Arfaptin 1 inhibits ADP‐ribosylation factor‐dependent matrix metalloproteinase‐9 secretion induced by phorbol ester in HT 1080 fibrosarcoma cells

Ho, Wan‐Ting; Exton, John H.; Williger, Ben-Tsion

doi:10.1016/s0014-5793(03)00098-x

Cited by 12 publications

(6 citation statements)

References 28 publications

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“…We hypothesize that these shed vesicles may play a role in pericellular proteolytic activity under physiological and pathological conditions. Our data show that BFA treatment on reactive astrocytes inhibits MMP-2 and MMP-9 secretion with a concomitant intracellular increase, indicating a Golgidependant secretory pathway for these proteins, as described in N2a, endothelioma, and fibrosarcoma cells (Ho et al, 2003;Sbai et al, 2008;Taraboletti et al, 2000). Our findings are in line with previous reports demonstrating secretion of metalloproteinases as a component of intact membrane vesicles rather than as soluble enzymes, as shown in cultured malignant mouse melanoma (Zucker et al, 1987).…”

Section: Vesicular Secretion Of Mmp-2 Mmp-9 and Their Endogenous Insupporting

confidence: 92%

Differential vesicular distribution and trafficking of MMP‐2, MMP‐9, and their inhibitors in astrocytes

Sbai

Ould-Yahoui

Ferhat

et al. 2009

Glia

112

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Astrocytes play an active role in the central nervous system and are critically involved in astrogliosis, a homotypic response of these cells to disease, injury, and associated neuroinflammation. Among the numerous molecules involved in these processes are the matrix metalloproteinases (MMPs), a family of zinc-dependent endopeptidases, secreted or membrane-bound, that regulate by proteolytic cleavage the extracellular matrix, cytokines, chemokines, cell adhesion molecules, and plasma membrane receptors. MMP activity is tightly regulated by the tissue inhibitors of MMPs (TIMPs), a family of secreted multifunctional proteins. Astrogliosis in vivo and astrocyte reactivity induced in vitro by proinflammatory cues are associated with modulation of expression and/or activity of members of the MMP/TIMP system. However, nothing is known concerning the intracellular distribution and secretory pathways of MMPs and TIMPs in astrocytes. Using a combination of cell biology, biochemistry, fluorescence and electron microscopy approaches, we investigated in cultured reactive astrocytes the intracellular distribution, transport, and secretion of MMP-2, MMP-9, TIMP-1, and TIMP-2. MMP-2 and MMP-9 demonstrate nuclear localization, differential intracellular vesicular distribution relative to the myosin V and kinesin molecular motors, and LAMP-2-labeled lysosomal compartment, and we show vesicular secretion for MMP-2, MMP-9, and their inhibitors. Our results suggest that these proteinases and their inhibitors use different pathways for trafficking and secretion for distinct astrocytic functions.

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Section: Vesicular Secretion Of Mmp-2 Mmp-9 and Their Endogenous Insupporting

confidence: 92%

Differential vesicular distribution and trafficking of MMP‐2, MMP‐9, and their inhibitors in astrocytes

Sbai

Ould-Yahoui

Ferhat

et al. 2009

Glia

112

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“…49,50 However, in this study, both brefeldin A and monensin failed to block the rapid MMP-9 release induced by ATP or PMA over 30 minutes, suggesting that rapid MMP-9 release may occur via granule secretion, similar to membrane type 1 matrix metalloproteinase (MT1-MMP), which rapidly traffics to the plasma membrane via an unconventional brefeldin A-resistant pathway. 51 In support of this concept, it has been shown that B lymphocytes contain MMP-9 in a granular distribution.…”

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confidence: 55%

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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“…We tested if DN‐ARF6 and DN‐Rac1 can inhibit PMA‐induced ruffling. We also examined if DN‐ARF1 also inhibits the ruffling because of evidence that ARF1 is involved in some aspects of PMA signaling (Ho et al, 2003) and PLD activation (Shome et al, 1998). RhoA and Cdc42 were used as controls.…”

Section: Resultsmentioning

confidence: 99%

Studies of the roles of ADP‐ribosylation factors and phospholipase D in phorbol ester‐induced membrane ruffling

Hiroyama¹,

Exton²

2004

Journal Cellular Physiology

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In this study, we have explored the roles of ADP-ribosylation factors (ARFs), phospholipase D (PLD) isozymes, and arfaptins in phorbol ester (PMA)-induced membrane ruffling in HeLa cells. PMA stimulation induced ruffling and translocated cortactin to the plasma membrane. The cortactin translocation was inhibited by dominant negative (DN)-ARF6, DN-ARF1, and DN-Rac1, but not by DN-RhoA and DN-Cdc42. The inability of DN-forms of ARF6, ARF1, and Rac1 to affect PLD activity in response to PMA indicated that this enzyme was not activated via these small G proteins and that its activation was not essential for the induction of ruffling. Endogenous-ARF1, -ARF6, and -Rac1 existed in the ruffling region along with cortactin after PMA stimulation. DN-ARF1 had no effect on the ruffling induced by DA-ARF6 or DA-Rac1, and DN-ARF6 had no effect on that induced by DA-ARF1 or DA-Rac1. On the other hand DN-Rac1 suppressed the effect of DA-ARF6 but not that of DA-ARF1. These results suggest that PMA causes membrane ruffling via an ARF6-Rac1 pathway and also an ARF1 pathway operating in parallel. Overexpression of PLD1 and PLD2 inhibited PMA-induced cortactin translocation and actin-cortactin complex formation, supporting the view that these enzymes are not required for ruffling, but actually suppress it. We conclude that PMA-induced membrane ruffling is caused via ARF6-Rac1 and ARF1 pathways operating in parallel and that PLD may be inhibitory.

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Arfaptin 1 inhibits ADP‐ribosylation factor‐dependent matrix metalloproteinase‐9 secretion induced by phorbol ester in HT 1080 fibrosarcoma cells

Cited by 12 publications

References 28 publications

Differential vesicular distribution and trafficking of MMP‐2, MMP‐9, and their inhibitors in astrocytes

Differential vesicular distribution and trafficking of MMP‐2, MMP‐9, and their inhibitors in astrocytes

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

Studies of the roles of ADP‐ribosylation factors and phospholipase D in phorbol ester‐induced membrane ruffling

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