We describe the accumulation and distribution of poly (A) RNA during oogenesis and early embryogenesis as revealed by in situ hybridization with a radio-labeled poly (U) probe. The amount of poly (A) RNA in nurse cell cytoplasm continuously increased untill mid-vitellogenic stage (st. 10), then decreased with the rapid increase of poly (A) RNA in the oocyte (st. 11). The localization of poly (A) RNA at stage 10 was in the anterior region of the oocyte, where it is connected by cytoplasmic bridge to the nurse cells. These observations indicate that most of the poly (A) RNA synthesized in the nurse cells is transferred to the oocyte through the cytoplasmic bridges at stage 10-11. During the remainder of oogenesis (st. 11-14) and during preblastodermal embryogenesis, poly (A) RNA was evenly distributed over the cytoplasm of oocytes and embryos. At blastoderm stage, poly(A) RNA became concentrated in the peripheral region of embryos. Though the somatic nuclei of the blastoderm contained a detectable amount of poly (A) RNA, the pole cell nuclei did not. The cytoplasmic RNA visualised by acridine orange staining and the poly (A) RNA detected by hybridization with [ H]poly (U) exhibited identical distributions during oogenesis and early embryogenesis. These observations provide a basis to assess the unique distributions of specific RNA sequences involved in early development.
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http://dx.doi.org/10.1111/j.1440-169X.1988.00251.x | DOI Listing |
J Immunother Cancer
January 2025
Division of Infection, Immunity and Respiratory Medicine, The University of Manchester, Manchester, UK
Background: Programmed cell death 1 (PD-1) signaling blockade by immune checkpoint inhibitors (ICI) effectively restores immune surveillance to treat melanoma. However, chronic interferon-gamma (IFNγ)-induced immune homeostatic responses in melanoma cells contribute to immune evasion and acquired resistance to ICI. Poly ADP ribosyl polymerase 14 (PARP14), an IFNγ-responsive gene product, partially mediates IFNγ-driven resistance.
View Article and Find Full Text PDFPLoS One
January 2025
Department of Pathology, the Second Xiangya Hospital, Central South University, Changsha, Hunan, China.
Background: Ras-GTPase-activating protein (GAP)-binding protein 1 (G3BP1) emerges as a pivotal oncogenic gene across various malignancies, notably including nasopharyngeal carcinoma (NPC). The use of automated image analysis tools for immunohistochemical (IHC) staining of particular proteins is highly beneficial, as it could reduce the burden on pathologists. Interestingly, there have been no prior studies that have examined G3BP1 IHC staining using digital pathology.
View Article and Find Full Text PDFMol Cancer Ther
January 2025
Tango Therapeutics (United States), Boston, United States.
Synthetic lethality approaches in BRCA1/2-mutated cancers have focused on poly(ADP-ribose) polymerase (PARP) inhibitors, which are subject to high rates of innate or acquired resistance in patients. Here, we used CRISPR/Cas9-based screening to identify DNA Ligase I (LIG1) as a novel target for synthetic lethality in BRCA1-mutated cancers. Publicly available data supported LIG1 hyperdependence of BRCA1-mutant cells across a variety of breast and ovarian cancer cell lines.
View Article and Find Full Text PDFInflammation is a complex host response to harmful infections or injuries, playing both beneficial and detrimental roles in tissue regeneration. Notably, clinical dentinogenesis associated with caries development occurs within an inflammatory environment. Reparative dentinogenesis is closely linked to intense inflammation, which triggers the recruitment and differentiation of dental pulp stem cells (DPSCs) into the dentin lineage.
View Article and Find Full Text PDFelements are primate-specific retrotransposon sequences that comprise ∼11% of human genomic DNA. sequences contain an internal RNA polymerase III promoter and the resultant RNA transcripts mobilize by a replicative process termed retrotransposition. retrotransposition requires the Long INterspersed Element-1 (LINE-1) open reading frame 2-encoded protein (ORF2p).
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