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Review
. 2007 Jul;23(9):727-33.
doi: 10.1016/s0828-282x(07)70818-8.

Matrix metalloproteinases and myocardial infarction

Wannakorn Phatharajaree  1 , Arintaya Phrommintikul, Nipon Chattipakorn
Affiliations
Review

Matrix metalloproteinases and myocardial infarction

Wannakorn Phatharajaree et al. Can J Cardiol. 2007 Jul.

Abstract
in English, French

Acute myocardial infarction (AMI) is currently one of the most important health problems in many countries around the world. Following AMI, many cytokines and proteolytic enzymes are released. Among these, matrix metalloproteinases (MMPs) are important proteolytic enzymes that lead to degradation of the extracellular matrix and to changes in cardiomyocytes in both infarcted and noninfarcted myocardium. This process is known as cardiac remodelling. It has been demonstrated that more than one type of MMP is present in the circulation after cardiomyocyte injury. A number of studies have demonstrated the correlations between these MMP levels and the severity of a coronary lesion, the progression of left ventricular dimension and the survival rate following AMI in both animal and human studies. MMPs have also been proposed as a possible novel prognostic indicator for myocardial infarction patients. Although the use of MMP inhibitors to improve cardiac outcome in AMI patients has been investigated, discrepancies in the results from those studies indicate that further research is still needed to warrant their beneficial effects. In the present review article, the roles of MMPs as prognostic indicators, as well as the factors influencing MMP expression, are discussed. Current findings on the role of MMP inhibitors in cardiac remodelling and the prognosis after AMI in both animal models and clinical studies are also examined.

L’infarctus aigu du myocarde (IAM) est l’un des principaux problèmes de santé dans le monde, aujourd’hui. Après un IAM, il y a libération de nombreuses cytokines et enzymes protéolytiques. Les métalloprotéinases matricielles (MPM), enzymes protéolytiques importantes, entraînent la dégradation de la matrice extracellulaire et une modification des cardiomyocytes, et ce, tant dans le myocarde infarci que dans le myocarde non infarci. Le processus s’appelle « remodelage cardiaque ». Il a été démontré que plus d’un type de MPM se trouve dans la circulation après une lésion des cardiomyocytes. Des corrélations ont été établies entre le taux de MPM et la gravité des lésions coronariennes, l’évolution de la grosseur du ventricule gauche et le taux de survie après un IAM dans des études expérimentales sur animal et dans des recherches chez les humains. Des chercheurs ont aussi suggéré de faire des MPM un nouvel indicateur de pronostic chez les patients ayant subi un infarctus aigu du myocarde. Même si des études ont été menées sur l’utilisation des inhibiteurs des MPM dans le but d’améliorer l’état du cœur après un IAM, des résultats divergents indiquent la nécessité de poursuivre les recherches sur le sujet afin de confirmer leurs bienfaits. Il sera question, dans le présent exposé de synthèse, du rôle des MPM comme indicateur de pronostic et des facteurs qui influent sur l’expression des MPM. Nous examinerons également les résultats actuels sur le rôle des inhibiteurs des MPM dans le remodelage cardiaque et sur le pronostic après un IAM dans des modèles animaux et dans des études cliniques.

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Figures

Figure 1)
Figure 1)
A Basic domain structure of a matrix metalloproteinase (MMP). MMPs contain at least three homologous protein domains: the signal peptide, which is a domain that targets the enzyme for secretion; the propeptide domain, which is removed when the enzyme becomes activated; and the catalytic domain, which contains the zinc-binding region and is responsible for the proteolytic activity of the enzyme. B Structural differences between various classes of MMPs. In gelatinases, the catalytic domain contains the gelatin-binding domain, which is homologous with the collagen-binding domain of fibronectin. The hemopexin domain has been shown to play a functional role in substrate binding and interactions with tissue inhibitors of metalloproteinases. Membrane-type MMPs contain a transmembrane domain at the C-terminal end. Modified from reference 4 with permission
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