Identification of an antigenic protein recognized by anti-Sm autoantibody

Schrier, Wayne H.; Reddy, Ram; Busch, Harris

doi:10.1016/0309-1651(82)90003-0

Cited by 10 publications

(3 citation statements)

References 11 publications

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“…Anti-Sm autoantibody (Schrier et al, 1982) was used at a dilution of 1:300 and anti-SC-35 monoclonal antibody (Fu and Maniatis, 1990) was used at a dilution of 1:50. For heat shock experiments Petri dishes containing coverslips and pre-warmed medium (45°C) were floated on a 45°C water bath for 15 min prior to fixation for immunofluorescence microscopy.…”

Section: Cell Culturementioning

confidence: 99%

“…Cells were prepared for immunofluorescence microscopy according to previously published procedures . Anti-Sm autoantibody (Schrier et al, 1982) was used at a dilution of 1:300 and anti-SC-35 monoclonal antibody (Fu and Maniatis, 1990) was used at a dilution of 1:50. Fluorescein isothiocyanate (FITC) conjugated goat anti-human IgG and Texas Red conjugated goat anti-mouse IgG (Cappel Laboratories) were used at a dilution of 1:30 for 1 h at 20°C.…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

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Associations between distinct pre-mRNA splicing components and the cell nucleus.

1991

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SC‐35 is a non‐snRNP spliceosome component that is specifically recognized by the anti‐spliceosome monoclonal antibody alpha SC‐35. In this paper we provide direct evidence that SC‐35 is an essential splicing factor and we examine the immunolocalization of SC‐35 by confocal laser scanning microscopy and by electron microscopy. We have found that the speckled staining pattern observed by fluorescence microscopy corresponds to structures previously designated as interchromatin granules and perichromatin fibrils. Although snRNP antigens are also concentrated in these nuclear regions, we show that the two types of spliceosome components are localized through different molecular interactions: The distribution of SC‐35 was not affected by treatment with DNase I or RNase A, or when the cells were heat shocked. In contrast, snRNP antigens become diffusely distributed after RNase A digestion or heat shock. Examination of cells at different stages of mitosis revealed that the SC‐35 speckled staining pattern is lost during prophase and speckles containing SC‐35 begin to reform in the cytoplasm of anaphase cells. In contrast, snRNP antigens do not associate with speckled regions until late in telophase. These studies reveal a dynamic pattern of assembly and disassembly of the splicing factor SC‐35 into discrete nuclear structures that colocalize with interchromatin granules and perichromatin fibrils. These subnuclear regions may therefore be nuclear organelles involved in the assembly of spliceosomes, or splicing itself.

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Section: Cell Culturementioning

confidence: 99%

Section: Immunofluorescence Microscopymentioning

confidence: 99%

Associations between distinct pre-mRNA splicing components and the cell nucleus.

1991

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“…Naked U1 RNA has been antibodies ( Fig. 4b) (White and Hoch, 1981;Schrier et shown to inhibit cell-free protein synthesis (Rao et al, al., 1982). We do not know why some of the U2 RNA did 1977).…”

Section: Presence Of U1 Rna In Ribonucleoprotein Particle Form In Submentioning

confidence: 99%

Associations of small nuclear RNAs in human cells

Smith

Eliceiri

1983

Journal Cellular Physiology

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Several observations have been made about the associations of small nuclear RNAs (snRNAs) in human cells. When nuclear RNA was extracted with phenol and chloroform under standard nondenaturing conditions, the proportion of the nuclear snRNA content that cosedimented with high molecular weight RNA was very low. These results do not support the proposal that it is a large percentage of the cellular snRNA content that is involved in relatively stable base-paired interactions with heterogeneous nuclear RNA at any given time. The various small nuclear ribonucleoprotein particles (snRNPs), in which the snRNAs are found in the cell, appear to differ substantially in their sedimentation rates under conditions of physiological ionic strength. Using anti-RNP and anti-Sm antibodies to analyze various subcellular fractions, we found that most, if not all, of the U1 snRNA cellular content is associated with the polypeptide(s) bearing the RNP determinant (in interphase and mitotic cells) and with the polypeptide(s) carrying the Sm determinant (in mitotic cells).

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snRNP Proteins

Lührmann

1988

Structure and Function of Major and Minor Small Nuclear Ribonucleoprotein Particles

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Identification of an antigenic protein recognized by anti-Sm autoantibody

Cited by 10 publications

References 11 publications

Associations between distinct pre-mRNA splicing components and the cell nucleus.

Associations between distinct pre-mRNA splicing components and the cell nucleus.

Associations of small nuclear RNAs in human cells

snRNP Proteins

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