scholarly journals Bcr-abl translocation can occur during the induction of multidrug resistance and confers apoptosis resistance on myeloid leukemic cell lines

1997 ◽  
Vol 4 (8) ◽  
pp. 806-814 ◽  
Author(s):  
Francis Belloc ◽  
Sophie Cotteret ◽  
Gilles Labroille ◽  
Valérie Schmit ◽  
Claudine Jaloustre ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Cell Lines ◽  
Leukemic Cell ◽  
Apoptosis Resistance ◽  
Leukemic Cell Lines ◽  
Myeloid Leukemic Cell

DIGE-Based Proteomic Analysis Identifies NPM/B23 and Nucleolin C23 as Overexpressed Proteins In Relapsed /Refractory Acute Leukemia

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 1711-1711
Author(s):  
Jian Da Hu ◽  
MinHui Lin ◽  
TingBo Liu ◽  
Jing Li ◽  
XinJi Chen ◽  
...  
Keyword(s):  
Treatment Outcome ◽  
Multidrug Resistance ◽  
Acute Leukemia ◽  
Western Blot ◽  
Cell Lines ◽  
Molecular Mechanisms ◽  
Expression Profiles ◽  
Leukemia Cell ◽  
Leukemic Cell ◽  
Leukemic Cell Lines

Abstract Abstract 1711 Resistance to chemotherapy is a challenge in treatment of acute leukemia. Although the classic multidrug resistance (MDR) phenotype is often characterized by expression of drug efflux pump P-glycoprotein or by multidrug resistance-associated proteins, precise molecular mechanisms are largely unknown. To investigate novel protein changes involved in resistance mechanism, protein expression profiles between human myeloid leukemia HL-60 cell lines and adriamycin- resistant HL-60 cell lines (HL-60/ADR) was compared, which was based on a differential proteomic approach — 2 dimensional difference in gel Electrophoresis(2D-DIGE) followed by mass spectrometry (MALDI-TOF-MS) and complemented by western blot validation. 16 protein spots were identified as being differentially expressed (> 1.2 fold change and p≤ 0.05) between above two cell lines, among which 13 protein spots were identified as up-regulated and 3 as down-regulated in the HL-60/ ADR cell line. Proteins found to have higher abundance levels in the resistant HL-60/ADR cells included enzymes, proteins and oncogenes related to signal transduction, protein synthesis, cell growth regulation and metabolism. 3 lower abundance proteins are related to transcription. From 16 proteins, 2 proteins, nucleophosmin B23 (NPM B23)and nucleolin C23, were selected and verified in leukemia cell lines and primary leukemia samples by western blot. Compared to healthy control samples, which showed no expressions of these 2 proteins, leukemic cell lines revealed an obvious up-regulation of B23 and C23. Moreover, significantly higher expressions of B23 and C23 were found in 3 resistant leukemic cell lines, HL-60/ADR, K562/ADR and KG01 cells, compared to the parent HL-60 and K562 cells, and other leukemic cell lines. In de novo leukemia samples, 43.8%(35/80) expressed B23 and C23 proteins, 37.9% (22/58) AML and 59.1% (13/22) ALL respectively. Meanwhile, concomitant expression of B23 and C23, both positive or negative, was noted in 97%(79/80)patients. Over-expressions of B23 and C23 were observed in 68.8% relapased/refractory leukemia patients. With regard to treatment outcome,among those patients who achieved ongoing CR, fewer patients expressed 2 proteins, only 13.35% (7/52) AML and 46%(7/15) ALL respectively. It implicated that B23 and C23 may be involved in drug resistance and be useful in assessing treatment outcome and prognosis of leukemia. To a conclusion, these results provide a novel clue for the molecular mechanism of MDR and suggest that B23 and C23 are prognostic indicators for leukemia. Disclosures: No relevant conflicts of interest to declare.

Selective Induction of Apoptosis in Myeloid Leukemic Cell Lines by Monoacetone Glucose-3 Butyrate

1994 ◽  
Vol 201 (1) ◽  
pp. 266-283 ◽  
Author(s):  
C. Calabresse ◽  
L. Venturini ◽  
G. Ronco ◽  
P. Villa ◽  
L. Degos ◽  
...  
Keyword(s):  
Cell Lines ◽  
Leukemic Cell ◽  
Leukemic Cell Lines ◽  
Induction Of Apoptosis ◽  
Myeloid Leukemic Cell

scholarly journals Expression of integrins and examination of their adhesive function in normal and leukemic hematopoietic cells

Blood ◽  
1993 ◽  
Vol 81 (1) ◽  
pp. 112-121 ◽  
Author(s):  
JL Liesveld ◽  
JM Winslow ◽  
KE Frediani ◽  
DH Ryan ◽  
CN Abboud
Keyword(s):  
Progenitor Cells ◽  
Cell Lines ◽  
Leukemic Cell ◽  
Binding Assays ◽  
Leukemic Cell Lines ◽  
Late Antigen ◽  
Acute Myelogenous ◽  
Acute Myelomonocytic Leukemia ◽  
Myeloid Leukemic Cell ◽  
Glycosylphosphatidyl Inositol

Adhesion of hematopoietic progenitor cells to marrow-derived adherent cells has been noted for erythroid, myeloid, and lymphoid precursors. In this report, we have characterized very late antigen (VLA) integrin expression on normal CD34+ marrow progenitors, on leukemic cell lines, and on blasts from patients with acute myelogenous or monocytic leukemias. CD34+ progenitor cells expressed the integrin beta 1 chain (CD29), VLA-4 alpha (CD49d), and VLA-5 alpha (CD49e). The myeloid lines KG1 and KG1a also expressed CD49d and CD49e as did the Mo7e megakaryoblastic line. CD29, CD18, and CD11a were also present on each of these cell lines. Only the Mo7e line expressed the cytoadhesins GPIIbIIIa or GPIb. Binding of KG1a to marrow stroma was partially inhibited by antibodies to CD49d and its ligand, vascular cell adhesion molecule (VCAM-1). The majority of leukemic blasts studied expressed CD49d and CD49e as well. Blasts from patients with acute myelomonocytic leukemia consistently bound to stroma at levels greater than 20%, and adhesion to stroma could in some cases be partly inhibited by anti- CD49d. No role for glycosylphosphatidyl-inositol (GPI)-linked structures was demonstrated in these binding assays because the adhesion of leukemic blasts to stroma was not diminished after treatment with phosphatidylinositol-specific phospholipase C (PI-PLC). These studies indicate that CD34+ myeloid progenitors, myeloid leukemic cell lines, and leukemic blasts possess a similar array of VLA integrins. Their functional importance individually or in combination with other mediators of attachment in adhesion, transendothelial migration, and differentiation has yet to be fully elucidated.

scholarly journals Dissociation of c-fos induction from macrophage differentiation in human myeloid leukemic cell lines.

1987 ◽  
Vol 7 (2) ◽  
pp. 769-774 ◽  
Author(s):  
B Calabretta
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Lines ◽  
Mrna Level ◽  
Leukemic Cell ◽  
Synthetic Analog ◽  
Macrophage Differentiation ◽  
Leukemic Cell Lines ◽  
Kinase C ◽  
Myeloid Leukemic Cell

Treatment of five human myeloid leukemic cell lines (KG1, ML3, HL-60, U-937, and HEL) with TPA was followed by macrophage differentiation and was accompanied by an early and transient increase in the mRNA level of c-fos proto-oncogene. The induction of c-fos was also observed in human cell lines K562 and K-Gla that did not respond to TPA with terminal macrophage differentiation. The treatment of HL-60 and U-937 cell lines with 1-oleoyl-2-acetylglycerol, a synthetic analog of diacylglycerol that, like TPA, stimulates protein kinase C activity, was followed by early and transient induction of c-fos mRNA in the absence of terminal macrophage differentiation. Finally, treatment of HL-60 with TPA in the presence of retinal, an inhibitor of protein kinase C, drastically reduced the induction of c-fos mRNA but had no effect on the terminal macrophage differentiation that is induced in this cell line by TPA. These results indicate that the induction of c-fos and terminal macrophage differentiation in response to TPA treatment can be dissociated in the in vitro models provided by human myeloid leukemic cell lines. Moreover, these findings suggest that the induction of c-fos is not only insufficient but may also be unnecessary for the differentiation along the monocyte-macrophage pathway.

Acute myeloid leukemic cell lines loaded with synthetic dsRNA trigger IFN-γ secretion by human NK cells

2009 ◽  
Vol 33 (4) ◽  
pp. 539-546 ◽  
Author(s):  
Eva Lion ◽  
Evelien L.J.M. Smits ◽  
Zwi N. Berneman ◽  
Viggo F.I. Van Tendeloo
Keyword(s):  
Nk Cells ◽  
Cell Lines ◽  
Leukemic Cell ◽  
Leukemic Cell Lines ◽  
Ifn Γ ◽  
Myeloid Leukemic Cell ◽  
Acute Myeloid
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