Formaldehyde treated albumin contains monomeric and polymeric forms that are differently cleared by endothelial and kupffer cells of the liver: Evidence for scavenger receptor heterogeneity

Jansen, Robert W.; Molema, Grietje; Harms, Geert; Kruijt, J. Kar; Berkel, Theo J.C. Van; Hardonk, M. J.; Meijer, Dirk K. F.

doi:10.1016/s0006-291x(05)81249-5

Cited by 50 publications

(25 citation statements)

References 19 publications

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“…The high endothelial cell uptake of Aco-HSA liposomes probably is related to the abundant presence of scavenger receptors on this cell type, which have been demonstrated to be responsible for the uptake of a large variety of polyanionic macromolecules, including negatively charged albumins (11). Involvement of macrophage scavenger receptors also has been suggested in the uptake of liposomes that were negatively charged by conjugation with polyacrylic acid (23).…”

Section: Discussionmentioning

confidence: 99%

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Massive targeting of liposomes, surface-modified with anionized albumins, to hepatic endothelial cells

Kamps¹,

Morselt²,

Meijer³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

118

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Human serum albumin (HSA) derivatized with cis-aconitic anhydride was covalently coupled to liposomes with a size of approximately 100 nm [polyaconitylated HSA (Aco-HSA) liposomes]. Within 30 min after injection into a rat, Aco-HSA liposomes were completely cleared from the blood and almost exclusively taken up by the liver, whereas in control liposomes 80% was still present in the blood at that time. Endothelial cells were shown to account for almost two-thirds of the hepatic uptake of the Aco-HSA liposomes, the remainder being recovered mainly in the liver macrophages

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Section: Discussionmentioning

confidence: 99%

“…The polyanionic nature of the Aco-HSA suggested the role of scavenger receptors on sinusoidal cell types in this process. These receptors have been implicated in the uptake from the blood of polyanionic macromolecules like acetylated low-density lipoprotein, oxidatively modified low-density lipoprotein, and various modified albumins (10,11).…”

mentioning

confidence: 99%

Massive targeting of liposomes, surface-modified with anionized albumins, to hepatic endothelial cells

Kamps¹,

Morselt²,

Meijer³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

118

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“…Similarly, particulate preparations of formaldehydetreated albumin were taken up by Kupffer cells via scavenger receptors but not by endothelial cells. 50 In the current study, cell-based assays were focused on SR-AI/II and CD36, whereas MARCO could not be examined in detail, because MARCO is not expressed in BMMs. Reduced CPP clearance in SR-A/MARCO double-deficient mice, however, suggests that in addition to SR-A MARCO might also be involved in CPP clearance.…”

Section: Discussionmentioning

confidence: 99%

Clearance of Fetuin-A–Containing Calciprotein Particles Is Mediated by Scavenger Receptor-A

Herrmann

Schäfer²,

Heiss³

et al. 2012

Circulation Research

143

118

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Rationale: Fetuin-A is a liver-derived plasma protein involved in the regulation of calcified matrix metabolism.Biochemical studies showed that fetuin-A is essential for the formation of protein-mineral complexes, called calciprotein particles (CPPs). CPPs must be cleared from circulation to prevent local deposition and pathological calcification.Objective: We studied CPP clearance in mice and in cell culture to identify the tissues, cells, and receptors involved in the clearance. Methods and Results:

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“…Little is currently known about the fraction when the animal is killed 1 hour after injection and the cell fractions are separated by centrifugal elutriation. Recently, Jansen et al 13 have shown that Kupffer cells can be involved in the endocytosis of f-Alb but only when the Abbreviations: RME, receptor-mediated endocytosis; LEC, liver endothelial cell; f-Alb, product has polymerized. Finally, the f-Alb receptor also recformaldehyde-modified albumin; LDL, low-density lipoprotein; BSA, bovine serum albumin; AA-Alb, acetaldehyde-modified albumin; GdCl3, gadolinium chloride.…”

mentioning

confidence: 99%

Long-term ethanol administration alters the degradation of acetaldehyde adducts by liver endothelial cells

Thiele¹

1996

Hepatology

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effects of ethanol on liver endothelial cells (LECs). However, Previous reports have shown that long-term ethanolRees et al. 1 have shown recently that the uptake and degradaadministration alters receptor-mediated endocytosis tion of formaldehyde-modified albumin (f-Alb) by the scaven-(RME) of a variety of macromolecules by liver endotheger receptor on LECs is decreased markedly by long-term lial cells (LEC). Acetaldehyde is the major metabolic ethanol consumption. product of ethanol metabolism and has been shown toResearch for the last several years has shown that LECs bind to proteins to form adducts. In this study, the level play an active role in the reticuloendothelial system of the of protein modification by acetaldehyde necessary for liver. Specifically, LECs are involved in clearance from blood the uptake and degradation of acetaldehyde-modified of a variety of substances, including connective tissue compoproteins by LEC was investigated. Bovine serum albunents and several types of modified proteins. 2 In fact, RME min (BSA) acetaldehyde adducts were prepared by incubation of albumin with acetaldehyde at 100 mmol/L for and degradation by LECs are the major mechanisms for 1 hour at 37ЊC, and 1 mmol/L or 0.2 mmol/L for 5 days clearance of circulating hyaluronic acid, denatured collagens, at 37ЊC. In situ liver perfusion in the presence of these the N-terminal propeptide of type III collagen PIIINP, lamiadducts resulted in the degradation of 107 { 10.02 mg, nin, mannosylated glycoproteins, acetylated low-density lipo-69.82 { 5 mg, and 2.5 { 0.42 mg of acetaldehyde-adducted protein (LDL), and f-Alb. Receptors for chemically modified albumin, respectively, during a 4-hour period. These val-proteins, such as acetylated LDL and f-Alb, have been collecues were decreased by 53%, 67%, and nearly 100%, re-tively referred to as scavenger receptors. There has been spectively, in livers from ethanol-fed rats. Additionally, some debate as to whether there is one receptor for acetylated modification of protein with 1 mmol/L of acetaldehyde LDL and f-Alb or whether there is one receptor for each. for different periods of time and/or pH altered the Although macrophages and LECs can clear f-Alb and aceamount of 14 C-acetaldehyde binding, but no signifi-tylated LDL, they are cleared predominantly from the circucant changes in degradation were observed. Finally, lation by LECs. 3,4 Horiuchi et al. have shown that, although an excess of formaldehyde-modified albumin totally acetylated LDL did inhibit binding of f-Alb to sinusoidal endoinhibited the degradation of acetaldehyde adducts, thelial cells, the converse did not occur. 5 Additionally, an suggesting that they use the same receptor. These antibody specific for the f-Alb receptor did not inhibit endocydata show that acetaldehyde-modified proteins may tosis of acetylated LDL. 6 Some investigators maintain that be taken up and degraded by the scavenger receptor there are different receptors for these modified proteins, 7,8 on LEC. This uptake and degradation are dependent ...

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Formaldehyde treated albumin contains monomeric and polymeric forms that are differently cleared by endothelial and kupffer cells of the liver: Evidence for scavenger receptor heterogeneity

Cited by 50 publications

References 19 publications

Massive targeting of liposomes, surface-modified with anionized albumins, to hepatic endothelial cells

Massive targeting of liposomes, surface-modified with anionized albumins, to hepatic endothelial cells

Clearance of Fetuin-A–Containing Calciprotein Particles Is Mediated by Scavenger Receptor-A

Long-term ethanol administration alters the degradation of acetaldehyde adducts by liver endothelial cells

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