Abstract P2098: A Novel Measure Of Myocardial Collagen Structure Using Ultrasonic Backscatter

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Aging and disease are associated with dysregulation of collagen deposition and collagen degradation and crosslinking. These modifications in collagen structure are key determinants of cardiac integrity and function, making it advantageous to monitor collagen’s state throughout disease. Although myocardial fibrosis often occurs alongside both cardiac and systemic disease, monitoring myocardial collagen typically requires expensive, invasive, and/or contraindicated methods. However, collagen content has been correlated to ultrasonic backscatter, a low-cost, non-invasive index. Preliminary studies in our lab suggested collagen also dominates the anisotropy of backscatter(variation in the brightness) in a left ventricular short-axis ultrasound. The purpose of the present study was to determine a relationship between myocardial collagen structure and anisotropy of ultrasonic backscatter while using collagenase to degrade myocardial collagen networks. Hearts were excised from Sprague Dawley rats and perfused with a collagenase-containing solution for either 10 (n=7) or 30 minutes (n=7) or control solution for 30 minutes (control n=8). Serial ultrasound images were acquired throughout collagenase digestion and ultrasonic backscatter was assessed where the collagen is primarily aligned perpendicular to the angle of insonification (bright on ultrasound image), and where collagen is primarily aligned parallel to the angle of insonification (darker on image). Our data suggested that collagenase digestion reduced backscatter anisotropy within the myocardium (p<0.001) with the lateral and septal walls (collagen parallel to ultrasound) showing the greatest change in backscatter intensity. Histology (Trichrome staining) and biochemistry (hydroxyproline assay) suggests that collagen remains present but its crosslinking is altered within 10 minutes (p<0.047). These data suggest that myocardial collagen fiber orientation and crosslinking of collagen correlates with the anisotropy of ultrasonic backscatter. Thus, anisotropy of ultrasonic backscatter could potentially be used to assess collagen crosslinking and deposition.