Control of lipoprotein lipase secretion in mouse macrophages

Goldman, Rachel; Sopher, Orit

doi:10.1016/0005-2760(89)90137-9

Cited by 11 publications

(6 citation statements)

References 41 publications

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“…In 3T3-L1 and in ob/ob cells lipoprotein lipase synthesis is turned on after the cells become confluent and differentiate into adipocyte-like cells [8,12]. In macrophages, on the other hand, lipoprotein lipase production is high in activated [7] and proliferating [6] cells; when the cells become growth-arrested, lipoprotein lipase production is remarkably suppressed. The constitutive expression of lipoprotein lipase in CHO cells may reflect a property in the ancestral ovarian cells.…”

Section: Discussionmentioning

confidence: 99%

“…Many studies on lipoprotein lipase have been carried out with cell lines [8][9][10][11][12][13] and with primary cultures of cells [14][15][16][17][18][19]. In the cell lines the expression of lipoprotein lipase is usually dependent on the growth conditions [6][7][8]12]. In the present paper we report that the enzyme is also produced in Chinese-hamster ovary (CHO) cells, where it is expressed both in growing and in confluent cells.…”

Section: Introductionmentioning

confidence: 96%

“…In general, these are cells engaged in rapid metabolism of fatty acids such as adipocytes and muscle cells. Another cell type which makes lipoprotein lipase is macrophages [6,7], but the function of this enzyme is less clear. Many studies on lipoprotein lipase have been carried out with cell lines [8][9][10][11][12][13] and with primary cultures of cells [14][15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

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Synthesis and secretion of active lipoprotein lipase in Chinese-hamster ovary (CHO) cells

Rojas

Enerbäck

Bengtsson‐Olivecrona

1990

Biochemical Journal

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Cultured Chinese-hamster ovary cells (CHO cells) were found to produce and secrete a lipase, which was identified as a lipoprotein lipase by the following criteria. Its activity was stimulated by serum and apolipoprotein CII, and was inhibited by high salt concentration. The lipase bound to heparin-agarose and co-eluted with 125I-labelled bovine lipoprotein lipase in a salt gradient. A chicken antiserum to bovine lipoprotein lipase inhibited the activity and precipitated a labelled protein of the same apparent size as bovine lipoprotein lipase from media of CHO cells labelled with [35S]methionine. The lipase activity and secretion were similar in growing cells and in cells that had reached confluency. Hence, lipoprotein lipase appears to be expressed constitutively in CHO cells and is not linked to certain growth conditions, as in pre-adipocyte and macrophage cell lines. At 37 degrees C, but not at 4 degrees C, heparin increased the release of lipase to the medium 2-4-fold. This increased release occurred without depletion of cell-associated lipase activity, suggesting that heparin enhanced release of newly synthesized lipase.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Synthesis and secretion of active lipoprotein lipase in Chinese-hamster ovary (CHO) cells

Rojas

Enerbäck

Bengtsson‐Olivecrona

1990

Biochemical Journal

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“…This experiment uniquely uses both VLDL and macrophages from rat sources and to our knowledge is the first study to compare macrophage utilisation of NEFA and TAG (VLDL), in both quiescent and active state. In the unstimulated (control) state, cVLDL-TAG was utilised to a similar extent as NEFA by 48h of incubation (VLDL-TAG utilisation rate peaked at 24-36h (data not shown) but this probably reflects alterations in substrate utilisation between glucose and lipids during rapid growth phase [16]). However, TAG from VLDL synthesised by endotoxic rat liver (eVLDL) was utilised at a greater rate than NEFA or cVLDL-TAG, suggesting that eVLDL is a better substrate for macrophages and apparently supporting similar findings of eVLDL efficacy in heart [8].…”

Section: Discussionmentioning

confidence: 99%

Utilisation of Fatty Acid and Triacylglycerol by Rat Macrophages: the Effect of Endotoxin

Hui‐Kang

Evans²

2002

Cell Physiol Biochem

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Background/Aims: Plasma very-low-density lipoprotein (VLDL) concentrations are increased during sepsis/endotoxaemia and VLDL may be substrates for the activated immune system. Lipid substrate utilisation by quiescent and activated macrophages was therefore examined. Methods: Rat R2 macrophages were incubated with oleate or rat VLDL, with or without lipopolysaccharide (LPS) stimulation. The metabolic fate of the lipids was examined. Results: Macrophages utilised both oleate and (control) VLDL-triacylglycerol (TAG) to a similar extent. Most was deposited as cellular lipid; about 10% of oleate was oxidised compared to 25% of cVLDL-TAG. LPS significantly increased oleate oxidation and its deposition as cellular lipid (mostly as TAG) at 48hrs but abolished both oxidation and storage of VLDL-TAG. VLDL produced during endotoxaemia (eVLDL) was assimilated by the unstimulated macrophage to a greater extent than oleate or cVLDL-TAG and selectively stored as cellular lipids (no oxidation); LPS decreased eVLDL utilisation. VLDL-TAG utilisation was decreased by the lipoprotein lipase (LPL) inhibitor terahydrolipstatin. LPL activity was greater in oleate than in VLDL incubations, but was increased by incubation with eVLDL. LPS had no effect (oleate, cVLDL) or increased (eVLDL) LPL activity. Conclusion: VLDL represented an efficient substrate for the macrophage. However under conditions of sepsis/endotoxaemia eVLDL utilisation was limited and directed away from oxidation, suggesting that the increased plasma TAG (eVLDL) concentrations resulting from sepsis is not a respiratory fuel for the macrophage but may supply cellular lipid.

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“…39 Lipopolysaccharide also suppresses LPL secretion from macrophages. 40 On the other hand, it has been reported that cholesterol-rich lipoproteins, 12 hypertriglyceridemic very low density lipoproteins, 13 and L-cell-conditioned medium 41 enhance LPL secretion from macrophages. L-cell-conditioned medium, which stimulates the macrophage lineage, increases LPL secretion from mouse bone marrow macrophages and thioglycollate-elicited peritoneal macrophages, whereas it has no effect on LPL secretion from resident peritoneal macrophages.…”

Section: Discussionmentioning

confidence: 99%

Effects of human recombinant macrophage colony-stimulating factor on the secretion of lipoprotein lipase from macrophages.

Mori

Gotoda

Ishibashi

et al. 1991

Arterioscler Thromb

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Control of lipoprotein lipase secretion in mouse macrophages

Cited by 11 publications

References 41 publications

Synthesis and secretion of active lipoprotein lipase in Chinese-hamster ovary (CHO) cells

Synthesis and secretion of active lipoprotein lipase in Chinese-hamster ovary (CHO) cells

Utilisation of Fatty Acid and Triacylglycerol by Rat Macrophages: the Effect of Endotoxin

Effects of human recombinant macrophage colony-stimulating factor on the secretion of lipoprotein lipase from macrophages.

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