PubMed · 4051978
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G Windus, R Urban, H D Tröger. 1985. [Postmortem cell morphology changes in the spleen].. https://pubmed.ncbi.nlm.nih.gov/4051978/
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In this issue of Cell Genomics, McKeever et al.1 generate a single-nucleus transcriptomic atlas of ALS/FTLD brain and reveal widespread alternative polyadenylation changes. Their findings highlight 3' end RNA processing as a central integrator of stress responses, cell-type specificity, and disease susceptibility, offering new mechanistic insight and potential therapeutic directions.
OBJECTIVE: To prepare DNA probe which can be used to accurately detect chromosome 21 copy number in human interphase nuclei by fluorescence in situ hybridization (FISH). METHODS: A probe was produced by universal primer PCR from YAC clone 881D2 and characterized by FISH to metaphases and interphase nuclei of peripheral lymphocytes from 8 normal individuals and 5 patients suffering from trisomy 21. RESULTS: A DNA probe was produced and its characteristics were :(1) Most of the probes ranged in size from 350bp to 750bp; (2) The hybridization signals of the probes were located near centromere on long arm of human chromosome 21; (3) In 1524 metaphases scored, about 99.95% of hybridization signals were located on chromosome 21; (4) The signals were very bright and recognizable easily in both metaphases and interphases nuclei; (5) The expected copy number of chromosome 21 was detected by FISH with the probe in more than 98.40% of interphase nuclei and 99.60% of metaphases. CONCLUSION: The DNA probe reported here is suitable for the detection of chromosome 21 copy number in interphase nuclei and for the study of segregation of chromosome 21 during mitoses of human lymphocytes in culture.
RNA polymerase II transcripts are complexed with heterogeneous nuclear ribonucleoprotein (hnRNP) proteins. These proteins are involved in several aspects of the maturation and transport of hnRNA. We performed a detailed study of the spatial distribution of four hnRNP proteins (hnRNP C, I, L, and U) in HeLa nuclei, using immunofluorescent labeling and confocal microscopy. Despite the fact that hnRNP proteins have been shown to coimmunoprecipitate, a hallmark of hnRNP proteins, we find that hnRNP C, I, and L have a spatial nuclear distribution that is not related to that of hnRNP U. We also examined the distribution of hnRNP proteins in relation to that of nascent transcripts. The four hnRNP proteins that we examined are not enriched at sites of RNA synthesis. Using antibodies against the nuclear poly(A)-binding protein (PAB II) we investigated the relationship between the distribution of hnRNP proteins and that of nuclear domains (nuclear speckles) that are enriched in splicing factors, poly(A)+RNA, and PAB II. We found that the four hnRNP proteins are not enriched in these domains. This indicates that the poly(A)+RNA, present in high concentration in speckles, is not complexed with these hnRNP proteins. This is in agreement with the notion that poly(A)+RNA in speckles is different from ordinary hnRNA. Previously, we have shown that hnRNP proteins are the major protein components of the fibrogranular internal nuclear matrix (K. A. Mattern et al. (1996) J. Cell. Biochem. 62, 275-289; K. A. Mattern et al. (1997) J. Cell. Biochem. 65, 42-52). We observed that in nuclear matrices the spatial distributions of the four hnRNP proteins, like that of nascent RNA and PAB II, are essentially the same as observed in intact nuclei. Moreover, also in nuclear matrix preparations, like in intact nuclei, nascent RNA and PAB II have spatial distributions that differ from those of hnRNP proteins. Our results are compatible with the notion that hnRNP proteins are able to form complexes of many different, probably overlapping, compositions.