Sulfoglycolipids bind to adhesive protein amphoterin (P30) in the nervous system

Mohan, Panaiyur S.; Laitinen, Jari; Merenmies, Jussi; Rauvala, Heikki; Jungalwala, Firoze B.

doi:10.1016/0006-291x(92)91787-q

Cited by 47 publications

(33 citation statements)

References 25 publications

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“…Furthermore, the anti-RAGE antibodies used in our study display some function-blocking activity. On the basis of these experiments the possibility still remains that other amphoterinbinding molecules in addition to RAGE, like proteoglycans 61 or sulfoglycolipids, 12 could play a role as amphoterin receptors in transendothelial migration.…”

Section: Discussionmentioning

confidence: 99%

“…3,9,10 Amphoterin binds to plasma membrane lipids, mainly to phosphatidylserine and sulfatide, and enhances and localizes plasminogen activation. 6,9,[11][12][13] In neurons, neurite outgrowth on amphoterin surface is mediated by receptor for advanced glycation end products (RAGE), a member of the immunoglobulin superfamily transmembrane receptors. 14,15 Consistent with a potential role of RAGE-amphoterin interaction, RAGE and amphoterin were shown to colocalize during brain development, and their signaling induces neurite outgrowth by way of the guanosine triphosphatases (GTPases) rac and Cdc42 and up-regulates expression of chromogranins.…”

Section: Introductionmentioning

confidence: 99%

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Regulation of monocyte migration by amphoterin (HMGB1)

Rouhiainen

Kuja-Panula²,

Wilkman³

et al. 2004

Blood

228

194

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Amphoterin (HMGB1) is a 30-kD heparinbinding protein involved in process extension and migration of cells by a mechanism involving the receptor for advanced glycation end products (RAGE). High levels of amphoterin are released to serum during septic shock. We have studied the expression of amphoterin in monocytes and the role of amphoterin and RAGE in monocyte transendothelial migration. Unactivated monocytes in suspension did not reveal amphoterin on their surface, but adherent monocytes exported amphoterin to the cell surface. Immunohistochemical staining of arterial thrombi in vivo revealed amphoterin in mononuclear cells and in surrounding extracellular matrix. Amphoterin was secreted from phorbol ester and interferon-␥ (IFN-␥)-activated macrophages, and the secretion was inhibited by blocking the adenosine 5-triphosphate (ATP)-binding cassette transporter-1, a member of the multidrug resistance protein family. Amphoterin was specifically adhesive for monocytes in peripheral blood leukocyte adhesion assay. Adhesion caused an extensive spreading of cells, which was inhibited by the dominant-negative RAGE receptor (soluble ectodomain of RAGE), and adhesion up-regulated chromogranin expression in monocytes, also suggesting a RAGE-dependent interaction. Monocyte transendothelial migration was efficiently inhibited by anti-amphoterin and anti-RAGE antibodies and by the soluble RAGE. We suggest that amphoterin is an autocrine/paracrine regulator of monocyte invasion through the endothelium. IntroductionCirculating monocytes adhere to sites of vascular injury where they participate together with other cells in the regulation of blood clotting, inflammation, and wound healing. Adhesion to other cells and extracellular matrix components is a prerequisite for migration and tissue recruitment of monocytes. 1,2 The knowledge of molecules involved in monocyte transendothelial migration is rapidly increasing. However, the overall picture of the transendothelial migration mechanism is not completely understood. 2 Amphoterin is a 30-kD heparin-binding protein widely expressed in humans and other organisms, and it is abundantly expressed in the developing brain as well as in various immature and transformed cell lines. [3][4][5][6] It was isolated as an extracellular neurite outgrowth-promoting protein, but its amino acid sequence turned out to be identical to high-mobility groupϪ1 protein. 5,7 In a new nomenclature of high-mobility group proteins amphoterin and other proteins identical in the cDNA sequence are called as HMGB1 (high-mobility group B-1). 8 We have used the designation amphoterin for the protein occurring in the extracellular space and interacting with the cell surface. 5 Surface-bound amphoterin is adhesive for neural cells and platelets, and it induces extension of membrane processes in adherent cells. 3,9,10 Amphoterin binds to plasma membrane lipids, mainly to phosphatidylserine and sulfatide, and enhances and localizes plasminogen activation. 6,9,[11][12][13] In neurons, neurite outgrowth on amphoterin s...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Regulation of monocyte migration by amphoterin (HMGB1)

Rouhiainen

Kuja-Panula²,

Wilkman³

et al. 2004

Blood

228

194

View full text Add to dashboard Cite

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“…However, functional inactivation of RAGE, the putative receptor for amphoterin, either by dominant negative or antisense strategies, failed to prevent retinoic acid-induced neurite outgrowth, raising the possibility that amphoterin may interact with one or more other molecules to exert its effect on outgrowth. Indeed, previous reports have shown that amphoterin does in fact interact with other mole- cules, including syndecan (31) and sulfoglycolipids (32), although the relevance of these interactions in neurite outgrowth remains uncertain. The possibility of amphoterin interacting with an as yet unidentified molecule may not be ruled out.…”

Section: Discussionmentioning

confidence: 99%

Receptor for Advanced Glycation End Products Plays a More Important Role in Cellular Survival than in Neurite Outgrowth during Retinoic Acid-induced Differentiation of Neuroblastoma Cells

Sajithlal

Huttunen

Rauvala

et al. 2002

Journal of Biological Chemistry

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The receptor for advanced glycation end products (RAGE), a member of the immunoglobulin superfamily, is known to interact with amphoterin. This interaction has been proposed to play a role in neurite outgrowth and process elongation during neurodifferentiation. However, there is as yet no direct evidence of the relevance of this pathway to neurodifferentiation under physiological conditions. In this study we have investigated a possible role of RAGE and amphoterin in the retinoic acid-induced differentiation of neuroblastoma cells. The functional inactivation of RAGE by dominant negative and antisense strategies showed that RAGE is not required for process outgrowth or differentiation, although overexpression of RAGE accelerates the elongation of neuritic processes. Using the antisense strategy, amphoterin was shown to be essential for process outgrowth and differentiation, suggesting that amphoterin may interact with other molecules to exert its effect in this context. Interestingly, the survival of the neuroblastoma cells treated with retinoic acid was partly dependent on the expression of RAGE, and inhibition of RAGE function partially blocked the increase in anti-apoptotic protein Bcl-2 following retinoic acid treatment. Based on these results we propose that a combination therapy using RAGE blockers and retinoic acid may prove as a useful approach for chemotherapy for the treatment of neuroblastoma.

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“…Other, as yet unidentified, cues from the environment may act together with amphoterin to modulate transcription and translation of RAGE. In this context, other cell surface interaction sites for amphoterin, such as syndecam (32) and sulfoglycolipids (33), have been identified. It is possible that ligation of such sites may initiate the generation of other mediators important in enhancing RAGE expression.…”

Section: Sp1-binding Elements and Expression Of Ragementioning

confidence: 99%

Sp1-binding Elements in the Promoter of RAGE Are Essential for Amphoterin-mediated Gene Expression in Cultured Neuroblastoma Cells

Schmidt

1998

Journal of Biological Chemistry

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Receptor for AGE (RAGE) and the polypeptide amphoterin are highly expressed and co-localized in neurons of the developing central nervous system of the rat. In vitro, the interaction of amphoterin with neuronal RAGE induces neurite outgrowth. We tested the hypothesis that interaction of amphoterin with neuronal cells enhances RAGE expression, thereby providing a mechanism by which amphoterin-mediated regulation of RAGE might contribute to promotion of neurite growth and spreading. Incubation of cultured neuroblastoma cells with amphoterin resulted in increased transcription and translation of RAGE, a process largely inhibited in the presence of anti-RAGE IgG but not by nonimmune IgG. To begin to delineate molecular mechanisms underlying these findings, we identified multiple putative binding elements within the 5-flanking region of the RAGE gene for Sp1, a transcription factor that has been critically linked to the process of normal development. DNase I footprinting and electrophoretic mobility shift assays demonstrated multiple functional Sp1-binding sites within the region ؊245 to ؊40 of the RAGE promoter. Transient transfection of cultured SK-N-SH neuroblastoma cells with chimeric 5-deletion constructs linked to luciferase reporter revealed that the region containing Sp1-binding elements did not contribute uniquely to basal expression of the RAGE gene. Simultaneous mutation of the multiple Sp1-binding elements in this region did not affect basal promoter function; however, promoter responsiveness to amphoterin was markedly attenuated. These results point to Sp1-dependent mechanisms underlying amphoterin-mediated increases in RAGE expression in neuroblastoma cells and further link amphoterin-RAGE interaction to development of the nervous system.The receptor for AGE (RAGE), 1 a member of the immunoglobulin superfamily of cell-surface molecules, interacts with a range of ligands (1-2). In pathophysiologic circumstances, advanced glycation end products (AGEs) result from nonenzymatic glycation and oxidation of proteins and lipids and accumulate in conditions such as diabetes, renal failure, and amyloidoses (3-4). AGEs interact with RAGE in a manner linked to perturbation of vascular and inflammatory cells (5-9). In addition, RAGE interacts with amyloid ␤-peptide, consequences of which include enhanced neuronal and microglial oxidant stress and dysfunction (10 -11). These processes may be important in the pathogenesis of neurodegenerative disorders such as Alzheimer's disease. The expression of RAGE is strikingly enhanced in cells affected in settings associated with increased accumulation of AGEs and amyloid ␤-peptide (12-14). We recently identified that an important means by which the expression of RAGE might be regulated in inflammatorytype milieu such as diabetic vasculature and wounds, and Alzheimer brain, is via two functional NF-kB-binding elements located with the 5Ј-flanking region of the RAGE gene (15). Transfection of 5Ј-deletion luciferase reporter gene constructs containing two mutated NF-kB-binding s...

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Sulfoglycolipids bind to adhesive protein amphoterin (P30) in the nervous system

Cited by 47 publications

References 25 publications

Regulation of monocyte migration by amphoterin (HMGB1)

Regulation of monocyte migration by amphoterin (HMGB1)

Receptor for Advanced Glycation End Products Plays a More Important Role in Cellular Survival than in Neurite Outgrowth during Retinoic Acid-induced Differentiation of Neuroblastoma Cells

Sp1-binding Elements in the Promoter of RAGE Are Essential for Amphoterin-mediated Gene Expression in Cultured Neuroblastoma Cells

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