Tumour cell nuclei display achromasia in smears relative to methylene blue and to other low-affinitive ionic dyes. In the course of the smear air-drying the tumour DNA undergoes conformational changes as evidenced by enhanced ethidium and monomer acridine orange uptake and increased sensitivity to DNAse I hydrolysis. Very mild treatment with bleomycin prevents nuclear achromasia with methylene blue in tumour cells. It is concluded that the phenomenon of nuclear achromasia of tumour cells is due to the properties of secondary structure of their DNA.

Download full-text PDF

Source

Publication Analysis

Top Keywords

phenomenon nuclear
8
methylene blue
8
nuclear achromasia
8
tumour cells
8
[conformational changes
4
changes chromatin
4
chromatin tumor
4
tumor cells
4
cells phenomenon
4
nuclear achromasia]
4

Similar Publications

Introduction: Ulcerative colitis (UC), a form of inflammatory irritable bowel disease, is characterized by a recurrent and persistent nonspecific inflammatory response. Polydatin (PD), a natural stilbenoid polyphenol with potent properties, exhibits unexpected beneficial effects beyond its well-documented anti-inflammatory and antioxidant activities. In this study, we presented evidence that PD confers protection against dextran sodium sulfate (DSS)-induced ulcerative colitis.

View Article and Find Full Text PDF

BrCYP71 mutation resulted in stay-green in pak choi (Brassica rapa L. ssp. chinensis).

Theor Appl Genet

January 2025

College of Horticulture, Shenyang Agricultural University, Shenyang, 110866, People's Republic of China.

BrCYP71 encoding multifunctional oxidase was mapped using BSA-Seq and linkage analysis, and its function in stay-green of pak choi was verified through Arabidopsis heterologous transgenic experiment. Stay-green refers to the phenomenon that plant leaves remain green during senescence and even after death, which is of great significance for improving the commerciality of leafy vegetables during storage or transportation and extending their shelf life. In this study, we identified a stay-green mutant of pak choi and named it nye2.

View Article and Find Full Text PDF

Endothelial TRIM35-Regulated MMP10 Release Exacerbates Calcification of Vascular Grafts.

Adv Sci (Weinh)

January 2025

Clinical Research Center, Postdoctoral Station of Clinical Medicine, The Third Xiangya Hospital, Central South University, Changsha, 410013, P. R. China.

Vascular calcification is a highly regulated process in cardiovascular disease (CVD) and is strongly correlated with morbidity and mortality, especially in the adverse stage of vascular remodeling after coronary artery bypass graft surgery (CABG). However, the pathogenesis of vascular graft calcification, particularly the role of endothelial-smooth muscle cell interaction, is still unclear. To test how ECs interact with SMCs in artery grafts, single-cell analysis of wild-type mice is first performed using an arterial isograft mouse model and found robust cytokine-mediated signaling pathway activation and SMC proliferation, together with upregulated endothelial tripartite motif 35 (TRIM35) expression.

View Article and Find Full Text PDF

Human Immunodeficiency Virus (HIV) proviral reservoirs are cells that harbor integrated HIV proviral DNA within their nuclear genomes. These cells form a heterogeneous group, represented by peripheral blood mononuclear cells (PBMCs), tissue-resident lymphoid and monocytic cells, and glial cells of the central nervous system. The importance of studying the properties of proviral reservoirs is connected with the inaccessibility of integrated HIV proviral DNA for modern anti-retroviral therapies (ARTs) that block virus reproduction.

View Article and Find Full Text PDF

The Dps Protein Protects DNA in the Form of the Trimer.

Int J Mol Sci

January 2025

Winogradsky Institute of Microbiology, Research Center of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.

The Dps protein is the major DNA-binding protein of prokaryotes, which protects DNA during starvation by forming a crystalline complex. The structure of such an intracellular DNA-Dps complex is still unknown. However, the phenomenon of a decrease in the size of the Dps protein from 90 Å to 69-75 Å during the formation of a complex with DNA has been repeatedly observed, and no explanation has been given.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!