# The alteration of the structure and macroscopic mechanical response of porcine patellar tendon by elastase digestion

**Authors:** Xiaoyun Liu, Yuping Deng, Zeyu Liang, Dan Qiao, Wentian Zhang, Mian Wang, Feifei Li, Jiannan Liu, Yaobing Wu, Guangxin Chen, Yan Liu, Wenchang Tan, Jian Xing, Wenhua Huang, Dongliang Zhao, Yanbing Li

PMC · DOI: 10.3389/fbioe.2024.1374352 · 2024-04-17

## TL;DR

This study shows how elastin affects the mechanical properties and structure of patellar tendons, using porcine samples treated with elastase.

## Contribution

The study reveals the specific role of elastin in patellar tendon mechanics and structure through elastase digestion and modeling.

## Key findings

- Elastin degradation reduced tensile modulus and altered viscoelastic behavior in patellar tendons.
- Collagen fibers became disordered and looser after elastin breakdown, increasing fiber wavelength.
- A dynamic constitutive model was developed to predict mechanical responses of patellar tendon.

## Abstract

Background: The treatment of patellar tendon injury has always been an unsolved problem, and mechanical characterization is very important for its repair and reconstruction. Elastin is a contributor to mechanics, but it is not clear how it affects the elasticity, viscoelastic properties, and structure of patellar tendon.

Methods: The patellar tendons from six fresh adult experimental pigs were used in this study and they were made into 77 samples. The patellar tendon was specifically degraded by elastase, and the regional mechanical response and structural changes were investigated by: (1) Based on the previous study of elastase treatment conditions, the biochemical quantification of collagen, glycosaminoglycan and total protein was carried out; (2) The patellar tendon was divided into the proximal, central, and distal regions, and then the axial tensile test and stress relaxation test were performed before and after phosphate-buffered saline (PBS) or elastase treatment; (3) The dynamic constitutive model was established by the obtained mechanical data; (4) The structural relationship between elastin and collagen fibers was analyzed by two-photon microscopy and histology.

Results: There was no statistical difference in mechanics between patellar tendon regions. Compared with those before elastase treatment, the low tensile modulus decreased by 75%–80%, the high tensile modulus decreased by 38%–47%, and the transition strain was prolonged after treatment. For viscoelastic behavior, the stress relaxation increased, the initial slope increased by 55%, the saturation slope increased by 44%, and the transition time increased by 25% after enzyme treatment. Elastin degradation made the collagen fibers of patellar tendon become disordered and looser, and the fiber wavelength increased significantly.

Conclusion: The results of this study show that elastin plays an important role in the mechanical properties and fiber structure stability of patellar tendon, which supplements the structure-function relationship information of patellar tendon. The established constitutive model is of great significance to the prediction, repair and replacement of patellar tendon injury. In addition, human patellar tendon has a higher elastin content, so the results of this study can provide supporting information on the natural properties of tendon elastin degradation and guide the development of artificial patellar tendon biomaterials.

## Linked entities

- **Proteins:** LIMK1 (LIM domain kinase 1), COL3A1 (collagen type III alpha 1 chain)
- **Chemicals:** elastase (PubChem CID 168009926), phosphate-buffered saline (PubChem CID 24978514)
- **Species:** Sus scrofa (taxon 9823)

## Full-text entities

- **Genes:** Elastin [NCBI Gene 100620140], ELN (elastin) [NCBI Gene 2006] {aka ADCL1, SVAS, WBS, WS}
- **Diseases:** patellar tendon injury (MESH:D013708)
- **Chemicals:** glycosaminoglycan (MESH:D006025), PBS (-)
- **Species:** Homo sapiens (human, species) [taxon 9606], Sus scrofa (pig, species) [taxon 9823]

## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC11061363/full.md

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Source: https://tomesphere.com/paper/PMC11061363