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Home / Equine Research Bank / J Anat / Concerted and adaptive alignment of decorin dermatan sulfate...
Journal of anatomy2011; 220(2); 156-163; doi: 10.1111/j.1469-7580.2011.01456.x

Concerted and adaptive alignment of decorin dermatan sulfate filaments in the graded organization of collagen fibrils in the equine superficial digital flexor tendon.

Abstract: The equine superficial digital flexor tendon (SDFT) has a graded distribution of collagen fibril diameters, with predominantly small-diameter fibrils in the region of the myotendinous junction (MTJ), a gradual increase in large-diameter fibrils toward the osteotendinous junction (OTJ), and a mixture of small- and large-diameter fibrils in the middle metacarpal (MM) region. In this study, we investigated the ultrastructure of the SDFT, to correlate the spatial relationship of the collagen fibrils with the graded distribution. The surface-to-surface distances of pairs of fibrils were found to be almost constant over the entire tendon. However, the center-to-center distances varied according to fibril diameter. Decorin is the predominant proteoglycan in normal mature tendons, and has one dermatan sulfate (DS) or chondroitin sulfate (CS) filament as a side chain which is associated with the surfaces of the collagen fibrils via its core protein. We identified a coordinated arrangement of decorin DS filaments in the equine SDFT. The sizes of the decorin DS filaments detected by Cupromeronic blue staining showed a unique regional variation; they were shortest in the MM region and longer in the MTJ and OTJ regions, and a considerable number of filaments were arranged obliquely to adjacent collagen fibrils in the MTJ region. This regional variation of the filaments may be an adaptation to lubricate the interfibrillar space in response to local mechanical requirements. The results of this study suggest that the MTJ region, which receives the muscular contractile force first, acts as a buffer for mechanical forces in the equine SDFT.
© 2011 The Authors. Journal of Anatomy © 2011 Anatomical Society.
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Publication Date: 2011-11-28 PubMed ID: 22122012PubMed Central: PMC3275770DOI: 10.1111/j.1469-7580.2011.01456.xGoogle Scholar: Lookup
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  • Journal Article

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.

The research investigates the structure of an equine tendon and the distribution of collagen fibril diameters, finding a correlation between fibril distribution and spatial relationship. Specifically, it observes the role of a protein, decorin, which is linked to collagen fibrils and appears to have a unique regional variation.

Overview of The Research

  • The research focuses on the superficial digital flexor tendon (SDFT) in horses, particularly the arrangement of collagen fibrils. Collagen is an important substance that provides structure and strength to bodily tissues such as tendons. The study found a varied distribution of fibril diameters within different regions of the tendon.
  • The distribution of fibrils had a significant degree of gradation from the myotendinous junction (MTJ) where the tendon joins a muscle, to the osteotendinous junction (OTJ) where it connects to bone, and finally in the middle metacarpal (MM) region, located in the central part of the horse’s leg. This careful organization is likely due to the different mechanical requirements of these regions.

Decorin Dermatan Sulfate (DS) Filaments

  • The researchers honed in on a protein called decorin, abundant in normal mature tendons. This protein has a side chain – a branch-off from the main chain of its molecular structure – which can be either dermatan sulfate (DS) or chondroitin sulfate (CS). This side chain becomes associated with the surfaces of collagen fibrils via the ‘core’ part of the decorin protein.
  • The team noticed a consistently arranged pattern of these decorin DS filaments in the horse’s SDFT. More interestingly, they observed a unique regional variation in the lengths of the decorin DS filaments. The shortest filaments were situated in the MM region while longer filaments were present in the MTJ and OTJ regions.

Implications of the Findings

  • From these findings, the team formulated a hypothesis that the regional variation of filament lengths might be an adaptive response of the tendon to its local mechanical needs. Specifically, the longer filaments near the muscle and bone junctions could potentially serve to lubricate interfibrillar spaces, reducing friction and allowing for smoother action when the tendon is put under strain.
  • In conclusion, it appears that the MTJ region may act as a buffer for the mechanical forces generated by muscle contraction, being the area first to receive these forces. The structural arrangement of collagen fibrils and the unique regional distribution of decorin DS filaments play a crucial role in this buffering mechanism.

Cite This Article

APA
Watanabe T, Imamura Y, Suzuki D, Hosaka Y, Ueda H, Hiramatsu K, Takehana K. (2011). 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, 220(2), 156-163. https://doi.org/10.1111/j.1469-7580.2011.01456.x

Publication

Journal of anatomy
ISSN: 1469-7580
NlmUniqueID: 0137162
Country: England
Language: English
Volume: 220
Issue: 2
Pages: 156-163

Researcher Affiliations

Watanabe, Takafumi
  • Laboratory of Animal Functional Anatomy, Department of Food Production Science, Faculty of Agriculture, Shinshu University, Nagano, Japan.
Imamura, Yasutada
    Suzuki, Daisuke
      Hosaka, Yoshinao
        Ueda, Hiromi
          Hiramatsu, Kohzy
            Takehana, Kazushige

              MeSH Terms

              • Animals
              • Blotting, Western
              • Collagen / chemistry
              • Collagen / ultrastructure
              • Decorin / analysis
              • Dermatan Sulfate / analysis
              • Electrophoresis
              • Horses / anatomy & histology
              • Microscopy, Electron
              • Tendons / chemistry
              • Tendons / ultrastructure

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              Citations

              This article has been cited 8 times.
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