Matrix metalloproteinase activity is enhanced during corneal wound repair in high glucose condition

Akiba, Kiyoshi; Noguchi, Takayasu; Ohmura, Takafumi; Takahashi, Ryoki; Ezure, Youji; Ohara, Kunitoshi; Zieske, James D.

doi:10.1076/0271-3683(200008)21:2;1-v;ft608

Cited by 10 publications

(8 citation statements)

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“…This result is in line with other findings showing that MMP activity was higher in aortic homogenates and plasma in rat models of diabetes (25). High glucose levels have also been shown to raise MMP activity in cultured cells (25,26). Nevertheless, despite this raise in MMP content, the quantity of cleaved collagen, reflecting the proteolytic process, was reduced in diabetic animals.…”

Section: Discussionsupporting

confidence: 80%

Blockade of advanced glycation end-product formation restores ischemia-induced angiogenesis in diabetic mice

Tamarat

Silvestre

Huijberts

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

147

113

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We hypothesized that formation of advanced glycation end products (AGEs) associated with diabetes reduces matrix degradation by metalloproteinases (MMPs) and contributes to the impairment of ischemia-induced angiogenesis. Mice were treated or not with streptozotocin (40 mg͞kg) and streptozotocin plus aminoguanidine (AGEs formation blocker, 50 mg͞kg). After 8 weeks of treatment, hindlimb ischemia was induced by right femoral artery ligature. Plasma AGE levels were strongly elevated in diabetic mice when compared with control mice (579 ؎ 21 versus 47 ؎ 4 pmol͞ml, respectively; P < 0.01). Treatment with aminoguanidine reduced AGE plasma levels when compared with untreated diabetic mice (P < 0.001). After 28 days of ischemia, ischemic͞nonischemic leg angiographic score, capillary density, and laser Doppler skin-perfusion ratios were 1.4-, 1.5-, and 1.4-fold decreased in diabetic mice in reference to controls (P < 0.01). Treatment with aminoguanidine completely normalized ischemiainduced angiogenesis in diabetic mice. We next analyzed the role of proteolysis in AGE formation-induced hampered neovascularization process. After 3 days of ischemia, MMP-2 activity and MMP-3 and MMP-13 protein levels were increased in untreated and aminoguanidine-treated diabetic mice when compared with controls (P < 0.05). Despite this activation of the MMP pathway, collagenolysis was decreased in untreated diabetic mice. Conversely, treatment of diabetic mice with aminoguanidine restored collagenolysis toward levels found in control mice. In conclusion, blockade of AGE formation by aminoguanidine normalizes impaired ischemia-induced angiogenesis in diabetic mice. This effect is probably mediated by restoration of matrix degradation processes that are disturbed as a result of AGE accumulation.

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Section: Discussionsupporting

confidence: 80%

Blockade of advanced glycation end-product formation restores ischemia-induced angiogenesis in diabetic mice

Tamarat

Silvestre

Huijberts

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

147

113

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“…It has been reported that glucose at concentrations up to 17.5 mM has stimulatory effects on human corneal epithelial cell migration, adhesion, and proliferation, but concentrations above 31 mM have an inhibitory effect. 34,35 To eliminate a possible competitive effect of glucose present in the culture medium with the effect of CMC on the HCLE cell migration, cell adhesion, and proliferation and scratch-wound closure, we included a control group of culture medium containing 12.5 mM glucose but with no CMC in all our assays.…”

Section: Iovsmentioning

confidence: 99%

Carboxymethylcellulose Binds to Human Corneal Epithelial Cells and Is a Modulator of Corneal Epithelial Wound Healing

Garrett

Simmons

et al. 2007

Invest. Ophthalmol. Vis. Sci.

128

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“…There are many external cues which can induce various transcription factors (TFs) to act on the MMP‐9 promoter, though evidence linking the extracellular cues to the intracellular pathways is scarce. In cell culture models, MMP‐9 production has been shown to be regulated by external factors such as osmolarity shifts (Li et al, 2004), high glucose (Takahashi et al, 2000), plating density (Bargagna‐Mohan et al, 1999), phorbol esters (Fini et al, 1995), and several growth factors and cytokines including interleukin 1β (IL‐1β) (Li et al, 2001), tumor necrosis factor‐alpha (TNF‐α) (Li et al, 2001), transforming growth factor β (TGF‐β) (Li et al, 2001), basic fibroblast growth factor (FGF‐2) (Mohan et al, 2000), and platelet activating factor (PAF) (Tao et al, 1995). Additionally, hyaluronan and several sulfated GAGs have been shown to stimulate MMP‐9 in both dermal and corneal explants (Isnard et al, 2003).…”

mentioning

confidence: 99%

Cytokines and signaling pathways regulating matrix metalloproteinase‐9 (MMP‐9) expression in corneal epithelial cells

Gordon

Ledee

Feuer

et al. 2009

Journal Cellular Physiology

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Matrix metalloproteinase-9 (MMP-9) is a well known regulator and effecter of many cellular processes including wound healing. In the cornea, either too much or too little MMP-9 can be detrimental to overall wound repair. We investigated the secreted factors as well as the intracellular signaling pathways and the promoter sequences that mediate this regulation. Primary culture rabbit corneal epithelial cells were treated with various cytokines alone or in different combinations and MMP-9 induction was assessed by gel zymography. Pharmacological inhibitors were used to determine the intracellular signaling pathways induced by the cytokines tested and deletion promoter constructs were created to determine the regions of the MMP-9 promoter involved in the cytokine regulation, thereby assessing the exact transcription factors binding the MMP-9 promoter. We found that two cytokine families, TGF-β and IL-1, act additively in an isoform non-specific manner to induce MMP-9 in this cell type. Our data suggest TGF-β mediated MMP-9 induction may be regulated by the NF-kB, Smad3, and JNK pathways, whereas the IL-1β mediated induction may be regulated by the NF-kB and p38 pathways. Inhibition of the p38, NF-kB, or JNK pathways significantly reduced, but did not abrogate, basal MMP-9 levels. Inhibition of the ERK pathway did not have an effect on MMP-9 mediated expression in either the treated or untreated co-transfected cells.

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Matrix metalloproteinase activity is enhanced during corneal wound repair in high glucose condition

Abstract: MMP activity was enhanced in healing corneal epithelium, both in in vitro and in vivo diabetic models, suggesting its involvement in diabetic keratopathy.

Cited by 10 publications

References 0 publications

Blockade of advanced glycation end-product formation restores ischemia-induced angiogenesis in diabetic mice

Blockade of advanced glycation end-product formation restores ischemia-induced angiogenesis in diabetic mice

Carboxymethylcellulose Binds to Human Corneal Epithelial Cells and Is a Modulator of Corneal Epithelial Wound Healing

Cytokines and signaling pathways regulating matrix metalloproteinase‐9 (MMP‐9) expression in corneal epithelial cells

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