Glycosaminoglycan metabolism of HL-60 cells during differentiation induction by tetradecanoylphorbol-13-acetate

Luikart, Sharon D; Sackrison, James L.

doi:10.1016/0145-2126(86)90053-6

Cited by 6 publications

(2 citation statements)

References 30 publications

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“…Agents that induce cell lines to differentiate have been shown to affect proteoglycan synthesis. For example, phorbol 12-myristate 13-acetate (PMA) caused a substantial decrease in GAG synthesis during macrophage-like differentiation of U-937-4 and HL-60 cells [16][17][18]20].…”

Section: Introductionmentioning

confidence: 99%

Proteoglycan synthesis in human erythroleukaemia (HEL) cells

Schick

Senkowski-Richardson

1992

Biochemical Journal

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Synthesis of sulphated proteoglycans was compared in human erythroleukaemia (HEL) cells grown under control conditions and under stimulation by dimethyl sulphoxide (DMSO) and phorbol 12-myristate 13-acetate (PMA). Synthesis of [35S]sulphate-labelled proteoglycans by DMSO-treated cells was decreased by about 35% relative to controls, but synthesis of proteoglycans by PMA-treated cells increased 3-4-fold. Control and DMSO-treated cells secreted 65% of the newly synthesized proteoglycans, but PMA-treated cells secreted more than 90%. Sepharose CL-6B chromatography and SDS/PAGE suggested the presence of several proteoglycans in the cells and culture medium. The PMA-treated cells synthesized a low-Mr proteoglycan (Kav. 0.3( that was not present in controls and DMSO-treated cultures. The proteoglycans of the cells and medium from control, DMSO-treated and PMA-treated cultures could be separated into three fractions by octyl-Sepharose chromatography. The proteoglycans were resistant to trypsin but were degraded by Pronase and papain to fragments similar in size to the NaOH/NaBH4-generated glycosaminoglycans. The average chain length of the glycosaminoglycans (Kav. 0.20 on Sepharose CL-6B for controls) was decreased by DMSO (Kav. 0.25) and by PMA (Kav. 0.30-0.38). Chondroitin ABC lyase digestion of the proteoglycans from the medium of the control cultures produced two core proteins at Mr 31,000 and 36,000. The DMSO medium proteoglycans had only the 31,000-Mr core protein, and the PMA culture medium proteoglycans had core proteins of Mr 27,000, 31,000 and 36,000. Changes in synthesis of proteoglycans induced by DMSO or PMA may have relevance for the maturation of haematopoietic cells.

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Section: Introductionmentioning

confidence: 99%

Proteoglycan synthesis in human erythroleukaemia (HEL) cells

Schick

Senkowski-Richardson

1992

Biochemical Journal

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“…Sulfated proteoglycan production by human macrophages (3,221, peripheral blood monocytes (5)(6)(7)(34)(35)(36) and several myeloid leukemia cells induced to differentiate into monocytic cells (4, 37-41) have been described previously. Whereas human peritoneal macrophages and differentiated HL 60 and U937 leukemia cells appear to synthesize only chondroitin sulfate (3,4,(37)(38)(39)(40)(41), peripheral blood monocytes, like rat liver macrophages, produce both chondroitin sulfate and heparan sulfate (5, 34,36). Peritoneal macrophages from both nude and normal Balb/c mice have also been found to synthesize heparan sulfate ( 22 ).…”

Section: Discussionmentioning

confidence: 99%

Changes in sulfated proteoglycan production after activation of rat liver macrophages

et al. 1991

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Production of extracellular matrix proteins-in particular, the proteoglycans-by macrophages is important in many of their functions, including cell-cell recognition, adhesion and phagocytosis. In this study, we characterized changes in sulfated proteoglycan production by hepatic macrophages following in vivo activation with lipopolysaccharide. We found that both resident Kupffer cells and liver macrophages from lipopolysaccharide-treated rats incorporated [35S]sulfate into proteoglycans. Lipopolysaccharide-activated macrophages incorporated two to three times more of the label than did resident Kupffer cells. In addition, although both cell types produced chondroitin sulfate and heparan sulfate, resident Kupffer cells synthesized more chondroitin sulfate whereas lipopolysaccharide-activated cells produced more heparan sulfate. Using specific antibodies and flow cytometry, we also found that hepatic macrophages produced chondroitin-4-sulfate, chondroitin-6-sulfate and chondroitin-O-sulfate. Lipopolysaccharide-activated macrophages contained more chondroitin-4-sulfate and chondroitin-O-sulfate and less heparan sulfate than did resident Kupffer cells. Both tunicamycin and beta-D-xylosides, inhibitors of sulfated proteoglycan biosynthesis, were found to block phagocytosis by the cells. Taken together, these results suggest that sulfated proteoglycans are important in activation and functional responsiveness of liver macrophages.

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Biosynthesis of Proteochondroitin Sulfate by HL-60 Human Promyelocytic Cells

Bentley

Kirby

1989

Journal of Leukocyte Biology

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Human promyelocytic cells (HL-60) were labeled with 35S-sulfate and either 3H-glucosamine or 3H-serine as precursors. Accumulation of 35S-labeled macromolecules was approximately linear for up to 96 h, with a mean cell:medium ratio of 5.5:1, although activity/10(5) viable cells reached a plateau level after 24 h. Virtually none of the cell-associated proteoglycan was removed by trypsinization, consistent with a predominantly intracellular localization. Proteoglycan heterogeneity was investigated by DEAE-Sephacel chromatography, isopyknic CsCl gradient centrifugation, and gel filtration chromatography. HL-60 cells appeared to synthesize a single proteoglycan species, Kav = 0.46 on Sepharose CL-4B and Kav = 0.32 on Sepharose CL-6B, recovered primarily from the high-density fractions of a dissociative CsCl gradient (rho greater than 1.40 g/l). Degradation products of lower charge density, lower buoyant density, and lower hydrodynamic size were also present, mainly in the cell pellets. The major proteoglycan was found to contain chondroitin sulfate chains of average Mr = 14.5 kD, yielding virtually 100% 4-sulfated disaccharides on digestion with chondroitinase ABC. The proteoglycan was resistant to trypsin, chymotrypsin, plasmin, and papain, and the core protein Mr was approximately 20 kD by molecular sieve chromatography. Induction of HL-60 cells with 0.15 dimethyl sulfoxide (DMSO) resulted in differentiation to a more mature granulocytic phenotype and was associated with a reduction in 35S-sulfate incorporation to 45% of control values or 32%, expressed as activity/10(5) cells. Proteoglycans synthesized by DMSO-treated cells were identical to those from untreated cells in terms of hydrodynamic size, glycosaminoglycan Mr, and sulfation.

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Glycosaminoglycan metabolism of HL-60 cells during differentiation induction by tetradecanoylphorbol-13-acetate

Cited by 6 publications

References 30 publications

Proteoglycan synthesis in human erythroleukaemia (HEL) cells

Proteoglycan synthesis in human erythroleukaemia (HEL) cells

Changes in sulfated proteoglycan production after activation of rat liver macrophages

Biosynthesis of Proteochondroitin Sulfate by HL-60 Human Promyelocytic Cells

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