Receptor recognition of maleyl-albumin induces chemotaxis in human monocytes.

Rasmussen, Ronald R.; Fogelman, Alan M.

doi:10.1172/jci112647

Cited by 16 publications

(3 citation statements)

References 32 publications

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“…However, none of these agents had chemotactic activity for circulating human monocytes (data not shown). These results agree with those recently reported by Haberland et al (26).…”

Section: Methodssupporting

confidence: 94%

Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis.

Quinn¹,

Parthasarathy²,

Fong³

et al. 1987

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

983

401

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Previous studies in this laboratory established that low density lipoprotein (LDL) incubated with cultured endothelial cells, smooth muscle cells, or macrophages undergoes a free radical-catalyzed oxidative modification that generates lipid peroxides and extensive structural changes in the LDL molecule. The oxidatively modified LDL strongly inhibited chemotactic responses of the mouse resident peritoneal macrophage. The present studies show that this oxidized LDL does not inhibit the motility of mouse monocytes and actually exhibits a chemotactic activity for human monocytes; the chemotactic activity of the oxidized LDL resides in the lipid fraction. These findings allow us to propose a pathogenetic sequence by which elevated plasma LDL levels, followed by oxidative modification in the arterial wall, could sufficiently account for the generation of the lipid-laden foam cells and the initiation of the fatty streak, the earliest well-defined lesion in atherogenesis.Accumulation of lipid in the arterial intima is central to the development of atherosclerosis. Intimal lipid accumulates intracytoplasmically in foam cells, which are derived both from medial smooth muscle cells (1, 2) and monocyte-derived macrophages (3)(4)(5), the latter probably being quantitatively more important (3-5). Exactly how monocytes are recruited and retained in the artery wall remains unclear, but probably the initial event is adhesion to the endothelial surface (3) followed by penetration that is influenced by a chemotactic factor(s). Many different factors chemotactic for monocytes have been described (6); the relative importance of these remains uncertain. Crude extracts of whole aorta contain chemotactic activity (7), and cultured arterial smooth muscle cells and macrophages release chemotactic activity into the culture medium (8). We recently described release of chemotactic activity for mouse resident peritoneal macrophages from cultured aortic endothelial cells (9) and showed that oxidatively modified low density lipoprotein (LDL) inhibited the chemotactic response of the macrophage. In the present studies we confirm the finding of Berliner et al. (10) that endothelial cell-conditioned medium is chemotactic also for human monocytes. However, oxidatively modified LDL, instead of inhibiting the motility of monocytes actually enhances their motility. We further show that the chemotactic activity resides in the lipid fraction of the modified LDL, presumably in one or another peroxidized lipid component. Thus oxidative modification of LDL, in addition to favoring the accumulation of cholesterol stores in developing foam cells (11), could play a role in recruitment and retention of monocyte/macrophages into the subendothelial space and, finally, may contribute to atherogenesis through injury to endothelial cells. MATERIALS AND METHODSHam's F-10 medium and fetal bovine serum were from HyClone (Logan, UT); female Swiss Webster mice were from Simonsen Laboratories (Gilroy, CA); Ficoll/Hypaque, bovine serum albumin, zymosan A, fucoidi...

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“…However, none of these agents had chemotactic activity for circulating human monocytes (data not shown). These results agree with those recently reported by Haberland et al (26).…”

Section: Methodssupporting

confidence: 94%

Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis.

Quinn¹,

Parthasarathy²,

Fong³

et al. 1987

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

983

401

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“…Unmodified BSA did not enhance any migratory activity by human monocytes. Chemotactic activity of AGE-albumin preparations was retained after extensive digestion by proteinase K (100 ;zg/mg of albumin), indicating that higher order protein structural features were not involved, as shown for albumin after maleylation (22) or single lysine glycosylation (23). Checkerboard analysis confirmed that movement of monocytes in the presence of AGEalbumin represented directed chemotaxis and not enhanced random cell migration (chemokinesis) ( Table 1): monocyte migration was enhanced only when the concentration of AGE-albumin in the lower compartment exceeded that in the upper compartment.…”

mentioning

confidence: 91%

Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging.

Kirstein

Brett

Radoff

et al. 1990

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

341

144

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Diabetes and aging are commonly accompanied by arterio-and atherosclerosis. Infiltration of the arterial subendothelial intima by macrophages/monocytes is an important early event preceding the development of atheromatous lesions; these macrophages are known to produce mitogenic factors in early atherosclerotic lesions. It has been previously shown that, over time, vascular matrix accumulates proteins nonenzymatically modified by advanced glycosylation end products (AGEs). In view of the fact that macrophages/ monocytes have AGE-specific receptors associated with the expression of several growth factors, we investigated the possibility that AGEs mediate initial monocyte-vessel wall interactions that occur before overt formation of vascular lesions.This study demonstrates that (a) in vitro-and in vivo-formed AGEs are chemotactic for human blood monocytes, (il) subendothelial AGEs can selectively induce monocyte migration across an intact endothelial cell monolayer, and (iii) subsequent monocyte interaction with AGE-containing matrix results in the expression of platelet-derived growth factor. These results support the existing hypothesis that in vivo-forming glucosederived protein adducts can act as signals for the normal turnover of senescent tissue protein by means of the AGEspecific receptor system. Time-dependent glucose-induced

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“…In addition. mBSA interaction with its macrophage receptor{s) elicits cellular activation and chemotaxis [11][12][13][14][15].…”

Section: Introductionmentioning

confidence: 99%

Aggregated Human Immunoglobulins Bind to Modified Proteins

et al. 1993

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Human immunoglobulins treated at 55 degrees C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with binding capacity for mBSA could also be generated in vitro by treatment of human IgG at 37 degrees C or 40 degrees C and by incubation with human neutrophils. Furthermore, IgG aggregates with binding activity for mBSA could be detected in untreated synovial fluids from rheumatoid arthritis patients, indicating that these complexes occur in vivo. The phenomenon of binding to aggregated IgG was extended to other modified proteins such as maleylated human serum albumin (mHSA), acetyl low density lipoprotein (Ac-LDL) and BSA reacted with oxidized linolenic acid. Soluble forms of these modified proteins were able to compete for the interaction between aggregated IgG and surface-bound mBSA. We also found that aggregated IgG enhanced the Ac-LDL-dependent foam cell formation. These findings suggest a role for aggregated IgG in the metabolism of oxidized proteins.

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Receptor recognition of maleyl-albumin induces chemotaxis in human monocytes.

Cited by 16 publications

References 32 publications

Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis.

Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis.

Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging.

Aggregated Human Immunoglobulins Bind to Modified Proteins

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