ArticleTranslational vision science & technology2021
Collagen Structural Changes in Rat Tarsus After Crosslinking.
Article in Translational vision science & technology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Crosslinking of tarsal collagen as a hypothetical therapy for dry eye disease.Medical hypothesis, discovery & innovation ophthalmology journal · 2025Article
- Changes in Rat Scleral Collagen Structure Induced by UVA-Riboflavin Crosslinking at Various Tissue Depths in Whole Globe Versus Scleral Patch.Translational vision science & technology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Purpose: Surgery is the standard treatment for floppy eyelid syndrome, but crosslinking (CXL) tarsus has recently been proposed as an alternative. To the best of our knowledge, this study is the first to use second-harmonic generation (SHG) microscopy to examine tarsal collagen ex vivo before and after photo-activated crosslinking. To quantify crosslinking, this study examined fluorescence recovery after photobleaching (FRAP), which indirectly measures tissue stiffness. Methods: Upper eyelid tarsal plates were dissected from 21 Sprague-Dawley rats (total of 42 tarsal plates). Six normal plates were sent for histopathology and SHG imaging; the remaining 36 were crosslinked with phosphate-buffered saline (PBS) alone or riboflavin in PBS (concentrations of 0.1%, 0.3%, and 0.5%). Tissues were irradiated with 365-nm ultraviolet A light (power, 0.45 mW/cm2) for 30 minutes and immediately underwent SHG microscopy. Stiffness was indirectly measured with FRAP using fluorescein isothiocyanate (FITC)-dextran. Results: SHG imaging of normal tarsus showed that the organization of collagen bundles is complex and varies greatly depending on location. After crosslinking with high-concentration riboflavin (0.5%), collagen fibers showed clear structural changes, becoming more densely packed and wavier compared to control. FRAP half-time to fluorescence recovery was significantly increased (P < 0.05), indirectly indicating increased tissue stiffness. No structural changes were observed after crosslinking with lower riboflavin concentrations of 0.1% and 0.3%. Conclusions: This is the first report of SHG microscopy used to image tarsus collagen before and after crosslinking. These results highlight collagen structural changes, with effects on tissue stiffness indirectly confirmed by FRAP. Translational Relevance: Collagen fibers in the tarsus may be a therapeutic target for crosslinking in order to treat symptomatic floppy eyelid syndrome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.