Revealing structural modifications in thermomechanical reshaping of collagenous tissues using optical coherence
Vladimir Y Zaitsev1, Alexander L Matveyev1, Lev A Matveev1
1Institute of Applied Physics, Russian Academy of Sciences, Nizhny Novgorod, Russia.
Journal of Biophotonics
|November 13, 2018
Summary
Infrared laser irradiation non-destructively modifies collagen tissues. Optical coherence tomography (OCT) visualizes and evaluates laser-induced micropores in situ, correlating with microscopic findings for clinical applications.
Area of Science:
- Biomedical Engineering
- Ophthalmology
- Tissue Engineering
Background:
- Infrared (IR) laser irradiation offers non-destructive modification of collagenous tissues like cornea and cartilage.
- Microscopic examination reveals pores post-irradiation but is limited for in situ averaged parameter evaluation.
- Assessing laser-induced tissue changes in real-time remains a challenge.
Purpose of the Study:
- To demonstrate Optical Coherence Tomography (OCT) for visualizing and evaluating laser-induced micropores in collagenous tissues.
- To assess averaged micropore properties in situ using OCT-based elastography.
- To correlate OCT findings with traditional microscopic examination for validation.
Main Methods:
- Utilized OCT to visualize tissue dilatation caused by IR laser irradiation.
- Employed OCT-based compressional elastography to measure Young's modulus reduction.
- Combined dilatation and elastography data to evaluate averaged micropore parameters in situ.
- Compared OCT-derived data with high-resolution microscopy results.
Main Results:
- OCT successfully visualized areas of micropore initiation in laser-irradiated cornea.
- OCT-based elastography quantified the reduction in Young's modulus due to micropores.
- Averaged micropore parameters derived from OCT correlated well with microscopic examination.
- Demonstrated significant modulus decrease in the irradiated region, indicative of micropores.
Conclusions:
- OCT, combined with elastography, provides an effective in situ method for evaluating laser-induced micropores in collagenous tissues.
- This approach overcomes limitations of traditional microscopy for averaged parameter assessment.
- The findings support the safe and effective clinical application of IR laser tissue modification technologies.
Keywords:
OCT elastographylaser-tissue interactionoptical coherence tomographyphase-resolved OCTstrain mappingthermo-mechanical cornea reshapingMore Related Videos
Related Concept Videos
Collagens are the Major Structural Proteins of ECM
5.8K
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Connective tissue proper includes loose...
5.8K
Histone Modification
16.1K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.1K
Histone Modification
4.5K
4.5K
Spreading of Chromatin Modifications
9.5K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
Writers
The writer...
9.5K
Fibril-associated Collagen
3.4K
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
3.4K
Structural Protein Function
30.0K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
30.0K


