Monocyte Membrane Type 1-Matrix Metalloproteinase

Shankavaram, Uma; Lai, Wan-Ching; Netzel‐Arnett, Sarah; Mangan, Paul R.; Ardans, Jeanette A.; Caterina, Nancy C.M.; Stetler-Stevenson, William G.; Birkedal‐Hansen, Henning; Wahl, Larry M.

doi:10.1074/jbc.m009562200

Cited by 72 publications

(18 citation statements)

References 44 publications

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“…11,33) Shankavaram et al also demonstrated that induction of monocyte MT1-MMP is regulated through the PG E 2 /cAMP pathway, indicating the important role of COX-2 in the regulation of MT1-MMP. 14) Taken together, these facts imply that MT1-MMP production through the COX-2 dependent pathway may also promote plaque instability, as does the production of other MMPs, including MMP-2 and MMP-9. 12,20) In our WHHLMI rabbits, relatively strong COX-2 staining was found also in more stable atherosclerotic lesions, such as neointimal and collagen-rich lesions (Figs.…”

Section: Distribution Of Cox-2 In Relation To Mt1-mmp Distributionmentioning

confidence: 95%

“…4,31) On the other hand, it is reported that MT1-MMP provided by macrophages may play a significant role in the activation of MMP-2 produced by other cells, such as SMCs. 11,14) MMP-2 is constitutively expressed in medial SMCs. 31) These facts may be another explanation for the uncoupling of MT1-MMP and MMP-2 distribution in the medial regions (SMCs).…”

Section: Distribution Of Mt1-mmp/mmp-2mentioning

confidence: 99%

“…1,12,13) Recently, Shankavaram et al demonstrated that induction of monocyte MT1-MMP is also regulated through the PG E 2 /cAMP pathway. 14) These findings indicate the involvement of cyclooxygenases (COXs), rate-limiting enzymes in the conversion of arachidonic acid into PGs and thromboxanes, in the regulation of MMP biosynthesis. 1,15) To date, at least 2 distinct isoforms of the COXs-a constitutive form (COX-1) and an inducible isoform (COX-2)-and several of their variants have been discovered.…”

mentioning

confidence: 97%

“…Most soluble MMPs, including MMP-2 and MMP-9, are released from cells as zymogens and require extracellular posttranslational cleavage to gain biological activity. 3,8) A membrane-bound MMP, membrane type-1 MMP (MT1-MMP or MMP- 14), has been demonstrated to mediate the activation of pro-MMP-2 to active MMP-2 on the cell surface. 8,9) The expression of MT1-MMP has also been found within human atherosclerotic plaques.…”

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confidence: 99%

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Distribution Profiles of Membrane Type-1 Matrix Metalloproteinase (MT1-MMP), Matrix Metalloproteinase-2 (MMP-2) and Cyclooxygenase-2 (COX-2) in Rabbit Atherosclerosis: Comparison with Plaque Instability Analysis

Kuge

Takai

Ishino

et al. 2007

Biological & Pharmaceutical Bulletin

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Our current understanding of the pathophysiology of atherosclerosis suggests the involvement of complex mechanisms that go beyond mere lipid storage disorders.1,2) It is of great importance to investigate causative factors in the destabilization of atherosclerotic plaques, which should help develop new therapeutic and diagnostic (imaging) agents of atherosclerosis, leading to the establishment of novel therapeutic strategies for preventing acute coronary syndromes and stroke.To date, several factors, including enhanced inflammatory responses and expression of matrix metalloproteinases (MMPs), have been suggested to play important roles in the destabilization of atherosclerotic plaques.1-4) Plaques prone to rupture are morphologically characterized by a thin fibrous cap overlying a large lipid core. MMPs have been shown to degrade extracellular matrix (ECM) that constitutes the fibrous cap of the plaques, resulting in the destabilization of atherosclerotic plaques. [3][4][5] Increased expression of MMP-2 and MMP-9 has been demonstrated within human atherosclerotic lesions and critically implicated in plaque rupture.5-7) MMP-2 and MMP-9 are known to cleave native type IV, V, VII, and X collagens and elastin, as well as the products of collagens types I, II, and III after proteolysis by collagenases, such as MMP-1 and MMP-13, and are considered to be involved in plaque instability.3) The MMPs can be divided into two groups: soluble MMPs and membranebound MMPs. Most soluble MMPs, including MMP-2 and MMP-9, are released from cells as zymogens and require extracellular posttranslational cleavage to gain biological activity.3,8) A membrane-bound MMP, membrane type-1 MMP (MT1-MMP or MMP-14), has been demonstrated to mediate the activation of pro-MMP-2 to active MMP-2 on the cell surface.8,9) The expression of MT1-MMP has also been found within human atherosclerotic plaques.10,11) Thus, MT1-MMP, an activator of pro-MMP-2 to active MMP-2, has been speculated to be an important determinant of the destabilization of atherosclerotic plaques.Production of MMP-2 and MMP-9 by monocytes/ macrophages occurs through a prostaglandin (PG) E 2 / cAMP-dependent pathway.1,12,13) Recently, Shankavaram et al. demonstrated that induction of monocyte MT1-MMP is also regulated through the PG E 2 /cAMP pathway. 14) These findings indicate the involvement of cyclooxygenases (COXs), rate-limiting enzymes in the conversion of arachidonic acid into PGs and thromboxanes, in the regulation of MMP biosynthesis. 1,15) To date, at least 2 distinct isoforms of the COXs-a constitutive form (COX-1) and an inducible isoform (COX-2)-and several of their variants have been discovered.16) COX-1 is constitutively expressed in most tissues and is responsible for maintaining homeostasis, whereas COX-2 is induced in response to inflammatory stimuli.17) Overexpression of COX-2 has been shown within human atherosclerotic plaques, localized predominantly in macrophages/foam cells, and to a lesser extent in medial smooth muscle cells and endothelial cells. 18,19) E...

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Section: Distribution Of Cox-2 In Relation To Mt1-mmp Distributionmentioning

confidence: 95%

Section: Distribution Of Mt1-mmp/mmp-2mentioning

confidence: 99%

mentioning

confidence: 97%

mentioning

confidence: 99%

See 2 more Smart Citations

Distribution Profiles of Membrane Type-1 Matrix Metalloproteinase (MT1-MMP), Matrix Metalloproteinase-2 (MMP-2) and Cyclooxygenase-2 (COX-2) in Rabbit Atherosclerosis: Comparison with Plaque Instability Analysis

Kuge

Takai

Ishino

et al. 2007

Biological & Pharmaceutical Bulletin

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show abstract

“…2,11 Oxidative stress can damage laminar epidermal cells because these cells have a lower metabolic rate than do epithelial cells in other organs, and the relative lack of superoxide dismutase activity makes them ill-equipped to deal with excessive amounts of ROS. 5,9 Furthermore, ROS induce cyclooxygenase-2 expression, 50 and a cyclooxygenase-2 metabolite, prostaglandin E 2 , has been found to promote the release and activation of matrix metalloproteinases-2 and -9 51 ; those matrix metalloproteinases are thought to play an important role in degradation of the basement membrane during acute laminitis. 46,52,53 Additionally, the myeloperoxidase-hydrogen peroxide system is able to inactivate antiprotease activity, 54 which creates an environment that favors the activity of proteases such as matrix metalloproteinases; this may contribute to additional laminar tissue damage.…”

Section: Discussionmentioning

confidence: 99%