Human leukemic cells: Cytochemical studies on nuclear proteins

Chromosoma ◽  
1972 ◽  
Vol 38 (3) ◽  
pp. 329-340 ◽  
Author(s):  
L. S. Desai ◽  
L. E. De Bault ◽  
G. Morrissey ◽  
G. E. Foley
Keyword(s):  
Nuclear Proteins ◽  
Leukemic Cells ◽  
Human Leukemic Cells

scholarly journals HUMAN LEUKEMIC CELLS CYTOCHEMICAL STUDIES ON ACIDIC NUCLEAR PROTEINS

1974 ◽  
Vol 22 (1) ◽  
pp. 40-45 ◽  
Author(s):  
L. S. DESAI ◽  
G. E. FOLEY
Keyword(s):  
Toluidine Blue ◽  
Diagnostic Category ◽  
Distribution Patterns ◽  
Dry Mass ◽  
Nuclear Proteins ◽  
Leukemic Cells ◽  
Control Mechanisms ◽  
Acidic Proteins ◽  
Human Leukemic Cells ◽  
Individual Human

Utilizing staining with alkaline fast green (pH 8.1) and toluidine blue O (pH 9.0) stains, the nuclear basic and acidic protein content of individual human lymphocytic cells has been quantitated cytochemically with high resolution, rapid scanning instruments. There were distinct differences in the distribution patterns of the acidic and basic proteins in these human lymphocytic cells. Nucleoli were densely stained by toluidine blue O, confirming the presence of acidic proteins. The acidic nuclear proteins:DNA and basic nuclear proteins:DNA ratios are consistent and quantitatively similar, irrespective of the diagnostic category from which the cells derived and there was a definite correlation between nuclear proteins and DNA content. However, the acidic nuclear proteins represented a larger proportion of the total dry mass of the cell than did the basic nuclear proteins, an observation which may prove to be of interest with respect to control mechanisms.

A novel mechanism for imatinib mesylate–induced cell death of BCR-ABL–positive human leukemic cells: caspase-independent, necrosis-like programmed cell death mediated by serine protease activity

Blood ◽  
2004 ◽  
Vol 103 (6) ◽  
pp. 2299-2307 ◽  
Author(s):  
Masayuki Okada ◽  
Souichi Adachi ◽  
Tsuyoshi Imai ◽  
Ken-ichiro Watanabe ◽  
Shin-ya Toyokuni ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Serine Protease ◽  
Imatinib Mesylate ◽  
Protease Activity ◽  
Kinase Inhibitor ◽  
Leukemic Cells ◽  
Endonuclease G ◽  
Serine Protease Activity ◽  
Human Leukemic Cells

Abstract Caspase-independent programmed cell death can exhibit either an apoptosis-like or a necrosis-like morphology. The ABL kinase inhibitor, imatinib mesylate, has been reported to induce apoptosis of BCR-ABL–positive cells in a caspase-dependent fashion. We investigated whether caspases alone were the mediators of imatinib mesylate–induced cell death. In contrast to previous reports, we found that a broad caspase inhibitor, zVAD-fmk, failed to prevent the death of imatinib mesylate–treated BCR-ABL–positive human leukemic cells. Moreover, zVAD-fmk–preincubated, imatinib mesylate–treated cells exhibited a necrosis-like morphology characterized by cellular pyknosis, cytoplasmic vacuolization, and the absence of nuclear signs of apoptosis. These cells manifested a loss of the mitochondrial transmembrane potential, indicating the mitochondrial involvement in this caspase-independent necrosis. We excluded the participation of several mitochondrial factors possibly involved in caspase-independent cell death such as apoptosis-inducing factor, endonuclease G, and reactive oxygen species. However, we observed the mitochondrial release of the serine protease Omi/HtrA2 into the cytosol of the cells treated with imatinib mesylate or zVAD-fmk plus imatinib mesylate. Furthermore, serine protease inhibitors prevented the caspase-independent necrosis. Taken together, our results suggest that imatinib mesylate induces a caspase-independent, necrosis-like programmed cell death mediated by the serine protease activity of Omi/HtrA2.

The impact of lithium on human leukemic cells

1991 ◽  
Vol 15 (8) ◽  
pp. 766 ◽  
Author(s):  
Ronald D. Barr ◽  
Delsworth Harnish
Keyword(s):  
Leukemic Cells ◽  
Human Leukemic Cells ◽  
The Impact

Altered catalytic activity of and DNA cleavage by DNA topoisomerase II from human leukemic cells selected for resistance to VM-26

Biochemistry ◽  
1988 ◽  
Vol 27 (24) ◽  
pp. 8861-8869 ◽  
Author(s):  
Mary K. Danks ◽  
Carla A. Schmidt ◽  
Margaret C. Cirtain ◽  
D. Parker Suttle ◽  
William T. Beck
Keyword(s):  
Catalytic Activity ◽  
Dna Cleavage ◽  
Topoisomerase Ii ◽  
Leukemic Cells ◽  
Dna Topoisomerase Ii ◽  
Dna Topoisomerase ◽  
Human Leukemic Cells

Immunological Markers of Human Leukemic Cells of the B Lineage

1983 ◽  
pp. 29-43
Author(s):  
M. Seligmann ◽  
L. B. Vogler ◽  
P. Guglielmi ◽  
J. C. Brouet ◽  
J. L. Preud’homme
Keyword(s):  
Leukemic Cells ◽  
Immunological Markers ◽  
B Lineage ◽  
Human Leukemic Cells

Effect of 4-hydroxynonenal on gene expression and differentiation of HL-60 human leukemic cells

1991 ◽  
Vol 27 ◽  
pp. S65 ◽  
Author(s):  
G. Barrera ◽  
R. Muraca ◽  
C. Di Mauro ◽  
V.M. Fazio ◽  
M.U. Dianzani
Keyword(s):  
Gene Expression ◽  
Leukemic Cells ◽  
Human Leukemic Cells

scholarly journals SALL4 is a key regulator of survival and apoptosis in human leukemic cells

Blood ◽  
2008 ◽  
Vol 112 (3) ◽  
pp. 805-813 ◽  
Author(s):  
Jianchang Yang ◽  
Li Chai ◽  
Chong Gao ◽  
Taylor C. Fowles ◽  
Zaida Alipio ◽  
...  
Keyword(s):  
Stem Cell ◽  
Leukemia Cell ◽  
Annexin V ◽  
Leukemic Cell ◽  
Leukemic Cells ◽  
Immunodeficient Mice ◽  
Leukemia Cell Lines ◽  
Human Leukemic Cells ◽  
Cell Phenotypes ◽  
Proliferation Assays

Abstract Increasing studies suggest that SALL4 may play vital roles in leukemogenesis and stem cell phenotypes. We have mapped the global gene targets of SALL4 using chromatin immunoprecipitation followed by microarray hybridization and identified more than 2000 high-confidence, SALL4-binding genes in the human acute promyelocytic leukemic cell line, NB4. Analysis of SALL4-binding sites reveals that genes involved in cell death, cancer, DNA replication/repair, and cell cycle were highly enriched (P < .05). These genes include 38 important apoptosis-inducing genes (TNF, TP53, PTEN, CARD9, CARD11, CYCS, LTA) and apoptosis-inhibiting genes (Bmi-1, BCL2, XIAP, DAD1, TEGT). Real-time polymerase chain reaction has shown that expression levels of these genes changed significantly after SALL4 knockdown, which ubiquitously led to cell apoptosis. Flow cytometry revealed that reduction of SALL4 expression in NB4 and other leukemia cell lines dramatically increased caspase-3, annexin V, and DNA fragmentation activity. Bromodeoxyuridine-incorporation assays showed decreased numbers of S-phase cells and increased numbers of G1- and G2-phase cells indicating reduced DNA synthesis, consistent with results from cell proliferation assays. In addition, NB4 cells that express low levels of SALL4 have significantly decreased tumorigenecity in immunodeficient mice. Our studies provide a foundation in the development of leukemia stem cell–specific therapy by targeting SALL4.

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