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The Journal of veterinary medical science2005; 67(9); 855-860; doi: 10.1292/jvms.67.855

Control of the collagen fibril diameter in the equine superficial digital flexor tendon in horses by decorin.

Abstract: The distribution pattern of collagen fibril diameter in the equine superficial digital flexor tendon (SDFT) is known to differ in central and peripheral areas of some regions. This study reports the essence of collagen fibril differences among different regions of the equine SDFT by transmission electron microscopic (TEM) and high-voltage electron microscopic observations and biochemical analysis. The distribution of large collagen fibrils increased but the density of collagen fibrils decreased from the proximal metacarpal region to the distal metacarpal region. Large collagen fibrils with an irregular cross-sectional profile were found more frequently in the middle metacarpal region than in other regions. Three-dimensional reconstruction of images of irregularly shaped collagen fibrils revealed that these fibrils are formed through fusion of small collagen fibrils with large ones. The amount of decorin, which reportedly inhibits the lateral fusion of collagen fibrils, decreased in the direction of the distal metacarpal region. On the other hand, the size of decorin gradually increased in the direction of the distal metacarpal region. These results suggest that regional differences in collagen fibril distribution and density of collagen fibrils in the SDFT are due, at least in part, to fusion of collagen fibrils and the concomitant regional differences in the amount and size of decorin.
Publication Date: 2005-10-08 PubMed ID: 16210795DOI: 10.1292/jvms.67.855Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article investigates how the collagen fibril diameter in the equine superficial digital flexor tendon (SDFT) in horses is controlled by decorin. It also explores how variation in decorin levels and size in different regions of the tendon leads to differences in collagen fibril distribution and density.

Understanding Collagen Fibril Differences in The Equine SDFT

  • The study discusses the differences of collagen fibril diameters in various regions of the equine SDFT which have been observed through transmission and high-voltage electron microscopic examinations and biochemical analysis.
  • The investigation shows an increase of large collagen fibril distribution and a decrease in fibril density from the proximal to distal metacarpal region.
  • Additionally, collagen fibrils with irregular cross-sections were more prevalent in the middle metacarpal region than in others, suggesting the potential formation of these fibrils through a fusion process between small and large fibrils.

The Role of Decorin in Collagen Fibril Formation

  • The amount of decorin, a protein that inhibits the lateral fusion of collagen fibrils, was found to decrease towards the distal metacarpal region.
  • Conversely, the size of decorin molecules was found to increase in the direction of the distal metacarpal region.

Impact of Decorin on Fibril Distribution and Density

  • The researchers propose that the regional differences observed in collagen fibril distribution and density in the SDFT are likely influenced in part by the fusion process of collagen fibrils.
  • It is suggested that changes in the amount and size of decorin in different regions contribute to this fusion process, leading to the observed differences in collagen fibril characteristics across regions.

This research opens up new avenues for understanding the mechanical properties of tendons and how they can be influenced by biological factors like proteins, thereby potentially informing the development of therapeutic strategies for tendon injuries or pathologies.

Cite This Article

APA
Watanabe T, Hosaka Y, Yamamoto E, Ueda H, Sugawara K, Takahashi H, Takehana K. (2005). Control of the collagen fibril diameter in the equine superficial digital flexor tendon in horses by decorin. J Vet Med Sci, 67(9), 855-860. https://doi.org/10.1292/jvms.67.855

Publication

ISSN: 0916-7250
NlmUniqueID: 9105360
Country: Japan
Language: English
Volume: 67
Issue: 9
Pages: 855-860

Researcher Affiliations

Watanabe, Takafumi
  • Department of Veterinary Anatomy, School of Veterinary Medicine, Rakuno Gakuen University, Hokkaido, Japan.
Hosaka, Yoshinao
    Yamamoto, Etsuko
      Ueda, Hiromi
        Sugawara, Kenji
          Takahashi, Heishichiro
            Takehana, Kazushige

              MeSH Terms

              • Animals
              • Blotting, Western / veterinary
              • Decorin
              • Extracellular Matrix Proteins
              • Fibrillar Collagens / metabolism
              • Fibrillar Collagens / ultrastructure
              • Forelimb / anatomy & histology
              • Forelimb / metabolism
              • Horses / anatomy & histology
              • Microscopy, Electron, Transmission / veterinary
              • Proteoglycans / metabolism
              • Tendons / ultrastructure

              Citations

              This article has been cited 10 times.
              1. Ribitsch I, Gueltekin S, Keith MF, Minichmair K, Peham C, Jenner F, Egerbacher M. Age-related changes of tendon fibril micro-morphology and gene expression.. J Anat 2020 Apr;236(4):688-700.
                doi: 10.1111/joa.13125pubmed: 31792963google scholar: lookup
              2. Thankam FG, Dilisio MF, Gross RM, Agrawal DK. Collagen I: a kingpin for rotator cuff tendon pathology.. Am J Transl Res 2018;10(11):3291-3309.
                pubmed: 30662587
              3. Takahashi N, Hirose T, Minaguchi JA, Ueda H, Tangkawattana P, Takehana K. Fibrillar architecture at three different sites of the bovine superficial digital flexor tendon.. J Vet Med Sci 2018 Mar 24;80(3):405-412.
                doi: 10.1292/jvms.17-0562pubmed: 29332865google scholar: lookup
              4. Szczesny SE, Fetchko KL, Dodge GR, Elliott DM. Evidence that interfibrillar load transfer in tendon is supported by small diameter fibrils and not extrafibrillar tissue components.. J Orthop Res 2017 Oct;35(10):2127-2134.
                doi: 10.1002/jor.23517pubmed: 28071819google scholar: lookup
              5. Hirose T, Ogura T, Tanaka K, Minaguchi J, Yamauchi T, Fukada T, Koyama Y, Takehana K. Comparative study of dermal components and plasma TGF-β1 levels in Slc39a13/Zip13-KO mice.. J Vet Med Sci 2015 Nov;77(11):1385-9.
                doi: 10.1292/jvms.15-0015pubmed: 26050750google scholar: lookup
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                doi: 10.1002/jor.22848pubmed: 25664422google scholar: lookup
              7. Shinozaki A, Takagi S, Hosaka YZ, Uehara M. The fibrous tapetum of the horse eye.. J Anat 2013 Nov;223(5):509-18.
                doi: 10.1111/joa.12100pubmed: 24102505google scholar: lookup
              8. Dunkman AA, Buckley MR, Mienaltowski MJ, Adams SM, Thomas SJ, Satchell L, Kumar A, Pathmanathan L, Beason DP, Iozzo RV, Birk DE, Soslowsky LJ. Decorin expression is important for age-related changes in tendon structure and mechanical properties.. Matrix Biol 2013 Jan;32(1):3-13.
                doi: 10.1016/j.matbio.2012.11.005pubmed: 23178232google scholar: lookup
              9. Watanabe T, Imamura Y, Suzuki D, Hosaka Y, Ueda H, Hiramatsu K, Takehana K. Concerted and adaptive alignment of decorin dermatan sulfate filaments in the graded organization of collagen fibrils in the equine superficial digital flexor tendon.. J Anat 2012 Feb;220(2):156-63.
              10. Song Y, Hong X, Yu Y, Lin Y. Changes of collagen type III and decorin in paraurethral connective tissue from women with stress urinary incontinence and prolapse.. Int Urogynecol J Pelvic Floor Dysfunct 2007 Dec;18(12):1459-63.
                doi: 10.1007/s00192-007-0356-2pubmed: 17396208google scholar: lookup