A review of the epithelial and stromal effects of corneal collagen crosslinking

Bradford, Samantha; Luo, Shangbang; Brown, Donald; Juhasz, Tibor; Jester, James

doi:10.1016/j.jtos.2023.09.003

Cited by 4 publications

(1 citation statement)

References 106 publications

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“…However, corneal thinning diseases distort vision, affecting daily life activities and the mental health of patients [4]. Keratoconus is a corneal disease characterized by bulging of the corneal surface due to progressive weakening and thinning of the corneal stroma [5][6][7]. A clinically proven method for treating patients with keratoconus is corneal crosslinking (CXL) [8].…”

Section: Introductionmentioning

confidence: 99%

A unique and biocompatible approach for corneal collagen crosslinking in vivo

Gulzar,

Kaleli,

Koseoglu

et al. 2024

Preprint

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Corneal crosslinking (CXL) is a widely applied technique to halt the progression of ectatic diseases by increasing the thickness and mechanical stiffness of the cornea. This study investigated the biocompatibility and efficiency of a novel CXL procedure using ruthenium and blue light in rat corneas and evaluated factors important for clinical application. To perform the CXL procedure, the corneal epithelium of rats was removed under anesthesia, followed by the application of a solution containing ruthenium and sodium persulfate (SPS). The corneas were then exposed to blue light at 430 nm at 3 mW/cm2 for 5 minutes. Rat corneas were examined and evaluated for corneal opacity, corneal and limbal neovascularization, and corneal epithelial regeneration at days 0, 1, 3, 6, 8, and 14. On day 28, the corneas were isolated for subsequent tissue follow-up and analysis. CXL with ruthenium and blue light showed rapid epithelial healing, with 100% regeneration of the corneal epithelium and no corneal opacity by day 6. The ruthenium group also exhibited significantly reduced corneal (p<0.01) and limbal neovascularization (p<0.001). Histological analysis revealed no signs of cellular damage or apoptosis, which further confirms the biocompatibility and nontoxicity of our method. Confocal and scanning electron microscopy (SEM) images showed a greater density of collagen fibrils, indicating efficient crosslinking and enhanced structural integrity. This study confirmed the in vivo safety, biocompatibility, and functionality of ruthenium and blue light CXL. This method can prevent toxicity caused by UV-A light and can be a rapid alternative treatment to standard crosslinking procedures.

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Section: Introductionmentioning

confidence: 99%

A unique and biocompatible approach for corneal collagen crosslinking in vivo

Gulzar,

Kaleli,

Koseoglu

et al. 2024

Preprint

View full text Add to dashboard Cite

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Collagen crosslinking-induced corneal morphological changes: a three-dimensional light sheet Microscopy-based evaluation

Stoecker,

Pinkert-Leetsch,

Koch

et al. 2024

Sci Rep

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Stiffness-related eye diseases such as keratoconus require comprehensive visualization of the complex morphological matrix changes. The aim of this study was to use three-dimensional (3D) light sheet fluorescence microscopy (LSFM) to analyze unlabeled corneal tissue samples, qualitatively visualizing changes in corneal stiffness. Isolated porcine corneal tissue samples were treated with either NaCl or 0.1% glutaraldehyde (GTA) prior to clearing with benzyl alcohol/benzyl benzoate (BABB) and subsequently scanned with LSFM. After analysis of the LSFM data sets, the samples were embedded in paraffin to validate the results by conventional planar microscopy. In the unlabeled corneal tissue samples the 2D/3D morphology of the entire tissue volume was identified by specific autofluorescence signals. An enhancement of collagen crosslinking was induced by applying GTA to the corneal tissue. Subsequent LSFM scans showed specific morphological changes due to altered autofluorescence signals of the corneal stroma, which were confirmed by conventional histology. Therefore, LSFM analysis of corneal tissue samples allowed label-free 3D autofluorescence assessment of the corneal morphology in its anatomical context. It provides the technical basis for the examination of the pathologically altered cornea and facilitates ophthalmologic examinations of corneal diseases based on the altered tissue stiffness.

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Hydroxyproline Concentration and Associated Factors of Preserved Small Incision Lenticule Extraction–Derived Corneal Stromal Lenticules

Han,

Li,

Zhao

et al. 2024

Cornea

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Purpose: To evaluate changes of hydroxyproline concentration and its influencing factors of small incision lenticule extraction (SMILE)-derived corneal stromal lenticules with different preservation methods. Methods: A total of 390 corneal stromal lenticules of 195 patients were derived from SMILE surgeries. Thirty of the lenticules were classified as the fresh (control) group, and the rest were randomly and evenly divided and stored in anhydrous glycerol, silicone oil, Optisol, and cryopreservation for 1 day, 1 week, or 1 month. A hydroxyproline assay kit (ab222941, Abcam) was used to measure the hydroxyproline concentration in each preservation method. Concentrations of MMP-2, TIMP-2, TNFα, TGFβ2, and reactive oxygen species were also evaluated. Results: In the anhydrous glycerol group, the concentration of hydroxyproline decreased within 1 week (fresh: 1 dΔ = 0.229, P < 0.001*; 1 d − 1 wΔ = 0.055, P < 0.001*) while that in the silicone oil group remained stable in 1 week (1 d − 1 wΔ = −0.005, P = 0.929) and decreased significantly in 1 m (1 m − 1 wΔ = −0.041, P = 0.003*). The sequence of hydroxyproline concentration in the Optisol group was 1 m > 1 day > 1 week. Hydroxyproline concentration in the cryopreservation group decreased within 1 m. Hydroxyproline concentration was highest in the Optisol group and lowest in the anhydrous glycerol group under the same preservation time. Hydroxyproline concentration was negatively correlated with MMP-2 (r = −0.16, P = 0.421) and TIMP-2 (r = −0.56, P = 0.002*) while MMP-2 and TNFα (r = 0.17, P = 0.242), TIMP-2 and TGFβ2 (r = 0.21, P = 0.207), and TNFα and reactive oxygen species (r = 0.52, P = 0.007*) were positively correlated. Conclusions: More collagen was retained in SMILE lenticules preserved in Optisol under the same preservation time. The mechanism of the changes of collagen in preserved SMILE-derived lenticules and oxidative stress requires additional investigation.

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A review of the epithelial and stromal effects of corneal collagen crosslinking

Cited by 4 publications

References 106 publications

A unique and biocompatible approach for corneal collagen crosslinking in vivo

A unique and biocompatible approach for corneal collagen crosslinking in vivo

Collagen crosslinking-induced corneal morphological changes: a three-dimensional light sheet Microscopy-based evaluation

Hydroxyproline Concentration and Associated Factors of Preserved Small Incision Lenticule Extraction–Derived Corneal Stromal Lenticules

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