Induction of Monocyte Binding to Endothelial Cells by MM-LDL

Honda, Henry M.; Leitinger, Norbert; Frankel, Matthew; Goldhaber, Joshua I.; Natarajan, Rama; Nadler, Jerry L.; Weiss, James N.; Berliner, Judith A.

doi:10.1161/01.atv.19.3.680

Cited by 68 publications

(55 citation statements)

References 43 publications

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“…There is also evidence for an additional pathway regulating monocyte adhesion involving lipoxygenase. 24 Treatment of endothelial cells with MM-LDL was shown to cause the release of arachidonic acid; furthermore, monocytes binding induced by MM-LDL and POVPC was reduced by inhibition of the lipoxygenase pathway 25 . Furthermore, 12-S-Hete mimicked the effect on monocyte binding and there was evidence for a role of CS-1 fibronectin.…”

Section: Monocyte Bindingmentioning

confidence: 99%

Endothelial cell regulation by phospholipid oxidation products

Berliner

Gharavi

2008

Free Radical Biology and Medicine

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Oxidized phospholipids accumulate in atherosclerotic lesions, on lipoproteins, in other states of chronic inflammation, on apoptotic cells, necrotic cells and cells exposed to oxidative stress. These lipids regulate the transcription of over 1000 gene, regulating many endothelial functions, by activating several different cell surface receptors and multiple signaling pathways. These lipids also have important effects not involving transcription that regulate cell junctions and leukocyte binding. Thus these lipids are potent regulators of endothelial cell function with broad effects comparable in extent but differing from those of cytokines.

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Section: Monocyte Bindingmentioning

confidence: 99%

Endothelial cell regulation by phospholipid oxidation products

Berliner

Gharavi

2008

Free Radical Biology and Medicine

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“…20 The induction of monocyte binding to endothelial cells exposed to mildly oxidized LDL also involves lipoxygenase (LO) metabolites. 21 The mechanism for the induction of MCP-1 and IL-8 in endothelial cells exposed to mildly oxidized LDL, Ox-PAPC, POVPC, or PGPC appears to involve the lipid-dependent transcription factor peroxisome proliferator-activated receptor-␣. 19 The response of endothelial cells to these oxidized phospholipids appears to be genetically determined.…”

Section: ;21:481-488)mentioning

confidence: 99%

HDL and the Inflammatory Response Induced by LDL-Derived Oxidized Phospholipids

Navab¹,

Berliner²,

Subbanagounder³

et al. 2001

ATVB

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406

253

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Abstract-Oxidation of low density lipoprotein (LDL) phospholipids containing arachidonic acid at the sn-2 position occurs when a critical concentration of "seeding molecules" derived from the lipoxygenase pathway is reached in LDL. When this critical concentration is reached, the nonenzymatic oxidation of LDL phospholipids produces a series of biologically active, oxidized phospholipids that mediate the cellular events seen in the developing fatty streak. Normal high density lipoprotein (HDL) contains at least 4 enzymes as well as apolipoproteins that can prevent the formation of the LDL-derived oxidized phospholipids or inactivate them after they are formed. In the sense that normal HDL can prevent the formation of or inactivate these inflammatory LDL-derived oxidized phospholipids, normal HDL is anti-inflammatory. HDL from mice that are genetically predisposed to diet-induced atherosclerosis became proinflammatory when the mice are fed an atherogenic diet, injected with LDL-derived oxidized phospholipids, or infected with influenza A virus. Mice that were genetically engineered to be hyperlipidemic on a chow diet and patients with coronary atherosclerosis, despite normal lipid levels, also had proinflammatory HDL. It is proposed that LDL-derived oxidized phospholipids and HDL may be part of a system of nonspecific innate immunity and that the detection of proinflammatory HDL may be a useful marker of susceptibility to atherosclerosis. (Arterioscler Thromb Vasc Biol. 2001;21:481-488.)Key Words: HDL Ⅲ LDL Ⅲ atherosclerosis Ⅲ oxidized phospholipids T he events involved in fatty streak formation resemble those elicited by mycobacteria. 1 Over the past decade, there has been increasing evidence that this inflammatory response may, in part, be elicited by the oxidation of phospholipids contained in LDL. 2,3 Several oxidized phospholipids that are able to induce the genes and proteins necessary for the cellular response seen in the fatty streak have been identified in mildly oxidized LDL and in lesions of animal models of atherosclerosis. 4 -9 Two of these oxidized phospholipids, 1-palmitoyl-2(5-oxovaleroyl)-sn-glycero-3-phosphorylcholine (POVPC) and 1-palmitoyl-2-glutaroyl-snglycero-3-phosphorylcholine (PGPC), both induced monocytes to bind to endothelial cells. 10 However, PGPC but not POVPC also induced neutrophils to bind to endothelial cells. 10 Indeed, POVPC strongly inhibited lipopolysaccharide-mediated induction of neutrophil binding and expression of E-selectin protein and mRNA. 10 This inhibition by POVPC was mediated by a protein kinase A-dependent pathway that resulted in downregulation of nuclear factor-B-dependent transcription. 10 PGPC, on the other hand, induced both E-selectin and vascular cell adhesion molecule-1 (VCAM-1) expression on endothelial cells. 10 On the basis of studies in Xenopus laevis oocytes, Leitinger et al 10 concluded that POVPC and PGPC bound to different receptors. Furthermore, they demonstrated that at concentrations equal to those present in mildly oxidized LDL, POVPC prevente...

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“…The 12-and 15-LOXs form hydroxyeicosatetraenoic acids (HETEs), and 5-LOX catalyzes the formation of 5-HETE and leukotrienes (LTs). HETEs and LTs are known to be involved in some aspects of adhesion (Damtew and Spagnuolo, 1997;Trikha and Honn, 1997;Rice et al, 1998;Honda et al, 1999) as well as inflammation (Lee et al, 1997;Natarajan et al, 1997;Conrad, 1999). There are two COX isoforms.…”

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Modulation of Cell-Substrate Adhesion by Arachidonic Acid: Lipoxygenase Regulates Cell Spreading and ERK1/2-inducible Cyclooxygenase Regulates Cell Migration in NIH-3T3 Fibroblasts

Stockton

Jacobson

2001

MBoC

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Adhesion of cells to an extracellular matrix is characterized by several discrete morphological and functional stages beginning with cell-substrate attachment, followed by cell spreading, migration, and immobilization. We find that although arachidonic acid release is rate-limiting in the overall process of adhesion, its oxidation by lipoxygenase and cyclooxygenases regulates, respectively, the cell spreading and cell migration stages. During the adhesion of NIH-3T3 cells to fibronectin, two functionally and kinetically distinct phases of arachidonic acid release take place. An initial transient arachidonate release occurs during cell attachment to fibronectin, and is sufficient to signal the cell spreading stage after its oxidation by 5-lipoxygenase to leukotrienes. A later sustained arachidonate release occurs during and after spreading, and signals the subsequent migration stage through its oxidation to prostaglandins by newly synthesized cyclooxygenase-2. In signaling migration, constitutively expressed cyclooxygenase-1 appears to contribute ϳ25% of prostaglandins synthesized compared with the inducible cyclooxygenase-2. Both the second sustained arachidonate release, and cyclooxygenase-2 protein induction and synthesis, appear to be regulated by the mitogen-activated protein kinase extracellular signal-regulated kinase (ERK)1/2. The initial cell attachment-induced transient arachidonic acid release that signals spreading through lipoxygenase oxidation is not sensitive to ERK1/2 inhibition by PD98059, whereas PD98059 produces both a reduction in the larger second arachidonate release and a blockade of induced cyclooxygenase-2 protein expression with concomitant reduction of prostaglandin synthesis. The second arachidonate release, and cyclooxygenase-2 expression and activity, both appear to be required for cell migration but not for the preceding stages of attachment and spreading. These data suggest a bifurcation in the arachidonic acid adhesion-signaling pathway, wherein lipoxygenase oxidation generates leukotriene metabolites regulating the spreading stage of cell adhesion, whereas ERK 1/2-induced cyclooxygenase synthesis results in oxidation of a later release, generating prostaglandin metabolites regulating the later migration stage. INTRODUCTIONCell adhesion to the extracellular matrix (ECM) is a sequential process of discrete temporal stages. Detached cells, e.g., leukocytes, metastasized cancer cells, or suspension-cultured cells, initially attach to an ECM protein substrate by means of plasma membrane receptors. Attached cells then undergo spreading, which results in flattening and the formation of focal adhesions. Subsequently, some cell types undergo migration on the ECM, whereas others remain stationary. Each of these stages of adhesion, i.e., attachment, spreading, migration, and immobilization, involves changes in morphology and cytoskeletal structure that are regulated by incompletely defined protein kinase and lipid second messenger pathways (reviewed in Huttenlocher et al., 1995;Heidemann an...

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Induction of Monocyte Binding to Endothelial Cells by MM-LDL

Cited by 68 publications

References 43 publications

Endothelial cell regulation by phospholipid oxidation products

Endothelial cell regulation by phospholipid oxidation products

HDL and the Inflammatory Response Induced by LDL-Derived Oxidized Phospholipids

Modulation of Cell-Substrate Adhesion by Arachidonic Acid: Lipoxygenase Regulates Cell Spreading and ERK1/2-inducible Cyclooxygenase Regulates Cell Migration in NIH-3T3 Fibroblasts

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