A macrophage receptor for apolipoprotein B48: Cloning, expression, and atherosclerosis

Brown, Matthew L.; Ramprasad, Mysore P.; Umeda, Patrick K.; Tanaka, Akira; Kobayashi, Yasushi; Watanabe, Teruo; Shimoyamada, Hiroaki; Kuo, Wen-Lin; Li, Ran; Song, Ruiling; Bradley, William A.; Gianturco, Sandra H.

doi:10.1073/pnas.120184097

Cited by 96 publications

(94 citation statements)

References 34 publications

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“…In this study, expression of the apoB48 receptor in M -transformed THP-1 cells and in HepG2 cells was shown, but HUVEC did not express this receptor. Brown et al 10) reported the expression of apoB48 receptors by M -transformed THP-1 and by HUVEC, but not by HepG2 cells. This different result was presumably ascribable to differences in the conditions of cell culture and the PCR primers used, but it will be necessary to perform further studies to identify the reasons.…”

Section: Discussionmentioning

confidence: 99%

“…The apoB48-containing lipoproteins isolated in the present study were shown to be apoE-rich by SDS-PAGE. In recent years, the existence of a receptor for TG-rich lipoproteins on macrophages with apoB48 as a ligand has been reported and this is known as the apoB48 receptor 10) . In this study, expression of the apoB48 receptor in M -transformed THP-1 cells and in HepG2 cells was shown, but HUVEC did not express this receptor.…”

Section: Discussionmentioning

confidence: 99%

“…In this study, we isolated apoB48-containing lipoproteins using our anti-apoB48 monoclonal antibody (4C8) and investigated their characteristics. Furthermore, the uptake of apoB48-containing lipoproteins by THP-1 cells (a human acute monocytic leukemia cell line), HepG2 cells (a human hepatoma cell line), and human umbilical vein endothelial cells (HUVEC) was tested, and the expression of apoB48 receptors 10) in these cells was examined by RT-PCR.…”

Section: Introductionmentioning

confidence: 99%

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Isolation and Characterization of Apolipoprotein B48-Containing Lipoproteins with a Monoclonal Antibody Against Apolipoprotein B48

Yoshimura

Kinoshita

Teramoto

2009

JAT

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Aim: Remnant lipoproteins are well known to play a pivotal role in atherosclerosis. In patients with postprandial dyslipidemia, metabolic pathways for exogenous lipoproteins are generally disturbed, resulting in accumulation of chylomicron remnants. Although it has been difficult to make a specific antibody against apolipoprotein B48 (apoB48), a constituent of exogenous lipoproteins, we succeeded in creating a specific monoclonal antibody against apoB48. In this study, we isolated apoB48-containing lipoproteins from lipoproteins with a density less than 1.019 g/mL using this anti-apoB48 monoclonal antibody (4C8). Methods: Apolipoproteins and lipids were analyzed to confirm whether apoB48-containing lipoproteins are isolated from other lipoproteins. The characteristics of apoB48-containing lipoproteins in the plasma of patients were compared with type 2 diabetes mellitus and non-diabetic patients. Furthermore, the uptake of apoB48-containing lipoproteins by THP-1 cells (a human acute monocytic leukemia cell line), HepG2 cells (a human hepatoma cell line), and human umbilical vein endothelial cells (HUVEC) was investigated. Also, the expression of apoB48 receptors in these cells was tested with RT-PCR. Results: Apolipoprotein analysis of 4C8-bound lipoproteins indicated the isolation of apoB48-containing lipoproteins, because the content of apoB100 was quite low (less than 5%). Compared with lipoproteins that were not bound to the antibody, apoB48-containing lipoproteins had a higher content of triglycerides. There was no significant difference in the composition of apoB48-containing lipoproteins between patients with and without type 2 diabetes. Uptake of fluorescence-labeled apoB48-containing lipoproteins by THP-1-derived macrophages and HepG2 cells, but not by HUVEC, was observed. The specificity of this uptake was confirmed because the fluorescent signal was competed out by an excess amount of the same unlabeled lipoproteins. RT-PCR revealed the expression of apoB48 receptors in THP-1 and HepG2 cells but not in HUVEC. These results suggest that specific uptake of apoB48-containing lipoproteins may occur via apoB48 receptors. Conclusion

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Isolation and Characterization of Apolipoprotein B48-Containing Lipoproteins with a Monoclonal Antibody Against Apolipoprotein B48

Yoshimura

Kinoshita

Teramoto

2009

JAT

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“…Improvement in diabetic control reduces the ApoB48 concentrations in VLDL [82]. The avid binding of ApoB48 to the intima, smooth muscle cells and macrophages indicates the presence of high receptor affinity and could explain the preferential appearance of ApoB48 derived from the large VLDL in the atherosclerotic plaques [83,84].…”

Section: Diabetes Complications: Atherosclerosis and Hyperlipidaemiamentioning

confidence: 99%

Diabetes: mellitus or lipidus?

Shafrir

Raz

2003

Diabetologia

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“…3 In addition, macrophages express an apoE-independent pathway for the uptake of triglyceride-rich lipoproteins that recognizes apoB-48 or the similar domain on apoB-100 and has been termed the apoB-48 receptor. 4 Finally, macrophages express several different scavenger receptors that recognize modified lipoproteins, particularly lipoproteins that have been modified by oxidation. 5 Other lipoprotein modifications, such as aggregation, proteoglycan complex formation, and glycation, can lead to lipid accumulation in macrophages via these as well as other receptor and nonreceptor pathways.…”

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confidence: 99%

Lipoprotein Receptors, Macrophages, and Sphingomyelinase

Kraemer

Suzuki

2000

ATVB

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C holesteryl ester-filled macrophages are the hallmark of atherosclerotic lesions. Unraveling the pathways responsible for lipid accumulation in macrophages has been viewed as an important aspect for understanding a piece of the atherosclerotic process. 1 Investigations into the mechanisms through which macrophages accumulate cholesteryl esters from lipoproteins have delineated the involvement of several different receptor-and non-receptormediated pathways. For instance, macrophages express LDL receptors as well as several other members of the LDL receptor family, such as the LDL receptor-related protein (LRP) and the VLDL receptor. 2 The LDL receptor family recognizes apolipoprotein (apo) B-100 -and particularly apoE-containing lipoproteins. The uptake of lipoproteins via LDL receptor family members is facilitated by additional apoE, as well as by the presence of lipoprotein lipase. Each member of the LDL receptor family appears to be capable of contributing to a portion of the uptake of lipoproteins by macrophages; however, the contribution of each particular member will vary depending on the underlying pathophysiological condition. For instance, the LDL receptor is not functional in LDL receptor deficiency, and the contribution of either the LRP or the VLDL receptor would be expected to be low in apoE deficiency. 3 In addition, macrophages express an apoE-independent pathway for the uptake of triglyceride-rich lipoproteins that recognizes apoB-48 or the similar domain on apoB-100 and has been termed the apoB-48 receptor. 4 Finally, macrophages express several different scavenger receptors that recognize modified lipoproteins, particularly lipoproteins that have been modified by oxidation. 5 Other lipoprotein modifications, such as aggregation, proteoglycan complex formation, and glycation, can lead to lipid accumulation in macrophages via these as well as other receptor and nonreceptor pathways.

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A macrophage receptor for apolipoprotein B48: Cloning, expression, and atherosclerosis

Cited by 96 publications

References 34 publications

Isolation and Characterization of Apolipoprotein B48-Containing Lipoproteins with a Monoclonal Antibody Against Apolipoprotein B48

Isolation and Characterization of Apolipoprotein B48-Containing Lipoproteins with a Monoclonal Antibody Against Apolipoprotein B48

Diabetes: mellitus or lipidus?

Lipoprotein Receptors, Macrophages, and Sphingomyelinase

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