Matrix metalloproteinases of vascular wall cells are increased in balloon-injured rat carotid artery

Zempo, Nobuya; Kenagy, Richard D.; Au, Y P; Bendeck, Michelle P.; Clowes, Monika M.; Reidy, Michael A.; Clowes, Alexander W.

doi:10.1016/0741-5214(94)90008-6

Cited by 249 publications

(173 citation statements)

References 43 publications

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“…4 -6 Among these proteases, MMPs and the serine protease system, plasminogen/plasmin, have been believed to contribute to matrix remodeling and to play an essential role in SMC migration. [7][8][9][10] This is supported by findings that MMPs and plasminogen activator levels are elevated after balloon injury to rat carotid arteries. 7,8,11 However, previous observations have suggested that the even effective inhibition of MMPs and serine proteases might not sufficiently arrest neointima formation.…”

supporting

confidence: 66%

“…[7][8][9][10] This is supported by findings that MMPs and plasminogen activator levels are elevated after balloon injury to rat carotid arteries. 7,8,11 However, previous observations have suggested that the even effective inhibition of MMPs and serine proteases might not sufficiently arrest neointima formation. [12][13][14][15] Cathepsins, lysosomal proteases within the papain superfamily, are thought to generally reside in and function optimally within acidic lysosomes.…”

supporting

confidence: 66%

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Increased Expression of Elastolytic Cysteine Proteases, Cathepsins S and K, in the Neointima of Balloon-Injured Rat Carotid Arteries

Cheng

Kuzuya

Sasaki

et al. 2004

The American Journal of Pathology

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The matrix-degrading activity of several proteases are involved in the accelerated breakdown of extracellular matrix associated with vascular remodeling during the development of atherosclerosis and vascular injury-induced neointimal formation. Previous studies have shown that the potent elastolytic cysteine proteases, cathepsins S and K, are overexpressed in atherosclerotic lesions in human and animal models. However, the role of these cathepsins in vascular remodeling remains unclear. In the present study, the expressions of cathepsin S and K and their inhibitor cystatin C were examined during arterial remodeling using a rat carotid artery balloon-injury model. The increase in both cathepsin S and K mRNA levels was observed from day 1 and day 3 through day 14 following the induction of balloon injury, respectively. Western blotting analysis revealed that both cathepsin S and K protein levels also increased in the carotid arteries during neointima formation, coinciding with an increase elastolytic activity assayed using Elastin-Congo red, whereas, no significant change in the expressions of cystatin C mRNA and protein was observed during follow-up periods after injury. Immunohistochemistry, Western blot, and in situ hybridization showed that the increase of cathepins S and K and the decrease of cystatin C occurred preferentially in the developing neointima. These findings suggest that cathepsin S and K may participate in the pathological arterial remodeling associated with restenosis.

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supporting

confidence: 66%

supporting

confidence: 66%

Increased Expression of Elastolytic Cysteine Proteases, Cathepsins S and K, in the Neointima of Balloon-Injured Rat Carotid Arteries

Cheng

Kuzuya

Sasaki

et al. 2004

The American Journal of Pathology

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“…Zempo et al (27) have shown that the activities of gelatinases A and B are increased in rat carotid artery after balloon catheter injury. In the present study, the expression of MT-MMPs, especially MT3-MMP, in cultured SMCs was strongly induced by the presence of serum.…”

Section: Discussionmentioning

confidence: 99%

“…These processes are presumed to require partial degradation of the vascular basement membrane and extracellular matrix surrounding the cells (27,28). However, less is known about MMP species involved in these processes and their roles.…”

mentioning

confidence: 99%

Expression of Three Membrane-type Matrix Metalloproteinases (MT-MMPs) in Rat Vascular Smooth Muscle Cells and Characterization of MT3-MMPs with and without Transmembrane Domain

Shofuda

Yasumitsu

Nishihashi

et al. 1997

Journal of Biological Chemistry

111

100

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“…In addition, the expression patterns of MMP-2, MMP-3 and MMP-9 in the kidney glomerulus, seem to be linked in a compensatory manner, as was shown in genetic knock-out mouse models [46]. Similarly, differential actions and expression profiles of MMP-2 and MMP-9 have been implicated in platelet aggregation [48] as well as in the response to injury in the carotid artery [49].…”

Section: Differential Metalloproteinase Expression Leads To Varying Pmentioning

confidence: 80%

Metalloproteinases in hypertension and cardiac disease: differential expression and mutual regulation

Bosonea

Wang

Odenbach

et al. 2011

Drug Discovery Today: Disease Models

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Arterial hypertension, a condition characterized by sustained elevated blood pressure, is associated with pathological cardiac remodeling (i.e. cardiac hypertrophy and fibrosis) and is a major risk factor for cardiac failure. These processes can be triggered by excess vasoconstrictive agonists, which induce metalloproteinase-dependent shedding of growth factors to transactivate growth factor receptors and initiate disease signaling. Here, we review emerging evidence that agonistactivated metalloproteinases exhibit different expression patterns and mutual transcriptional regulation during the development of hypertension and cardiac remodeling.

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Matrix metalloproteinases of vascular wall cells are increased in balloon-injured rat carotid artery

Cited by 249 publications

References 43 publications

Increased Expression of Elastolytic Cysteine Proteases, Cathepsins S and K, in the Neointima of Balloon-Injured Rat Carotid Arteries

Increased Expression of Elastolytic Cysteine Proteases, Cathepsins S and K, in the Neointima of Balloon-Injured Rat Carotid Arteries

Expression of Three Membrane-type Matrix Metalloproteinases (MT-MMPs) in Rat Vascular Smooth Muscle Cells and Characterization of MT3-MMPs with and without Transmembrane Domain

Metalloproteinases in hypertension and cardiac disease: differential expression and mutual regulation

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