FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / J Physiol / Structural changes in loaded equine tendons can be monitored...
The Journal of physiology2003; 554(Pt 3); 791-801; doi: 10.1113/jphysiol.2003.054809

Structural changes in loaded equine tendons can be monitored by a novel spectroscopic technique.

Abstract: This study aimed to investigate the preferential collagen fibril alignment in unloaded and loaded tendons using elastic scattering spectroscopy. The device consisted of an optical probe, a pulsed light source (320-860 nm), a spectrometer and a PC. Two probes with either 2.75 mm or 300 microm source-detector separations were used to monitor deep and superficial layers, respectively. Equine superficial digital flexor tendons were subjected to ex vivo progressive tensional loading. Seven times more backscattered light was detected parallel rather than perpendicular to the tendon axis with the 2.75 mm separation probe in unloaded tendons. In contrast, using the 300 microm separation probe the plane of maximum backscatter (3-fold greater) was perpendicular to the tendon axis. There was no optical anisotropy in the cross-sectional plane of the tendon (i.e. the transversely cut tendon surface), with no structural anisotropy. During mechanical loading (9-14% strain) backscatter anisotropy increased 8.5- to 18.5-fold along the principal strain axis for 2.75 mm probe separation, but almost disappeared in the perpendicular plane (measured using the 300 microm probe separation). Optical (anisotropy) and mechanical (strain) measurements were highly correlated. We conclude that spatial anisotropy of backscattered light can be used for quantitative monitoring of collagen fibril alignment and tissue reorganization during loading, with the potential for minimally invasive real-time structural monitoring of fibrous tissues in normal, pathological or repairing tissues and in tissue engineering.
Get Full Text
Publication Date: 2003-10-24 PubMed ID: 14578479PubMed Central: PMC1664808DOI: 10.1113/jphysiol.2003.054809Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study explores a new spectroscopic technique for tracking structural changes in loaded equine tendons. Re-searchers used an optical probe to monitor the alignment of collagen fibrils in tendons under static and dynamic conditions. The results suggest that this technique could potentially be used for real-time, non-invasive monitoring of fibrous tissue structures during normal, pathological, or repairing stages, as well as in tissue engineering.

Methods

  • The researchers used a device with an optical probe, a pulsed light source, a spectrometer, and a personal computer.
  • They deployed two probes with varying source-detector separations to monitor both deep and superficial layers.
  • Equine superficial digital flexor tendons were subjected to ex vivo progressive tensional loading to mimic the stress conditions experienced by tendons during physical activity.

Key Findings

  • Among unloaded tendons, if probed with a 2.75 mm separation, seven times more backscattered light was detected parallel to the tendon axis. In contrast, using a 300 micrometer separation probe, maximum backscatter (3-fold greater) was perpendicular to the tendon axis.
  • No optical anisotropy was found in the cross-sectional plane of the tendon. Additionally, there was no observed structural anisotropy.
  • During a mechanical strain of 9-14%, the backscatter anisotropy increased significantly along the principal strain axis with the 2.75 mm probe. However, it almost disappeared when measured using the 300 micrometer probe.
  • Their findings revealed a strong correlation between optical measurements (anisotropy) and mechanical strain measurements.

Conclusions

  • The manipulation and variation of the source-detector separations probe allowed researchers to analyze deep and superficial layers, suggesting possible applications in multiple tensile layers.
  • This study established that the spatial anisotropy of backscattered light can be used for quantitative monitoring of collagen fibril alignment and tissue reorganization during loading. This points to the potential for this technique to be used in non-invasive monitoring of fibrous tissues.
  • The method holds promise for application in various scenarios involving normal, pathological, or repairing tissues, as well as in the field of tissue engineering.

Cite This Article

APA
Kostyuk O, Birch HL, Mudera V, Brown RA. (2003). Structural changes in loaded equine tendons can be monitored by a novel spectroscopic technique. J Physiol, 554(Pt 3), 791-801. https://doi.org/10.1113/jphysiol.2003.054809

Publication

The Journal of physiology
ISSN: 0022-3751
NlmUniqueID: 0266262
Country: England
Language: English
Volume: 554
Issue: Pt 3
Pages: 791-801

Researcher Affiliations

Kostyuk, Oksana
  • University College London, Tissue Repair and Engineering Centre, Institute of Orthopaedics and Musculoskeletal Science, RNOH Campus, Brockley Hill, Stanmore HA7 4LP, UK. rehkrab@ucl.ac.uk
Birch, Helen L
    Mudera, Vivek
      Brown, Robert A

        MeSH Terms

        • Animals
        • Anisotropy
        • Fiber Optic Technology
        • Horses / anatomy & histology
        • Horses / physiology
        • Light
        • Optics and Photonics
        • Reference Values
        • Scattering, Radiation
        • Tendons / physiology
        • Tendons / ultrastructure
        • Weight-Bearing / physiology

        References

        This article includes 27 references
        1. Bigio IJ, Mourant JR. Ultraviolet and visible spectroscopies for tissue diagnostics: fluorescence spectroscopy and elastic-scattering spectroscopy.. Phys Med Biol 1997 May;42(5):803-14.
          pubmed: 9172260doi: 10.1088/0031-9155/42/5/005google scholar: lookup
        2. Birch HL, Bailey AJ, Goodship AE. Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition.. Equine Vet J 1998 Nov;30(6):534-9.
          pubmed: 9844973doi: 10.1111/j.2042-3306.1998.tb04530.xgoogle scholar: lookup
        3. Butler DL, Grood ES, Noyes FR, Zernicke RF. Biomechanics of ligaments and tendons.. Exerc Sport Sci Rev 1978;6:125-81.
          pubmed: 394967
        4. Canpolat M, Mourant JR. Particle size analysis of turbid media with a single optical fiber in contact with the medium to deliver and detect white light.. Appl Opt 2001 Aug 1;40(22):3792-9.
          pubmed: 18360413doi: 10.1364/ao.40.003792google scholar: lookup
        5. Charvet I, Thueler P, Vermeulen B, Saint-Ghislain M, Biton C, Jacquet J, Bevilacqua F, Depeursinge C, Meda P. A new optical method for the non-invasive detection of minimal tissue alterations.. Phys Med Biol 2002 Jun 21;47(12):2095-108.
          pubmed: 12118603doi: 10.1088/0031-9155/47/12/307google scholar: lookup
        6. Crevier-Denoix N, Collobert C, Sanaa M, Bernard N, Joly C, Pourcelot P, Geiger D, Bortolussi C, Bousseau B, Denoix JM. Mechanical correlations derived from segmental histologic study of the equine superficial digital flexor tendon, from foal to adult.. Am J Vet Res 1998 Aug;59(8):969-77.
          pubmed: 9706200
        7. Diamant J, Keller A, Baer E, Litt M, Arridge RG. Collagen; ultrastructure and its relation to mechanical properties as a function of ageing.. Proc R Soc Lond B Biol Sci 1972 Mar 14;180(1060):293-315.
          pubmed: 4402469doi: 10.1098/rspb.1972.0019google scholar: lookup
        8. Fechete R, Demco DE, Blümich B, Eliav U, Navon G. Anisotropy of collagen fiber orientation in sheep tendon by 1H double-quantum-filtered NMR signals.. J Magn Reson 2003 May;162(1):166-75.
          pubmed: 12762993doi: 10.1016/s1090-7807(02)00200-8google scholar: lookup
        9. Gathercole LJ, Keller A. Crimp morphology in the fibre-forming collagens.. Matrix 1991 Jun;11(3):214-34.
          pubmed: 1870453doi: 10.1016/s0934-8832(11)80161-7google scholar: lookup
        10. Ghosh N, Mohanty SK, Majumder SK, Gupta PK. Measurement of optical transport properties of normal and malignant human breast tissue.. Appl Opt 2001 Jan 1;40(1):176-84.
          pubmed: 18356989doi: 10.1364/ao.40.000176google scholar: lookup
        11. Han S, Gemmell SJ, Helmer KG, Grigg P, Wellen JW, Hoffman AH, Sotak CH. Changes in ADC caused by tensile loading of rabbit achilles tendon: evidence for water transport.. J Magn Reson 2000 Jun;144(2):217-27.
          pubmed: 10828190doi: 10.1006/jmre.2000.2075google scholar: lookup
        12. Hansen KA, Weiss JA, Barton JK. Recruitment of tendon crimp with applied tensile strain.. J Biomech Eng 2002 Feb;124(1):72-7.
          pubmed: 11871607doi: 10.1115/1.1427698google scholar: lookup
        13. Johnston DE. Tendons, skeletal muscles, and ligaments in health and disease.. 1985;pp. 65–76.
        14. Kastelic J, Galeski A, Baer E. The multicomposite structure of tendon.. Connect Tissue Res 1978;6(1):11-23.
          pubmed: 149646doi: 10.3109/03008207809152283google scholar: lookup
        15. Khan KM, Cook JL, Bonar F, Harcourt P, Astrom M. Histopathology of common tendinopathies. Update and implications for clinical management.. Sports Med 1999 Jun;27(6):393-408.
          pubmed: 10418074doi: 10.2165/00007256-199927060-00004google scholar: lookup
        16. Kondoh T, Westesson PL. Ultrathin arthroscope for use in the lower compartment of the temporomandibular joint.. Oral Surg Oral Med Oral Pathol 1991 Aug;72(2):146-9.
          pubmed: 1923391doi: 10.1016/0030-4220(91)90153-4google scholar: lookup
        17. Kostyuk O, Brown RA. Orientation of collagen fibrils in tissue-engineered constructs can be determined using spatial anisotropy of diffused light reflectance.. Program and Abstract Booklet, 6th International Conf Cell Eng 20–22 August, 2003; Sydney, Australia. 2003. p. 21.
        18. Marenzana M, Pickard D, MacRobert AJ, Brown RA. Optical measurement of three-dimensional collagen gel constructs by elastic scattering spectroscopy.. Tissue Eng 2002 Jul;8(3):409-18.
          pubmed: 12167227doi: 10.1089/107632702760184673google scholar: lookup
        19. Marquez G, Wang LV, Lin SP, Schwartz JA, Thomsen SL. Anisotropy in the absorption and scattering spectra of chicken breast tissue.. Appl Opt 1998 Feb 1;37(4):798-804.
          pubmed: 18268655doi: 10.1364/ao.37.000798google scholar: lookup
        20. Nickell S, Hermann M, Essenpreis M, Farrell TJ, Krämer U, Patterson MS. Anisotropy of light propagation in human skin.. Phys Med Biol 2000 Oct;45(10):2873-86.
          pubmed: 11049177doi: 10.1088/0031-9155/45/10/310google scholar: lookup
        21. Shah JS, La Monaca A, Bigi A, Roveri N. X-ray diffraction and continuous small-angle scattering of turkey tendons with the improved area detector at Frascati.. Nucl Instrum Meth A 1991;A308:285–290.
        22. Schmitt JM, Kumar G. Optical scattering properties of soft tissue: a discrete particle model.. Appl Opt 1998 May 1;37(13):2788-97.
          pubmed: 18273225doi: 10.1364/ao.37.002788google scholar: lookup
        23. Stephens PR, Nunamaker DM, Butterweck DM. Application of a Hall-effect transducer for measurement of tendon strains in horses.. Am J Vet Res 1989 Jul;50(7):1089-95.
          pubmed: 2774333
        24. Tuchin VV. Light scattering study of tissues.. Physics – Uspekhi Fizicheskih Nauk (Russian Acad Sci) 1997;40:495–515.
        25. Williams IF, Heaton A, McCullagh KG. Cell morphology and collagen types in equine tendon scar.. Res Vet Sci 1980 May;28(3):302-10.
          pubmed: 7414083
        26. Ying M, Yeung E, Li B, Li W, Lui M, Tsoi CW. Sonographic evaluation of the size of Achilles tendon: the effect of exercise and dominance of the ankle.. Ultrasound Med Biol 2003 May;29(5):637-42.
          pubmed: 12754062doi: 10.1016/s0301-5629(03)00008-5google scholar: lookup
        27. Zonios G, Perelman LT, Backman V, Manoharan R, Fitzmaurice M, Van Dam J, Feld MS. Diffuse reflectance spectroscopy of human adenomatous colon polyps in vivo.. Appl Opt 1999 Nov 1;38(31):6628-37.
          pubmed: 18324198doi: 10.1364/ao.38.006628google scholar: lookup

        Citations

        This article has been cited 4 times.
        1. Hamandi F, Goswami T. Hierarchical Structure and Properties of the Bone at Nano Level. Bioengineering (Basel) 2022 Nov 10;9(11).
          doi: 10.3390/bioengineering9110677pubmed: 36354587google scholar: lookup
        2. Georgakoudi I, Rice WL, Hronik-Tupaj M, Kaplan DL. Optical spectroscopy and imaging for the noninvasive evaluation of engineered tissues. Tissue Eng Part B Rev 2008 Dec;14(4):321-40.
          doi: 10.1089/ten.teb.2008.0248pubmed: 18844604google scholar: lookup
        3. Yang L, van der Werf KO, Fitié CF, Bennink ML, Dijkstra PJ, Feijen J. Mechanical properties of native and cross-linked type I collagen fibrils. Biophys J 2008 Mar 15;94(6):2204-11.
          doi: 10.1529/biophysj.107.111013pubmed: 18032556google scholar: lookup
        4. Kostyuk O, Brown RA. Novel spectroscopic technique for in situ monitoring of collagen fibril alignment in gels. Biophys J 2004 Jul;87(1):648-55.
          doi: 10.1529/biophysj.103.038976pubmed: 15240498google scholar: lookup
        Subscribe to our newsletter
        Join 99,383 horse owners like you who receive our email updates on horse health and nutrition.