scholarly journals Induction of programmed cell death in human hematopoietic cell lines by fibronectin via its interaction with very late antigen 5.

1994 ◽  
Vol 179 (6) ◽  
pp. 1757-1766 ◽  
Author(s):  
H Sugahara ◽  
Y Kanakura ◽  
T Furitsu ◽  
K Ishihara ◽  
K Oritani ◽  
...  

Extracellular matrix (ECM) molecules such as fibronectin (FN), collagens, and laminin have important roles in hematopoiesis. However, little is known about the precise mechanisms by which ECM molecules regulate proliferation of human hematopoietic progenitor cells. In this study, we have investigated the effects of ECM molecules, particularly of FN, on the proliferation of a myeloid leukemia cell line, M07E, which proliferates in response to either human granulocyte/macrophage colony-stimulating factor (GM-CSF) or stem cell factor (SCF). The [3H]thymidine incorporation and cell enumeration assays showed that FN strikingly inhibited GM-CSF- or SCF-induced proliferation of M07E cells in a dose-dependent manner, whereas little or no inhibition was induced by collagen types I and IV. The growth suppression of M07E cells was not due to the inhibitory effect of FN on ligand binding or very early events in the signal transduction pathways from the GM-CSF or SCF receptors. DNA content analysis using flow cytometry after staining with propidium iodide revealed that the treatment of M07E cells with FN did not block the entry of the cells into the cell cycle after stimulation with GM-CSF or SCF, whereas the treatment resulted in the appearance of subdiploid peak. Furthermore, FN was found to induce oligonucleosomal DNA fragmentation and chromatin condensation in the cells even in the presence of GM-CSF or SCF, suggesting the involvement of programmed cell death (apoptosis) in the FN-induced growth suppression. The growth suppression or apoptosis induced by FN was rescued by the addition of either anti-FN antibody, anti-very late antigen 5 monoclonal antibody (anti-VLA5 mAb), or GRGDSP peptide, but not by that of anti-VLA4 mAb or GRGESP peptide, suggesting that the FN effects on M07E cells were mediated through VLA5. In addition, the FN-induced apoptosis was detectable in VLA5-positive human hematopoietic cell lines other than M07E cells, but not in any of the VLA5-negative cell lines. These results suggest that FN is capable of inducing apoptosis via its interaction with VLA5, and also raise the possibility that the FN-VLA5 interaction may contribute, at least in part, to negative regulation of hematopoiesis.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2476-2476 ◽  
Author(s):  
Mwe Mwe Chao ◽  
David A. Erichsen ◽  
Megan L. Krajewski ◽  
Stefan K. Bohlander ◽  
Daniel S. Wechsler

Abstract Background: Clathrin Assembly Lymphoid Myeloid leukemia (CALM) gene rearrangements occur in a subset of aggressive leukemias and lymphomas, in which CALM is fused to the MLL or AF10 genes. Previous studies have shown that expression of MLL-CALM or CALM-AF10 fusion proteins immortalizes murine hematopoietic progenitor cells, an observation that often correlates with leukemogenesis in vivo. While disruption of MLL or AF10 activity contributes to malignant transformation, perturbation of normal CALM function may also play a role. Indeed, the identification of significant hematologic abnormalities in fit1 mice that harbor calm mutations suggests a role for CALM in normal hematopoiesis. The native CALM protein is primarily cytoplasmic and functions in Clathrin-Dependent Endocytosis (CDE). We have demonstrated that expression of native CALM or a CALM C-terminal domain in COS7 cells impairs endocytosis of both Transferrin and Epidermal Growth Factor (EGF). Since cell surface growth factor (GF) signaling may be downregulated by receptor internalization via CDE, we hypothesize that disruption of CDE by CALM-containing fusion proteins interferes with attenuation of GF signaling in hematopoietic cells; this results in sustained proliferation that contributes to leukemogenesis. Objectives: 1) To demonstrate that expression of CALM fusion proteins interferes with the endocytosis of hematopoietic GF; 2) To analyze the time course of phosphorylation of Janus kinases (JAK), downstream targets of GF signaling; 3) To determine whether cells expressing CALM-containing fusion proteins have a survival advantage. Methods: COS7 cells transfected with CALM-containing constructs, and hematopoietic cell lines that natively harbor CALM-AF10 translocations (U937, P31/Fuji) were incubated with 125I-EGF or 125I-GM-CSF, respectively, and the amount of internalized radioactivity was measured. To measure the functional significance of impaired endocytosis, the pattern of JAK phosphorylation in these cells was analyzed by Western blot. The 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay was employed to measure cell proliferation rates. Results: Expression of CALM fusion proteins in COS7 cells was associated with a 40–50% reduction in the rate of EGF endocytosis when compared to control cells. Hematopoietic cell lines that natively harbor CALM-AF10 translocations (U937, P31/Fuji) exhibited reduced rates of GM-CSF endocytosis in comparison with hematopoietic cells lacking such translocations (HL60, K562). EGF treatment of CALM fusion-expressing COS7 cells resulted in increased and prolonged JAK1 phosphorylation. JAK2 phosphorylation was similarly affected in GM-CSF-treated hematopoietic cell lines that natively express CALM-AF10 fusion proteins. Finally, expression of MLL-CALM or CALM-AF10 proteins in COS7 cells was associated with a reduced serum requirement in vitro, showing increased proliferation in low serum relative to controls. Conclusion: We have demonstrated that CALM-dependent perturbation of endocytosis in hematopoietic cells is associated with increased GF signaling, as well as a proliferative advantage in low serum. These observations argue for a crucial and previously unappreciated role for CDE dysregulation in leukemogenic transformation.


2015 ◽  
Vol 39 (1) ◽  
pp. 18-29 ◽  
Author(s):  
Hans G. Drexler ◽  
Stefan Ehrentraut ◽  
Stefan Nagel ◽  
Sonja Eberth ◽  
Roderick A.F. MacLeod

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1740-1748 ◽  
Author(s):  
G Klein ◽  
CA Muller ◽  
E Tillet ◽  
ML Chu ◽  
R Timpl

Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within the molecule seems to be restricted to the triple helical domain of all three alpha (VI) chains, because individual alpha (VI) chains were not active in the attachment assays. Adhesion of the hematopoietic cell lines to collagen VI was dose-dependent and could be inhibited by heparin. Although the triple helix contains several RGD sequences, adhesion of the hematopoietic cell types to collagen VI could be blocked neither by RGD-containing peptides nor by a neutralizing antibody to the beta 1 integrin subunit. In combination with an antiadhesive substrate, the binding properties of collagen VI could be downregulated. These data suggest that this collagen type may play an important role in the adhesion of hematopoietic cells within the BM microenvironment.


PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e43696 ◽  
Author(s):  
Colin Correnti ◽  
Vera Richardson ◽  
Allyson K. Sia ◽  
Ashok D. Bandaranayake ◽  
Mario Ruiz ◽  
...  

1989 ◽  
Vol 86 (21) ◽  
pp. 8536-8540 ◽  
Author(s):  
W. F. Shen ◽  
C. Largman ◽  
P. Lowney ◽  
J. C. Corral ◽  
K. Detmer ◽  
...  

1997 ◽  
Vol 23 (3) ◽  
pp. 422-433 ◽  
Author(s):  
Denise E. Sabatino ◽  
Bao-Khanh Q. Do ◽  
Louise C. Pyle ◽  
Nancy E. Seidel ◽  
Laurie J. Girard ◽  
...  

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