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Show 18 Yuan Li college of engineering Fascia is a vitally important connective tissue that covers, supports, and holds together major tissues/ organs within the human body. However, fascia can be damaged/wore out through extreme movement or physical stress. Modern surgeries do not account variations in the biological composition and mechani-cal properties of fascial tissue. By studying these basic properties and compositions, strategies can be designed to minimize surgical complications and optimize surgical outcomes. Therefore, the focus of this project is to measure the mechanical strength and examine the biological composition of fascial tissue. The mechanical properties were explored by determining the elastic moduli and Poisson's ratios of twenty-five 5 by 5 centimeter tissue samples from their stress-strain curves. We found significant varia-tion between fascia samples. We hypothesized that the measured variations were due to heterogeneity in the biological composition of fascia, specifically in its matrix proteins density. We selected immuno-fluorescence to quantify the density of collagen type I and elastin, because they are the two most abun-dant matrix proteins in fascia. For both, we treated three adjacent (i.e. from essentially the same location) tissue samples of 1 by 1 centimeter with three different concentrations (1 mg/ml of antibody diluted 1:50 in bovine blocking serum, diluted 1:100, and the control without antibody) of the primary anti-collagen I or anti-elastin antibodies. The samples were examined using fluorescent microscopy, under both the blue(~450 nm) excitation light to observe the cell nuclei and red(~700 nm) excitation light to observe the targeted proteins. The results at both dilutions for the proteins showed strong intensity at red wavelength, indicating the presence of matrix protein, whereas control (without antibody) gave off almost no color. The outcome from the immunofluoresence study demonstrated that both collagen I and elastin are present within the fascia and are heterogeneously distributed. Remarkably, the heterogeneity of these matrix proteins of each sample displayed unique fluorescence intensities, and also exhibited different stress-strain curves, which explained the significant variations among the samples. For future studies, the relative and absolute concentrations of both collagen I and elastin will be quantified and correlated with the mechanical properties. A. B. C. Figure 1. Tissue stained with collagen I antibody at a) 1:50 dilution, b) 1:100 dilution, c) control (no anti-body), a) and b) showed significant amount of red intensity, whereas c) showed little or none. EXPLORING THE ROLE OF MATRIX PROTEIN IN THE MECHANICAL PROPERTIES OF BOVINE FASCIAL TISSUE Yuan Li ( Leonard Pease) Department of Chemical Engineering University of Utah UNDERGRADUATE RESEARCH ABSTRACTS Leonard Pease |