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<publisher>HAL CCSD</publisher>
<title lang=en>Determination of extracellular matrix collagen fibril architectures and pathological remodeling by polarization dependent second harmonic microscopy</title>
<creator>Rouède, Denis</creator>
<creator>Schaub, Emmanuel</creator>
<creator>Bellanger, Jean-Jacques</creator>
<creator>Ezan, Frédéric</creator>
<creator>Scimeca, Jean-Claude</creator>
<creator>Baffet, Georges</creator>
<creator>Tiaho, François</creator>
<contributor>Institut de Physique de Rennes (IPR) ; Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Laboratoire Traitement du Signal et de l'Image (LTSI) ; Université de Rennes 1 (UR1) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Institut de Biologie Valrose (IBV) ; Université Nice Sophia Antipolis (UNS) ; Université Côte d'Azur (UCA) - Université Côte d'Azur (UCA) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<description>International audience</description>
<source>ISSN: 2045-2322</source>
<source>EISSN: 2045-2322</source>
<source>Scientific Reports</source>
<publisher>Nature Publishing Group</publisher>
<identifier>hal-01592192</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-01592192</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-01592192/document</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-01592192/file/s41598-017-12398-0.pdf</identifier>
<source>https://hal.archives-ouvertes.fr/hal-01592192</source>
<source>Scientific Reports, Nature Publishing Group, 2017, 7, pp.12197. 〈10.1038/s41598-017-12398-0〉</source>
<identifier>DOI : 10.1038/s41598-017-12398-0</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-017-12398-0</relation>
<identifier>PUBMED : 28939903</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/28939903</relation>
<language>en</language>
<subject>[SDV.IB.IMA] Life Sciences [q-bio]/Bioengineering/Imaging</subject>
<subject>[SDV.MHEP.AHA] Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Polarization dependence second harmonic generation (P-SHG) microscopy is gaining increase popularity for in situ quantification of fibrillar protein architectures. In this report, we combine P-SHG microscopy, new linear least square (LLS) fitting and modeling to determine and convert the complex second-order non-linear optical anisotropy parameter ρ of several collagen rich tissues into a simple geometric organization of collagen fibrils. Modeling integrates a priori knowledge of polyhelical organization of collagen molecule polymers forming fibrils and bundles of fibrils as well as Poisson photonic shot noise of the detection system. The results, which accurately predict the known sub-microscopic hierarchical organization of collagen fibrils in several tissues, suggest that they can be subdivided into three classes according to their microscopic and macroscopic hierarchical organization of collagen fibrils. They also show, for the first time to our knowledge, intrahepatic spatial discrimination between genuine fibrotic and non-fibrotic vessels. CCl 4-treated livers are characterized by an increase in the percentage of fibrotic vessels and their remodeling involves peri-portal compaction and alignment of collagen fibrils that should contribute to portal hypertension. This integrated P-SHG image analysis method is a powerful tool that should open new avenue for the determination of pathophysiological and chemo-mechanical cues impacting collagen fibrils organization. </description>
<date>2017</date>
</dc>
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