heparitin-sulfate and Leukemia

heparitin-sulfate has been researched along with Leukemia* in 4 studies

Other Studies

4 other study(ies) available for heparitin-sulfate and Leukemia

ArticleYear
Human leukemia cell lines bind basic fibroblast growth factor (FGF) on FGF receptors and heparan sulfates: downmodulation of FGF receptors by phorbol ester.
    Blood, 1996, Jan-01, Volume: 87, Issue:1

    Basic fibroblast growth factor (bFGF) has been identified as an important cytokine for blood cells. To determine whether hematopoietic cells have receptors that recognize bFGF, the ability of human leukemia cell lines to bind 125I-bFGF was investigated. Specific bFGF-binding sites were identified on K562 and HL60 cells, but not on U937 cells. DAMI cells bound low amounts of 125I-bFGF specifically. Binding of 125I-bFGF to K562 cell surfaces was reduced in a dose-dependent manner by unlabeled bFGF or by heparin. Scatchard analysis of binding to K562 cells revealed two classes of binding sites: 1,650 high affinity binding sites per cell with a dissociation constant (kd) of 192 pmol/L, and 36,600 low affinity sites per cell with a kd of 9.3 nmol/L. Chemical crosslinking experiments with K562, HL60, and DAMI cells revealed receptor-growth factor complexes with molecular masses of 140 to 160 kD, similar in size to complexes formed by known receptor species. Binding of 125I-bFGF to K562 cells was sensitive to heparinase treatment but not to chondroitinase treatment, suggesting that heparan sulfate proteoglycans (HSPGs) may be responsible for the low affinity binding sites. To further investigate whether K562 cells make HSPG, the incorporation of 35SO4 into proteoglycans was assessed. Metabolically labeled cell-surface proteoglycans with molecular masses of 180 to 300 kD were identified in K562 cells. These proteoglycans were sensitive to heparinase, demonstrating that K562 cells synthesize bFGF-binding HSPG. Treatment of K562 cells with phorbol-12-myristate-13-acetate (PMA) caused a loss of bFGF-binding capacity. This decreased binding capacity reflected a rapid loss of high affinity receptors. The ability to form bFGF-receptor complexes decreased by 65% to 70% within 1 hour and declined continuously thereafter. The decrease in binding of bFGF was not due to an autocrine downregulation of bFGF receptors, because there was no increase in bFGF after PMA treatment as detected by Western blotting, and suramin, which blocks bFGF binding to receptors, did not prevent the loss of receptors after exposure to PMA. In addition, inhibitors of either protein synthesis or protease activity did not prevent the loss of bFGF receptors in PMA-treated cells. In summary, this work demonstrates that leukemia cell lines have receptors that specifically bind bFGF and supports the hypothesis that bFGF acts directly on certain blood cells to stimulate their proliferation.

    Topics: Animals; Binding Sites; CHO Cells; Cricetinae; Down-Regulation; Fibroblast Growth Factor 2; Heparan Sulfate Proteoglycans; Heparin; Heparitin Sulfate; HL-60 Cells; Humans; Leukemia; Leukemia, Megakaryoblastic, Acute; Leukemia, Myelogenous, Chronic, BCR-ABL Positive; Lymphoma, Large B-Cell, Diffuse; Megakaryocytes; Neoplasm Proteins; Protein Binding; Proteoglycans; Receptors, Fibroblast Growth Factor; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured

1996
Effects of glycosaminoglycans on U-937 leukemia cell proliferation and differentiation: structure-function relationship.
    Experimental cell research, 1994, Volume: 215, Issue:1

    Glycosaminoglycans (heparins, dermatan sulfate, chondroitin sulfate) with different structures and physicochemical properties were evaluated for their capacity to influence proliferation and differentiation of U-937 cell line. The contrasting and specific effects of glycosaminoglycans (depending on their structures and properties) on a leukemia cell line could help explain the regulation of proliferative and/or differentiative processes of hematopoietic cells in order to clarify the control of development and differentiation of hematopoietic progenitor cells by bone marrow extracellular matrix. Heparin from beef intestinal mucosa, heparan sulfate from beef spleen, dermatan sulfate from beef intestinal mucosa, and chondroitin sulfate from bovine trachea were extracted and purified, and their purity, structures, and physicochemical properties were evaluated. Fast-moving heparin was obtained by its selective precipitation as barium salt, and partially desulfated and re-N-sulfated heparin was produced by chemical modifications. Different glycosaminoglycans were tested to evaluate their effects on proliferation and differentiation processes of a monoblastic leukemia cell line (U-937). Heparin and derivatives (from 0.1 to 100 micrograms/ml) inhibit cell proliferation; heparan sulfate does not produce modifications, while chondroitin sulfate and dermatan sulfate (from 0.01 to 100 micrograms/ml) significantly stimulate cell growth. Cell differentiation was evaluated by cytoenzymatic determination of alpha-naphthyl butyrate esterase and by fluorescein-labeled anti-HLA-DR, anti-CD11b, and anti-CD14 antibodies. Nitro blue tetrazolium reduction and phagocytosis were also evaluated. Heparin and derivatives significantly increase U-937 differentiation. Heparin sulfate has no effect, while chondroitin sulfate and, to a lesser extent, dermatan sulfate, induce a strong decrease of differentiative markers. The regulation of U-937 cell properties appears to be related to charge density and to the amount of N-sulfate and N-acetyl groups. In particular, glycosaminoglycans with lower sulfate-to-carboxyl ratios and N-sulfate group percentages (chondroitin sulfate and dermatan sulfate) stimulate proliferation and produce a decrease of differentiative markers; on the contrary, polysaccharides with high charge density and N-sulfate group amounts (heparin and derivatives) inhibit U-937 proliferation and induce terminal differentiation. A previous paper (N. Volpi, L. Bolognani, A. C

    Topics: Animals; Carbohydrate Conformation; Carbohydrate Sequence; Cattle; Cell Differentiation; Cell Division; Cell Line; Chondroitin Sulfates; Chromatography, High Pressure Liquid; Dermatan Sulfate; Disaccharides; DNA, Neoplasm; Glycosaminoglycans; Heparin; Heparitin Sulfate; Humans; Intestinal Mucosa; Leukemia; Lymphoma, Large B-Cell, Diffuse; Molecular Sequence Data; Molecular Structure; Structure-Activity Relationship; Thymidine; Tumor Cells, Cultured

1994
Glycosaminoglycans enhance human leukemic cell growth in vitro.
    Leukemia research, 1994, Volume: 18, Issue:11

    We have previously shown that heparin and heparan sulfate stimulate the growth of human erythroleukemia cells in vitro in the presence of serum or plasma. To determine whether heparin and other glycosaminoglycans (GAGs) are involved in the growth of leukemia cells, effects of GAGs on the growth of three leukemia cell lines expressing different phenotypes, the HEL, HL60 and U937 cell lines were studied using both plasma clot and serum-free agar systems. The cells were cultured with different doses of six GAGs: hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate, heparin and heparan sulfate. It was found that, in serum-free agar system, no GAG was able to stimulate (HEL) cell growth. In contrast, when serum-containing culture systems were used, all six GAGs promoted colony formation of HL60 and U937 cells. In addition, all GAGs, except keratan sulfate, stimulated the growth of HEL cells. The findings suggest that the GAGs may play an indirect role in enhancing leukemia cell proliferation by different mechanisms.

    Topics: Cell Division; Chondroitin; Culture Media; Dermatan Sulfate; Glycosaminoglycans; Heparin; Heparitin Sulfate; Humans; Hyaluronic Acid; Keratan Sulfate; Leukemia; Leukemia, Monocytic, Acute; Leukemia, Promyelocytic, Acute; Tumor Cells, Cultured

1994
Involvement of glycosaminoglycans in detachment of early myeloid precursors from bone-marrow stromal cells.
    Biochimica et biophysica acta, 1981, Aug-17, Volume: 676, Issue:2

    Fibroblast-like cells were obtained by in vitro cultivation of needle aspirations of human bone-marrow. These cells show a unique composition of coat-associated glycosaminoglycans: 10% chondroitin 4-sulfate, 30% hyaluronic acid and 60% heparan sulfate which were resolved and characterized by electrophoresis, nitrous acid treatment and enzymatic degradation. Chondroitin 4-sulfate is the only glycosaminoglycan detectable on the surface of mature granulocytes, whereas the immature cells do not seem to possess surface glycosaminoglycans. Immature hemopoietic cells can adhere on to marrow-derived fibroblast cells, whereas mature granulocytes cannot. Treatment with mucopolysaccharidases of both mature leukocytes and marrow stromal cells can interfere in these adhesive relationships, suggesting a role of glycosaminoglycans in regulating short-range interactions during hematopoiesis.

    Topics: Bone Marrow Cells; Cell Adhesion; Chondroitin Sulfates; Fibroblasts; Glycosaminoglycans; Heparitin Sulfate; Humans; Hyaluronic Acid; Hyaluronoglucosaminidase; Leukemia; Leukocytes; Polysaccharide-Lyases

1981