Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1868, Issue 12, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbadis.2022.166494
Keywords
Collagen; Phase-ContrastMicroComputedTomography; FourierTransformInfraredImaging; spectroscopy; TransmissionElectronMicroscopy; Uterineleiomyoma; Omega-3fattyacids
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Collagen, as a crucial component of the extracellular matrix, plays a key role in tissue structural support, particularly in fibrotic diseases. Investigating collagen structure can help identify specific pathological markers. Uterine leiomyoma serves as a valuable model to study collagen self-organization in a pathological condition using innovative multidisciplinary approaches.
Collagen is one of the main components of the extracellular matrix (ECM), involved, among all, in the main-tenance of the structural support of tissues. In fibrotic diseases, collagen is overexpressed, and its production determines the formation of a significantly stiffer ECM. The cross-linking of high-resolution analytical tools, able to investigate both the tridimensional organization and the secondary structure of collagen in fibrotic diseases, could be useful to identify defined markers correlating the status of this protein with specific pathological conditions. To this purpose, an innovative multidisciplinary approach based on Phase-Contrast MicroComputed Tomography, Transmission Electron Microscopy, and Fourier Transform Infrared Imaging Spectroscopy was exploited on leiomyoma samples and adjacent myometrium to characterize microstructural collagen features. Uterine leiomyoma is a common gynecological disorder affecting women in fertile age. It is characterized by a massive collagen production due to the repairing processes occurring at myometrium level, and, hence, it rep-resents a valuable model to investigate collagen self-organization in a pathological condition. Moreover, to evaluate the sensitivity of this multidisciplinary approach, the effects of eicosapentaenoic (EPA) and docosa-hexaenoic (DHA) omega-3 fatty acids in collagen reduction were also investigated.
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