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D L Spector

Publications and source records attributed to D L Spector.

58 records · Page 4Linked to original sources

Colocalization of U1 and U2 small nuclear RNPs by immunocytochemistry.

The in situ localization of U1 and U2 snRNPs was examined, using autoantibodies directed against each of these snRNPs, by immunofluorescence and immunoelectron microscopy. This study has shown U1 and U2 snRNPs to colocalize in the nuclei of PtK2 cells. Thirty to fifty immunostained clusters were observed per interphase nucleus. This study suggests these nuclear protein clusters to be the sites of RNA processing.

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Immunoelectron microscopic localization of snRNPs.

Small nuclear ribonucleoprotein particles (snRNPs) were identified in nuclear sonicates of Novikoff hepatoma ascites cells and in intact Novikoff hepatoma and PtK2 cells by immunofluorescence and immunoelectron microscopy. Auto-antibodies (anti-Sm and anti-RNP) obtained from patients with systemic lupus erythematosus an autoimmune disease, were used to localize snRNP particles. The Sm antibody is specific for U1, U2, U4, U5 and U6 containing snRNPs. The RNP antibody is specific for only U1 containing snRNPs. Isolated particles, 120 +/- 10 A in diameter, were found to be associated with ferritin-conjugated goat anti-human antibodies coupled to Sm antibodies. In addition, these particles (snRNPs) were occasionally associated with larger particles measuring 230 +/- 10 A in diameter which are presumed to be hnRNP particles. Double label immunofluorescence and immunoelectron microscopy have shown Sm and RNP antibodies to colocalize in PtK2 cells. However, the perinucleolar chromatin and juxtanuclear envelope chromatin was devoid of RNP immunostaining. Therefore, U1 containing snRNPs do not appear to be in these regions. The Sm antibody localizes in a nuclear network including the perinucleolar chromatin and juxtanuclear envelope chromatin. Cells treated with the drug DRB (5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole), which inhibits hnRNA synthesis, show an altered pattern of Sm immunostaining. Such cells contain large clusters of snRNPs which do not extend to the perinucleolar chromatin or perinuclear lamina chromatin. Nuclear matrix preparations maintain an snRNP nuclear network as visualized by Sm immunofluorescence. It is notable that the size and density of the immunostained particles in the nuclear network during interphase, is similar to that of interchromatinic granules.

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Chromosome structure and mitosis in the dinoflagellates: an ultrastructural approach to an evolutionary problem.

Chromosome structure and mitosis have been examined in three evolutionarily diverse members of the Pyrrophyta. Chromosome uncoiling, revealing the chromonema, has been correlated with the uptake of [3H]thymidine. In addition, chromosome uncoiling has been observed during gamete formation, gamete fusion, and in the nucleolar organizing region of the chromosomes suggesting that dinoflagellate chromosomes undergoing duplication, transcription or pairing have a morphology different from the characteristic tightly banded structure generally observed during most of interphase and mitosis. The dinoflagellate chromonema is composed of 2.5-nm fibers and 9.0-nm granules coiled into a helix around a central core of 9.0-nm fibers. Chromosome attachment to nuclear channels and kinetochore division and separation have been examined in several dinoflagellates. After evaluating many nuclear and cytoplasmic characteristics of the dinoflagellates it appears that this group of organisms are true eukaryotes which may be on the main line to the evolution of the mitotic spindle typical of higher plant and animals cells.U

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