Different Signaling Pathways Stimulate a Disintegrin and Metalloprotease-17 (ADAM17) in Neutrophils during Apoptosis and Activation

Wang, Yue; Robertson, Janet; Walcheck, Bruce

doi:10.1074/jbc.m111.277087

Cited by 33 publications

(42 citation statements)

References 63 publications

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“…Nox4 involvement in ECM accumulation has been reported by several groups (2,6,8,22,38,44). Additionally, there is evidence that ROS activates ADAM17 (16,37,49). However, only one publication has shown upregulation of NADPH oxidases and subsequent ROS production, which results in shedding of known ADAM17 substrates (36).…”

Section: Discussionmentioning

confidence: 97%

ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice

Ford

Eid

Göõz

et al. 2013

American Journal of Physiology-Renal Physiology

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Ford BM, Eid AA, Göőz M, Barnes JL, Gorin YC, Abboud HE. ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice. Am J Physiol Renal Physiol 305: F323-F332, 2013. First published May 15, 2013 doi:10.1152/ajprenal.00522.2012.-Matrix protein accumulation is a prominent feature of diabetic nephropathy that contributes to renal fibrosis and decline in renal function. The pathogenic mechanisms of matrix accumulation are incompletely characterized. We investigated if the matrix metalloprotease a disintegrin and metalloprotease1 7 (ADAM17), known to cleave growth factors and cytokines, is activated in the kidney cortex of OVE26 type 1 diabetic mice and the potential mechanisms by which ADAM17 mediates extracellular matrix accumulation. Protein expression and activity of ADAM17 were increased in OVE26 kidney cortex. Using a pharmacological inhibitor to ADAM17, TMI-005, we determined that ADAM17 activation results in increased type IV collagen, Nox4, and NADPH oxidase activity in the kidney cortex of diabetic mice. In cultured mouse proximal tubular epithelial cells (MCTs), high glucose increases ADAM17 activity, Nox4 and fibronectin expression, cellular collagen content, and NADPH oxidase activity. These effects of glucose were inhibited when cells were pretreated with TMI-005 and/or transfected with small interfering ADAM17. Collectively, these data indicate a novel mechanism whereby hyperglycemia in diabetes increases extracellular matrix protein expression in the kidney cortex through activation of ADAM17 and enhanced oxidative stress through Nox enzyme activation. Additionally, our study is the first to provide evidence that Nox4 is downstream of ADAM17. ADAM17; Nox4; diabetic nephropathy; OVE26 mice; extracellular matrix DIABETIC NEPHROPATHY (DN) is characterized by diverse pathophysiological changes in the kidney including extracellular matrix (ECM) accumulation in glomeruli and tubulointerstitium (50). Matrix metalloproteases (MMPs) are a large and diverse family of proteins implicated in regulating ECM turnover and tissue remodeling. Several studies have suggested that metalloproteases contribute to ECM turnover in diabetes. However, relatively little information is available regarding the role of the a disintegrin and a metalloprotease, or ADAM, family of MMPs. Members of this family are modular membrane proteins involved in proteolytic processing or shedding of membrane-bound proteins and receptors (24,25,32,43). ADAM metalloproteases have adhesive and proteolytic properties that modulate cell signaling and biological responses of cells (5,12,19). ADAM17, a member of this ADAM family of MMPs, was originally described as the sheddase of tumor necrosis factor-␣, referred to as TNF␣-converting enzyme (4, 34). In addition, ADAM17 is also responsible for cleaving membrane-bound growth factors and receptors such as transforming growth factor-␣ (TGF␣), heparin-bound epidermal growth factor (HB-EGF), TNF receptor I and II, adhesion molecules, proinflammatory molecules, amyloid pr...

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Section: Discussionmentioning

confidence: 97%

ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice

Ford

Eid

Göõz

et al. 2013

American Journal of Physiology-Renal Physiology

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“…Cells were stained with antibodies against extracellular antigens and were then fixed and permeabilized before intracellular staining to detect IFN-g. A highly selective ADAM17 inhibitor (BMS566394) from Bristol-Myers Squibb (referred to as inhibitor 32) 23 was used at a 10 mM concentration, as previously described, 24 and was added to 1 3 10 6 /mL purified NK cells 30 minutes before testing. We also used a specific ADAM17 inhibitory monoclonal antibody (D1[A12], 6 mg/mL) generated by phage display that contains individual antibody variable domains to 2 distinct ADAM17-specific epitopes 25 to confirm ADAM17 specificity (kindly provided by Dr Gillian Murphy, University of Cambridge, UK).…”

Section: Cytokine Stimulationmentioning

confidence: 99%

NK cell CD16 surface expression and function is regulated by a disintegrin and metalloprotease-17 (ADAM17)

Romee

Foley

Lenvik

et al. 2013

Blood

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436

440

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• Activated NK cells loose CD16 (FcRgIII) and CD62L through a metalloprotease called ADAM17. • Inhibition of ADAM17enhances CD16 mediated NK cell function by preserving CD16 on the NK cell surface to enhance ADCC.The Fc receptor CD16 is present on essentially all CD56 dim peripheral blood natural killer (NK) cells. Upon recognition of antibody-coated cells it delivers a potent signal to NK cells, which eliminate targets through direct killing and cytokine production. Here we investigated the regulation of CD16 surface expression after NK cell activation. Cytokine activation and target cell stimulation led to marked decreases in CD16 expression. Activation of CD56 dim NK cells by cross-linking CD16 with antibodies resulted in a loss of CD16 and CD62L, which correlated with increased interferon-g production. A disintegrin and metalloprotease-17 (ADAM17) is shown to be expressed by NK cells, and its selective inhibition abrogated CD16 and CD62L shedding, and led to enhanced interferon-g production, especially when triggering was delivered through CD16. Fc-induced production of cytokines by NK cells exposed to rituximab-coated B cell targets was also enhanced by ADAM17 inhibition. This supports an important role for targeting ADAM17 to prevent CD16 shedding and improve the efficacy of therapeutic antibodies. Our findings demonstrate that over-activation of ADAM17 in NK cells may be detrimental to their effector functions by down-regulating surface expression of CD16 and CD62L. (Blood. 2013;121(18):3599-3608)

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“…It has been previously reported that MPTP opening induces mitochondria to produce large amounts of ROS [34][35][36][37][38]. Several reports have confirmed that ROS activate ADAM17 [39,40]. In order to demonstrate that A23187 induces mitochondria to produce ROS, we used MitoSOXÔ Red, an indicator of mitochondrial superoxide production, to detect mitochondrial ROS.…”

Section: A23187 Induces Elevation Of Mitochondrial Rosmentioning

confidence: 96%

“…It is known that the enhanced production of ROS is associated with ADAM17-mediated ectodomain shedding in various cells [40,43]. However, whether ROS are implicated in A23187induced GPIba ectodomain shedding remains unknown.…”

Section: A23187-induced Gpiba Ectodomain Shedding Is Partially Inhibimentioning

confidence: 99%

The role of mitochondrial permeability transition pore in regulating the shedding of the platelet GPIbα ectodomain

Wang¹,

Cai²,

Hu³

et al. 2013

Platelets

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Agonists induce platelet activation or apoptosis with concomitant shedding of the platelet receptor glycoprotein Ibα (GPIbα) ectodomain in a disintegrin and metalloproteinase 17 (ADAM17)-dependent mechanism. Mitochondrial permeability transition pore (MPTP) plays a pivotal role in platelet activation or apoptosis. However, its impact on ADAM17-mediated GPIbα ectodomain shedding remains unclear. Here, we aimed to test the hypothesis that MPTP regulates ADAM17-dependent GPIbα ectodomain shedding. We showed that calcium ionophore A23187- or thrombin plus collagen-induced GPIbα ectodomain shedding was partially inhibited by a MPTP inhibitor, and a MPTP potentiator promoted A23187-induced GPIbα cleavage. Furthermore, A23187-induced elevation of mitochondrial Ca(2+) levels was blocked by the mitochondrial calcium uniporter (MCU) inhibitor Ru360 or treatment with the membrane-permeable Ca(2+) chelator BAPTA-AM. We also demonstrated that an increase in mitochondrial Ca(2+) levels triggered MPTP opening, as revealed by the examination of mitochondrial inner transmembrane potential depolarization. In addition, A23187 induced-mitochondrial reactive oxygen species (ROS) generation was blocked by the MPTP inhibitor or by treatment with the mitochondria-targeted ROS scavenger. Lastly, A23187-induced GPIbα shedding was partially blocked by inhibitors of either ROS or calpain, and was completely inhibited when platelets were exposed to both inhibitors. Therefore, these observations indicate that MPTP opening triggered mitochondrial ROS production, which plays an important role in regulating ADAM17-mediated shedding of the GPIbα ectodomain in A23187-treated platelets.

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Different Signaling Pathways Stimulate a Disintegrin and Metalloprotease-17 (ADAM17) in Neutrophils during Apoptosis and Activation

Cited by 33 publications

References 63 publications

ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice

ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice

NK cell CD16 surface expression and function is regulated by a disintegrin and metalloprotease-17 (ADAM17)

The role of mitochondrial permeability transition pore in regulating the shedding of the platelet GPIbα ectodomain

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