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| Content Provider | IEEE Xplore Digital Library |
|---|---|
| Author | Ying Yang Rupani, A. Weightman, A. Wimpenny, I. Ahearne, M. |
| Copyright Year | 2011 |
| Description | Author affiliation: Institute of Science and Technology in Medicine, Keele University, Stoke-on-Trent, UK (Ying Yang; Rupani, A.; Weightman, A.; Wimpenny, I.; Ahearne, M.) |
| Abstract | Tendons are load-bearing collagenous tissues consisting mainly of type I collagen and various proteoglycans (PGs) including decorin and versican. It is widely accepted that highly orientated collagen fibers in tendons a play critical role for transferring tensile stress and demonstrate birefringent optical properties. However, the influence that proteoglycans have on the optical properties of tendons is yet to be fully elucidated. Tendinopathy (defined as a syndrome of tendon pain, tenderness and swelling that affects the normal function of the tissue) is a common disease associated with sporting injuries or degeneration. PG's are the essential components of the tendon extracellular matrix; changes in their quantities and compositions have been associated with tendinopathy. In this study, polarization sensitive optical coherence tomography (PS-OCT) has been used to reveal the relationship between proteoglycan content/location and birefringent properties of tendons. Tendons dissected from freshly slaughtered chickens were imaged at regular intervals by PS-OCT and polarizing light microscope during the extraction of PGs or glycosaminoglycans using established protocols (guanidine hydrochloride (GuHCl) or proteinase K solution). The macroscopic and microscopic time lapsed images are complimentary; mutually demonstrating that there was a higher concentration of PG's in the outer sheath region than in the fascicles; and the integrity of the sheath affected extraction process and the OCT birefringence bands. Extraction of PGs using GuHCl disturbed the organization of local collagen bundles, which corresponded to a reduction in the frequency of birefringence bands and the band width by PS-OCT. The feature of OCT penetration depth helped us to define the heterogeneous distribution of PG's in tendon, which was complimented by polarizing light microscopy. The results provide new insight of tendon structure and also demonstrate a great potential for using PS-OCT as a diagnostic tool to examine tendon pathology. |
| Starting Page | 2350 |
| Ending Page | 2354 |
| File Size | 1793808 |
| Page Count | 5 |
| File Format | |
| ISBN | 9781424493517 |
| e-ISBN | 9781424493524 |
| DOI | 10.1109/BMEI.2011.6098761 |
| Language | English |
| Publisher | Institute of Electrical and Electronics Engineers, Inc. (IEEE) |
| Publisher Date | 2011-10-15 |
| Publisher Place | China |
| Access Restriction | Subscribed |
| Rights Holder | Institute of Electrical and Electronics Engineers, Inc. (IEEE) |
| Subject Keyword | Optical fiber polarization Proteins tendon interfibrillar connections Microscopy Organizations Optical fiber theory PS-OCT polarizing light microscopy Tendons proteoglycan |
| Content Type | Text |
| Resource Type | Article |
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