNPs, the co-localization with the U 1 RNA complexes shown in this report indicate that they too participate in some aspect of mRNA processing. The results suggest that computer-assisted analysis of nuclear immunofluorescence patterns will be a useful tool in studies of the spatial and functional organization of the interphase nucleus. IMMUNE staining of mammalian cells with autoimmune sera frequently results in a speckled nuclear pattern. The two major specificities that produce speckled patterns are known as Sm and RNP. These autoantibodies occur primarily in systemic lupus erythematosus, mixed connective tissue disease, and less frequently in other autoimmune diseases (3,31,35).The Sm and RNP antigenic structures are thus concentrated in certain nuclear domains. Immunochemical and biochemical studies have elucidated the nature of the antigens (1, 11-13, 16, 18, 20, 25, 33, 34, 37, 38). Sm-antibodies were shown to immunoprecipitate RNA-protein complexes containing a class of small nuclear RNAs designated U l, U2, U4, U5, and U6 snRNAs) RNP-antibodies, on the other hand, immunoprecipitated only U 1 RNA-containing complexes (18). Proteins were required for antigenicity (18). The fact that small, U3 is nucleolar and not precipitated by Sm/RNP antibodies. nuclear RNA-protein complex (snRNP) 2 particles containing only U l RNA can be immunoprecip...

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Section: Specificity Of the Antiserasupporting

confidence: 91%

Section: Specificity Of the Antiserasupporting

confidence: 91%

Section: Deteetion Of Peptide Antigens By Immunoblottingmentioning

confidence: 99%

mentioning

confidence: 98%

See 2 more Smart Citations

Intranuclear localization of snRNP antigens.

Nyman¹,

Hallman²,

Hadlaczky³

et al. 1986

The Journal of Cell Biology

Self Cite

144

View full text Add to dashboard Cite

show abstract

“…Immunoprecipitates of leucine-labeled cell extracts with a U2 specific serum specifically precipitates the ~/and B" U2 specific proteins along with the core snRNP proteins (lane 1, Mimori et al, 1984;Craft et al, 1988). The mobility of the U2-specific protein B # is slightly slower than the B protein.…”

Section: Identification Of U1 and U2 Snrnp-specific Proteinsmentioning

confidence: 99%

Nuclear exchange of the U1 and U2 snRNP-specific proteins.

Feeney

Zieve

1990

The Journal of Cell Biology

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Abstract. The snRNP particles include a set of common core snRNP proteins and snRNP specific proteins. In rodent cells the common core proteins are the B, D, D', E, F and G proteins in a suggested stoichiometry of BzD'2D2EFG. The additional U1-and U2-specific proteins are the 70-kD, A and C proteins and the £ and B" proteins, respectively. Previous cell fractionation and kinetic analysis demonstrated the snRNP core proteins are stored in the cytoplasm in large partially assembled snRNA-free intermediates that assemble with newly synthesized snRNAs during their transient appearance in the cytoplasm (Sauterer, R. A., R. J. Feeney, and G. W. Zieve. 1988. Exp. Cell Res. 176:344-359). This report investigates the assembly and intracellular distribution of the U1 and U2 snRNP-specific proteins. Cell enucleation and aqueous cell fractionation are used to prepare nuclear and cytoplasmic fractions and the U1-and U2-specific proteins are identified by isotopic labeling and immunoprecipitation or by immunoblotting with specific autoimmune antisera. The A, C, and/¢ proteins are found both assembled into mature nuclear snRNP particles and in unassembled pools in the nucleus that exchange with the assembled snRNP particles. The unassembled proteins leak from isolated nuclei prepared by detergent extraction. The unassembled £ protein sediments at 4S-6S in structures that may be multimers. The 70-kD and B" proteins are fully assembled with snRNP particles which do not leak from isolated nuclei. The kinetic studies suggest that the B" protein assembles with the U2 particle in the cytoplasm before it enters the nucleus.

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Whither the ANA?

Lerner¹,

Lerner²

1987

Arch Dermatol

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Autoantibodies to the U2 small nuclear ribonucleoprotein in a patient with scleroderma-polymyositis overlap syndrome.

Cited by 166 publications

References 45 publications

Intranuclear localization of snRNP antigens.

Intranuclear localization of snRNP antigens.

Nuclear exchange of the U1 and U2 snRNP-specific proteins.

Whither the ANA?

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