Up-regulation of MMP-2 and MMP-9 Leads to Degradation of Type IV Collagen During Skeletal Muscle Reperfusion Injury; Protection by the MMP Inhibitor, Doxycycline

Roach, Denise; Fitridge, Robert; Laws, Peter; Millard, Susan; Varelias, Antiopi; Cowled, Prue

doi:10.1053/ejvs.2002.1598

Cited by 110 publications

(98 citation statements)

References 40 publications

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“…Ischemia and reperfusion are recognized as being involved in both acute and chronic rejection [20]. Recent studies have reported that ischemia and reperfusion increase the expression and activity of MMP-2 and MMP-9 in rat muscle and lung, but not in the kidney [23,331. Thus, our results are in agreement with these studies and indicate that ischemia/ reperfusion did not contribute to the changes in MMP activity measured during acute rejection.…”

Section: Discussionmentioning

confidence: 99%

Modulation of matrix gelatinases and metalloproteinase-activating process in acute kidney rejection

et al. 2003

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Changes in matrix metalloproteinase (MMP) activities would contribute to the accumulation of extracellular matrix during acute kidney allograft rejection. MMP-2 and MMP-9 and other gelatinolytic activities were examined in the rejected graft and the urine of a rat model of acute kidney rejection (orthotopic allotransplantation from a Buffalo donor to a Wistar-Furth recipient) by either zymography or fluorescence assay. MMP-2, membrane type 1 (MT1)-MMP, and tissue inhibitor of metalloproteinase (T1MP)-2 were also examined by immunodetection. The proMMP-2 activity and protein level increased in the graft during rejection when compared with normal Buffalo kidney, whereas activated MMP-2 decreased. TIMP-2 protein levels were markedly decreased and MTI-MMP proteolytic fragments (4440 kDa) were undetectable. This suggests an altered MTl-MMP-dependent processing of proMMP-2 into active MMP-2 due to a diminished TIMP-2 level in acute kidney rejection. In the urine the overall gelatinolytic activity decreased considerably, although activity associated with an as yet unidentified 78-kDa protein appeared 6 days after transplantation.

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Section: Discussionmentioning

confidence: 99%

Modulation of matrix gelatinases and metalloproteinase-activating process in acute kidney rejection

et al. 2003

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“…The intensity of fluorescence was digitized and measured using Scion Image TM to compare the relative intensity of fluorescence between samples as described by Roach. 17 …”

Section: Immunohistochemistymentioning

confidence: 99%

Matrix metalloproteinase‐2 expression and promoter/enhancer activity in skeletal muscle atrophy

Skittone

Liu

Tseng

et al. 2007

Journal Orthopaedic Research

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Matrix metalloproteinase-2 (MMP-2) appears to be the dominant MMP activated during skeletal muscle atrophy. However, little is known about cell-specific regulatory mechanisms of MMP-2 transcription in vivo. In this study, we used a mouse model of muscle atrophy induced by complete Achilles tendon transection. Time-dependent muscle weight loss, nuclei density reduction, and extracellular matrix degeneration were observed consistently after Achilles tendon transection. Increased MMP-2 expression was confirmed at the mRNA and protein level. Experiments using transgenic mice with a MMP-2 promoter/enhancer reporter construct demonstrated markedly increased MMP-2 promoter/enhancer activity in atrophic skeletal muscle. Tissue-specific upregulation of MMP-2 promoter activity was observed not only in myocytes, but also in blood vessels, nerve, and fascia. The transcription factors c-Jun and FosB were expressed at high levels in atrophic muscle, suggesting a role in MMP-2 upregulation. These findings show that increased MMP-2 activity in disused atrophic muscle and supporting tissues is regulated, at least in part, by increased MMP-2 promoter/enhancer activity. ß

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“…In contrast, MMP-9 shows none or a very modest basal expression, but its promoter region contains a variety of response elements sensitive to a wide range of growth factors and cytokines (33). MMP-9 has been proposed to affect general collagen turnover in skeletal muscle and in vitro models of disease (7,9,28). It might also to be a regulator of growth factor bioavailability via proteolytic release (8,21).…”

mentioning

confidence: 99%

“…Physical exercise is a complex process constituting several factors that could affect the expression levels of MMP-2 and MMP-9 in skeletal muscle, such as local ischemia and increases in muscle stretching; in shear stress; and in the wall tension of blood vessels (2,24,28). Despite the established importance of ECM remodeling in the skeletal muscle during adaptation to exercise and the central role of MMPs in these processes, MMP levels in exercising skeletal muscle have been largely overlooked.…”

mentioning

confidence: 99%

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

Rullman¹,

Norrbom²,

Strömberg³

et al. 2009

Journal of Applied Physiology

106

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Up-regulation of MMP-2 and MMP-9 Leads to Degradation of Type IV Collagen During Skeletal Muscle Reperfusion Injury; Protection by the MMP Inhibitor, Doxycycline

Cited by 110 publications

References 40 publications

Modulation of matrix gelatinases and metalloproteinase-activating process in acute kidney rejection

Modulation of matrix gelatinases and metalloproteinase-activating process in acute kidney rejection

Matrix metalloproteinase‐2 expression and promoter/enhancer activity in skeletal muscle atrophy

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

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