1 March 2007 Fluorescence spectroscopy and birefringence of molecular changes in maturing rat tail tendon
Author Affiliations +
J. of Biomedical Optics, 12(2), 024011 (2007). doi:10.1117/1.2714055
Tissue remodeling during maturation, wound healing, and response to vascular stress involves molecular changes of collagen and elastin in the extracellular matrix (ECM). Two optical techniques are effective for investigating these changes—laser-induced fluorescence (LIF) spectroscopy and polarizing microscopy. LIF spectroscopy integrates the signal from both elastin and collagen cross-linked structure, whereas birefringence is a measure of only collagen. Our purpose is (1) to evaluate the rat tail tendon (RTT) spectroscopy against data from purified extracted protein standards and (2) to correlate the two optical techniques in the study of RTT and skin. Spectra from tissue samples from 27 male rats and from extracted elastin and collagen were obtained using LIF spectroscopy (357 nm). Birefringence was measured on 5-μm histological sections of the same tissue. Morphometric analysis reveals that elastin represents approximately 10% of tendon volume and contributes to RTT fluorescence. RTT maximum fluorescence emission intensity (FEImax), which includes collagen and elastin, increases with animal weight (R2=0.64). Birefringence, when plotted against weight, increases to a plateau (nonlinear correlation: R2=0.90), tendon having greater birefringence than skin. LIF spectroscopy and collagen fiber birefringence are shown to provide complementary measurements of molecular structure (tendon birefringence versus FEImax at R2=0.60).
Renee M. Korol, Helen M. Finlay, Melanie J. Josseau, Alexandra R. Lucas, Peter B. Canham, "Fluorescence spectroscopy and birefringence of molecular changes in maturing rat tail tendon," Journal of Biomedical Optics 12(2), 024011 (1 March 2007). http://dx.doi.org/10.1117/1.2714055







Fluorescence spectroscopy


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