Journal
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY
Volume 282, Issue 6, Pages H2324-H2335Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpheart.00711.2001
Keywords
matrix metalloproteinases; muscle; stiffness; viscosity
Funding
- NHLBI NIH HHS [P01-HL-48788, R01-HL-55444-03] Funding Source: Medline
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To determine whether and to what extent one component of the extracellular matrix, fibrillar collagen, contributes causally to abnormalities in viscoelasticity, collagen was acutely degraded by activation of endogenous matrix metalloproteinases (MMPs) with the serine protease plasmin. Papillary muscles were isolated from normal cats and cats with right ventricular pressure overload hypertrophy (POH) induced by pulmonary artery banding. Plasmin treatment caused MMP activation, collagen degradation, decreased the elastic stiffness constant, and decreased the viscosity constant in both normal and POH muscles. Thus, whereas many mechanisms may contribute to the abnormalities in myocardial viscoelasticity in the POH myocardium, changes in fibrillar collagen appear to play a predominant role.
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