Related Experiment Video
Updated: May 12, 2026

06:07
Preparing Porcine Eyes for Confocal Reflectance Microscopy to Visualize the Vitreous Collagen Fiber Network
Published on: October 17, 2025
Visualizing collagen network within human and rhesus monkey vocal folds using polarized light microscopy
Margaret Julias1, Tobias Riede, Douglas Cook
1Division of Engineering, New York University, Abu Dhabi, United Arab Emirates.
The Annals of Otology, Rhinology, and Laryngology
|March 29, 2013
Summary
Investigating vocal fold collagen using polarized light microscopy revealed species-specific fiber distribution. This difference in collagen networks between humans and rhesus monkeys helps explain variations in their vocal fold viscoelastic properties.
Area of Science:
- Vocal fold biomechanics
- Connective tissue histology
- Comparative anatomy
Background:
- Collagen fiber content and orientation are crucial for vocal fold viscoelasticity and oscillation.
- Understanding the vocal fold collagen network at micron-scale resolution is essential but challenging.
- Polarized light microscopy offers a method to visualize collagen distribution and alignment.
Purpose of the Study:
- To investigate the distribution and alignment of collagen fibers in human and rhesus monkey vocal folds.
- To compare the collagen networks between the two species.
- To correlate collagen network structure with vocal fold viscoelastic properties.
Main Methods:
- Human and rhesus monkey vocal fold sections were analyzed using polarized light microscopy.
- Tissue sections were cut at three different angles to capture network complexity.
- Picrosirius red staining was employed to visualize collagen fibers.
Main Results:
- Significant differences in collagen fiber distribution were observed across different section angles.
- Human vocal folds showed continuous variation in collagen distribution and high birefringence near the thyroarytenoid muscle and epithelium.
- Rhesus monkey vocal folds exhibited high birefringence near the epithelium and lower birefringence near the thyroarytenoid muscle.
Conclusions:
- The study identified distinct differences in collagen networks between human and rhesus monkey vocal folds.
- These structural variations provide a morphological basis for observed differences in species-specific vocal fold viscoelastic properties.
Related Concept Videos
Fibril-associated Collagen
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...
Type IV Collagen of Basal Lamina
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
A type IV collagen molecule has six alpha chains which can exist in...

