Interleukin-1β increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCα/β<sub>1</sub> and MAPKs

Mountain, Deidra J.H.; Singh, Mahipal; Menon, Bindu; Singh, Krishna

doi:10.1152/ajpcell.00161.2006

Cited by 93 publications

(77 citation statements)

References 59 publications

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“…We reported previously that basement membrane degrading enzyme, matrix metalloproteinase-2 (MMP-2), is downregulated by shear stress in a p38 dependent manner (Milkiewicz et al, 2006). Conversely, ERK1/2 activation increases MMP-2 production (Boyd et al, 2005;Mountain et al, 2007). ERK1/2 also promotes proliferation in endothelial cells (Pages et al, 2000;Pages et al, 1993), and minimal proliferation occurs during shear stress-mediated angiogenesis (Zhou et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

Gee

Milkiewicz

Haas

2009

Journal Cellular Physiology

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Increased capillary shear stress induces angiogenesis in skeletal muscle, but the signaling mechanisms underlying this response are not known. We hypothesize that shear stress-dependent activation of vascular endothelial growth factor receptor 2 (VEGFR2) causes p38 and ERK1/2 phosphorylation, which contribute to shear stress-induced angiogenesis. Skeletal muscle microvascular endothelial cells were sheared (12 dynes/cm 2 , 0.5-24 hours). VEGFR2-Y1214 phosphorylation increased in response to elevated shear stress and VEGF stimulation. p38 and ERK1/2 phosphorylation increased at 2 hours of shear stress, but only p38 remained phosphorylated at 6 and 24 hours of shear stress. VEGFR2 inhibition abrogated p38, but not ERK1/2 phosphorylation. VEGF production was increased in response to shear stress at 6 hours, and this increased production was abolished by p38 inhibition. Male Sprague-Dawley rats were administered prazosin (50 mg/L drinking water, 1, 2, 4 or 7 days) to induce chronically elevated capillary shear stress in skeletal muscle. In some experiments, mini-osmotic pumps were used to dispense p38 inhibitor SB203580 or its inactive analog SB202474, to the extensor digitorum longus (EDL) of control and prazosin treated rats. Immunostaining and Western blotting showed increases in p38 phosphorylation in capillaries from rats treated with prazosin for 2 days but returned to basal levels at 4 and 7 days. p38 inhibition abolished the increase in capillary to muscle fibre ratio seen after 7 days of prazosin treatment. Our data suggest that p38 activation is necessary for shear stress-dependent angiogenesis.

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Section: Discussionmentioning

confidence: 99%

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

Gee

Milkiewicz

Haas

2009

Journal Cellular Physiology

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“…The outcome of myocardial infarction (MI) closely depends on a adequate ventricular architecture remodeling. The process is mainly driven by the deposition of ECM macromolecules in a tightly regulated manner in order to prevent stiffness and/or other pathological conditions that often impairs myocardial viscoelasticity ending up with a heart failure (Mountain et al, 2007). The role of MMP-2 in cardiac tissue encompasses critical steps in heart and cardiovascular system development during embryogenesis: nonetheless, the enzyme is well represented in pathological conditions that require ECM remodeling and restoration of cardiomyocytes homeostasis (Linask et al, 2005).…”

Section: Biological Aspectsmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

210

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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“…All the activated MMPs (including MMP2 and MMP9) are specifically inhibited by endogenous inhibitors, tissue inhibitor of metalloproteinases (TIMPs; Visse & Nagase 2003, Kessenbrock et al 2010). MMP2 and MMP9 can be induced in multiple cells by inflammatory cytokines including interleukin 1b (IL1b (IL1B)) and tumor necrosis factor a (TNFa; Mackay et al 1992, Li et al 1999, Siwik et al 2000, Jones et al 2005, Redondo-Munoz et al 2006, Mountain et al 2007. Our pervious study showed that IL1b increased the permeability of the human umbilical vein endothelial cell (HUVEC) monolayer by damaging adherens junctions and enlarging the junctions cleft width (Yuan et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Melatonin inhibits IL1β-induced MMP9 expression and activity in human umbilical vein endothelial cells by suppressing NF-κB activation

Qin

Lu²,

Li³

et al. 2012

Journal of Endocrinology

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Matrix metalloproteinases (MMPs) have been involved in inflammatory and degradative processes in pathologic conditions. The purpose of this study was to investigate the protective effect of melatonin in human umbilical vein endothelial cell (HUVEC) monolayer permeability and the regulation of MMP9 induced by interleukin 1b (IL1b (IL1B)) in HUVECs. Protection studies were carried out with melatonin, a well-known antioxidant and antiinflammatory molecule. MMP9 expression was increased with IL1b induction in HUVECs. Melatonin showed a barrier-protective role by downregulation of MMP9 and upregulation of tissue inhibitor of metalloproteinase-1 expression in HUVECs. Meanwhile, melatonin also decreased sodium fluorescein permeability and counteracted the downregulation of vascular endothelial cadherin and occludin expression in HUVECs. During inflammatory stimulus, nuclear factor-kB (NF-kB) plays a significant role in regulating MMP genes expression, thus the function of NF-kB in HUVECs' barrier disruption was investigated. IL1b induced nuclear translocation of NF-kB in HUVECs and regulated MMP9 expression. However, NF-kB translocation into the nucleus was inhibited significantly by melatonin. Our results show that melatonin decreases the permeability of monolayer endothelial cell induced by IL1b. At the same time, melatonin decreased the expression and activity of MMP9 by a NF-kB-dependent pathway in HUVECs induced by IL1b.

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Interleukin-1β increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCα/β₁ and MAPKs

Abstract: Mountain DJ, Singh M, Menon B, Singh K. Interleukin-1␤ increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKC␣/␤ 1 and MAPKs.

Cited by 93 publications

References 59 publications

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Melatonin inhibits IL1β-induced MMP9 expression and activity in human umbilical vein endothelial cells by suppressing NF-κB activation

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Interleukin-1β increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCα/β1 and MAPKs

Abstract: Mountain DJ, Singh M, Menon B, Singh K. Interleukin-1␤ increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKC␣/␤ 1 and MAPKs.

Cited by 93 publications

References 59 publications

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

p38 MAPK activity is stimulated by vascular endothelial growth factor receptor 2 activation and is essential for shear stress‐induced angiogenesis

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Melatonin inhibits IL1β-induced MMP9 expression and activity in human umbilical vein endothelial cells by suppressing NF-κB activation

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Interleukin-1β increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCα/β₁ and MAPKs