Activation of Macrophage Promatrix Metalloproteinase-9 by Lipopolysaccharide-Associated Proteinases

Min, Danqing; Moore, Anthony G.; Bain, Michael; Breit, Samuel N.; Lyons, J. Guy

doi:10.4049/jimmunol.168.5.2449

Cited by 32 publications

(30 citation statements)

References 35 publications

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“…18 However, maturation of IL-1␤ requires a large K ϩ efflux from the cell either via the P2X 7 pathway or via the K ϩ ionophore nigericin, 19 while MMP-9 precursor is activated in vivo by other members of the MMP family such as MMP-3 (stromelysin) 10 or by variant proteinases such as LPSassociated proteinases. 11 Furthermore, LPS activation of monocytes is required for ATP-induced IL-1␤ or IL-18 release but not for ATP-induced MMP-9 release, making the latter applicable to PBMCs (1 ϫ 10 7 /mL) with wild-type P2X7 receptors were pretreated with or without brefeldin A (10 g/mL), monensin (5 g/mL), or cycloheximide (50 g/mL) for 60 minutes in NaCl medium with 0.1 mM CaCl2 and washed once. Cells then were resuspended at 2 ϫ 10 7 /mL in the same medium with the same concentration of inhibitors, followed by incubation with or without 1 mM ATP (gray bar) or 100 nM PMA (dark gray bar) at 37°C for 30 minutes.…”

Section: Discussionmentioning

confidence: 99%

“…8 Besides the inhibitory effect of TIMP-1, MMP-9 activity also is regulated at various levels from production to secretion, including transcription of the gene by cytokines such as tumor necrosis factor-␣ (TNF-␣) and interleukin 1␤ (IL-1␤) or by cellular interactions such as cell-cell contact between monocytes and activated T lymphocytes, activation of pro-enzyme by other MMPs, 9,10 or by variant proteinases such as lipopolysaccharide (LPS)-associated proteinases. 11 The P2X 7 receptor is a ligand-gated cation channel activated by extracellular adenosine triphosphate (ATP) and highly expressed on monocytes, macrophages, and lymphocytes. Activation of this receptor by exposure to extracellular ATP opens a cation selective channel that allows Ca 2ϩ and Na ϩ influx and K ϩ efflux.…”

Section: Introductionmentioning

confidence: 99%

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Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor

Wiley

2006

Blood

147

117

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Matrix metalloproteinase-9 (MMP-9) activity is required for inflammatory response, leukocyte recruitment, and tumor invasion. There is increasing evidence suggesting that the P2X 7 receptor of mononuclear cells, which is activated by extracellular adenosine triphosphate (ATP), is involved in inflammatory responses. In this study, ATP caused a rapid release of MMP-9 and a moderate decrease in tissue inhibitor of metalloproteinase 1 (TIMP-1) release from human peripheral-blood mononuclear cells (PBMCs) over a 30-minute time course. The release was time-and dose-dependent and dissociated from ATP-induced cell death. BzATP, which is the most potent agonist for the P2X 7 receptor, also caused a similar effect at a lower dosage. ATP-induced MMP-9 release was inhibited by the P2X 7 receptor antagonists periodate oxidized ATP and KN-62, or by calcium chelators, as well as by a loss-offunction polymorphism in the P2X 7 receptor, but not by brefeldin A, monensin, or cycloheximide, or by anti-tumor necrosis factor-␣ (TNF-␣) or anti-interleukin-1␤ (IL-1␤) monoclonal antibodies. Results from purified subsets of PBMCs showed monocytes were the major source for MMP-9 and TIMP-1 release, and ATP remained effective in purified monocyte and T-cell populations. These observations suggest a novel role for P2X 7 as a pro-inflammatory receptor involved in rapid MMP-9 release and leukocyte recruitment. IntroductionSynthesis and secretion of matrix metalloproteinases (MMPs) have been demonstrated for all cells of the immune and hemopoietic lineages as well as fibroblasts and endothelial cells. A wide variety of neoplastic cells also have been shown to secrete MMPs, and these MMPs are considered to participate in the metastatic dissemination of tumors 1 and cyclic changes in the endometrium. 2 Other studies have shown that MMPs are involved in physiologic processes such as angiogenesis wound repair 3 and the inflammatory response. 4 Among the members of the MMP family, the gelatinases A and B (MMP-2 and 9) are important, since both can produce proteolytic degradation of type 4 collagen, which is the principal component of basement membrane. Many studies have shown that MMP-2 is secreted constitutively, while secretion of MMP-9 is regulated by inflammatory stimuli that differ according to cell type. 5 Like the other MMPs, gelatinases are produced in a latent form containing a prodomain, which requires activation by a cysteine-switch mechanism. 6 Both gelatinases form tight noncovalent and stable complexes with tissue inhibitor of metalloproteinases (TIMPs). Thus, pro-MMP-2 (72 kDa) specifically binds TIMP-2, 7 whereas pro-MMP-9 (92 kDa) specifically binds TIMP-1, which plays a major role in regulating MMP-9 activity. 8 Besides the inhibitory effect of TIMP-1, MMP-9 activity also is regulated at various levels from production to secretion, including transcription of the gene by cytokines such as tumor necrosis factor-␣ (TNF-␣) and interleukin 1␤ (IL-1␤) or by cellular interactions such as cell-cell contact between monocytes and activate...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor

Wiley

2006

Blood

147

117

View full text Add to dashboard Cite

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“…50 Lipopolysaccharide-associated proteinases have the ability to activate MMP-9 zymogens in vitro. 51 In addition, lipopolysaccharide produces chemotactic gradients that will attract neutrophils to the damaged intestine, further enhancing the activity of MMP-9. 52 Intestinal lumen-derived lipopolysaccharide and pancreatic trypsin could thus serve as cofactors in the recruitment and activation of MMP-9 in intestinal I/R.…”

Section: Discussionmentioning

confidence: 99%

Pancreatic Trypsin Increases Matrix Metalloproteinase-9 Accumulation and Activation during Acute Intestinal Ischemia-Reperfusion in the Rat

Rosario¹,

Waldo²,

Becker³

et al. 2004

The American Journal of Pathology

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Ischemia-reperfusion of the intestine produces a set of inflammatory mediators, the origin of which has recently been shown to involve pancreatic digestive enzymes. Matrix metalloproteinase-9 (MMP-9) participates in a variety of inflammatory processes including myocardial, hepatic, and pancreatic ischemiareperfusion. In the present study, we explore the role of neutrophil-derived MMP-9 in acute intestinal ischemia-reperfusion and its interaction with pancreatic trypsin. Male Sprague-Dawley rats were subjected to 45 minutes of superior mesenteric arterial occlusion followed by 90 minutes of reperfusion. In situ zymography of the proximal jejunum reveals increased gelatinase activity in the intestinal wall after ischemiareperfusion. Gel electrophoresis zymography and immunofluorescence co-localization suggests that this gelatinase activity is derived from MMP-9 released from infiltrating neutrophils. The role of intraluminal trypsin in this process was investigated using an in vivo isolated jejunal loop model of intestinal ischemia-reperfusion. Trypsin increased the inflammatory response after reperfusion, with an augmented neutrophil infiltration of the intestinal wall. Furthermore, trypsin stimulated a rapid conversion of neutrophil-released proMMP-9 into the lower molecular weight enzymatically active MMP-9. This process represents a powerful in vivo pathophysiological mechanism for trypsin-induced MMP-9 activation and is likely to play a central role in the development of acute intestinal inflammation and shock. Intestinal ischemia-reperfusion (I/R) is a localized pathology that often leads to multi-organ dysfunction and shock.

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“…The human promonocytic leukemic cell line (THP1 cells; ATCC, Manassas, VA) were routinely cultured under serumfree conditions containing 0.1% BSA (16). Primary cultures of human fetal mesangial cells were obtained from isolated glomeruli, maintained in RPMI medium containing 10% fetal calf serum, and used between the third and fourth passage (13).…”

Section: Reagentsmentioning

confidence: 99%

“…To examine the effect of coculture of THP1 cells and mesangial cells on degradative activity, the CM was assayed using a solution-phase fluorescent assay as previously described (16).…”

Section: Measurement Of Mmp-9 Gene Expression By Real-time Pcrmentioning

confidence: 99%

Mesangial cell-derived factors alter monocyte activation and function through inflammatory pathways: possible pathogenic role in diabetic nephropathy

Min

Lyons

Bonner

et al. 2009

American Journal of Physiology-Renal Physiology

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Mesangial cell-derived factors alter monocyte activation and function through inflammatory pathways: possible pathogenic role in diabetic nephropathy. Am J Physiol Renal Physiol 297: F1229 -F1237, 2009. First published September 9, 2009 doi:10.1152/ajprenal.00074.2009.-Infiltration of macrophages to the kidney is a feature of early diabetic nephropathy. For this to happen monocytes must become activated, migrate from the circulation, and infiltrate the mesangium. This process involves degradation of extracellular matrix, a process mediated by matrix metalloproteinases (MMPs). In the present study we investigate the expression of proinflammatory cytokines TNF-␣, IL-6, and MMP-9 in glomeruli of control and diabetic rodents and use an in vitro coculture system to examine whether factors secreted by mesangial cells in response to a diabetic milieu can induce monocyte MMP-9 expression and infiltration. After 8 wk of diabetes, the glomerular level of TNF-␣, IL-6, and macrophage number and colocalization of MMP-9 with macrophage were increased (P Ͻ 0.01). Coculture of THP1 monocytes and glomerular mesangial cells in 5 or 25 mM glucose increased MMP-9 (5 mM: 65% and 25 mM: 112%; P Ͻ 0.05) and conditioned media degradative activity (5 mM: 30.0% and 25 mM: 33.5%: P Ͻ 0.05). These effects were reproduced by addition of mesangial cell conditioned medium to THP1 cells. High glucose (25 mM) increased TNF-␣, IL-6, and monocyte chemoattractant protein-1 in mesangial cell conditioned medium. These cytokines all increased adhesion and differentiation of THP1 cells (P Ͻ 0.05), but only TNF-␣ and IL-6 increased MMP-9 expression (50-and 60-fold, respectively; P Ͻ 0.05). Our results show that mesangial cellsecreted factors increase monocyte adhesion, differentiation, MMP expression, and degradative capacity. High glucose could augment these effects by increasing mesangial cell proinflammatory cytokine secretion. This mesangial cell-monocyte interaction may be important in activating monocytes to migrate from the circulation to the kidney in the early stages of diabetic nephropathy. matrix metalloproteinases; matrix degradation; cell adhesion and infiltration; inflammation response

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Activation of Macrophage Promatrix Metalloproteinase-9 by Lipopolysaccharide-Associated Proteinases

Cited by 32 publications

References 35 publications

Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor

Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor

Pancreatic Trypsin Increases Matrix Metalloproteinase-9 Accumulation and Activation during Acute Intestinal Ischemia-Reperfusion in the Rat

Mesangial cell-derived factors alter monocyte activation and function through inflammatory pathways: possible pathogenic role in diabetic nephropathy

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