Cell morphology and collagen types in equine tendon scar

Williams, I.F.; Heaton, A.; McCullagh, K.G.

doi:10.1016/s0034-5288(18)32713-9

Cited by 110 publications

(79 citation statements)

References 21 publications

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“…Collagen fibrils are hybrid fibrils formed by interactions between these GRADED ARRANGEMENT OF COLLAGEN FIBRILS 333 collagens, although type I collagen is predominantly involved. An increase in the relative ratio of type III or V collagens to type I collagen apparently regulates the collagen fibril diameter negatively [9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Graded Arrangement of Collagen Fibrils in the Equine Superficial Digital Flexor Tendon

Watanabe

Imamura

Hosaka

et al. 2007

Connective Tissue Research

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By using ultramorphological and biochemical methods, we analyzed the regional differences between the three parts of the equine superficial digital flexor tendon (SDFT), namely, the myotendinous junction (MTJ), middle metacarpal (mM), and osteotendinous junction (OTJ). Cross-sectional images showed unique distributions of collagen fibrils of varying diameters in each region. Small collagen fibrils (diameter <100 nm) were distributed predominantly in the MTJ region, and the OTJ region was relatively rich in large collagen fibrils (diameter >200 nm). In the mM region, the collagen fibrils were intermediately distributed between the MTJ and OTJ. The results indicate a graded arrangement of collagen fibrils in the tendon. Type V collagen was detected preferentially in the MTJ region. Since type V collagen is believed to be one of the collagens regulating collagen fibril formation, its possible functionality in the MTJ region in terms of fibril formation and fibril arrangement in the tendon has been discussed here.

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Section: Introductionmentioning

confidence: 99%

Graded Arrangement of Collagen Fibrils in the Equine Superficial Digital Flexor Tendon

Watanabe

Imamura

Hosaka

et al. 2007

Connective Tissue Research

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“…There is potential that the increased type I collagen in the matrix may improve the strength of the repaired tendon in the M + S group. During tendon repair, type III collagen is increased initially and persistent in scaring tissue [34,35]. In the present study, type III collagen was indifference among the three groups in either staining area or intensity.…”

Section: Discussionmentioning

confidence: 43%

Efficacy of a mesenchymal stem cell loaded surgical mesh for tendon repair in rats

Schon

Gill

Thorpe

et al. 2014

Journal of Translational Medicine

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ObjectivesThe purpose of this study was to investigate the efficacy of a composite surgical mesh for delivery of mesenchymal stem cells (MSCs) in tendon repair.MethodsThe MSC-loaded mesh composed of a piece of conventional surgical mesh and a layer of scaffold, which supported MSC-embedded alginate gel. A 3-mm defect was surgically created at the Achilles tendon-gastrocnemius/soleus junction in 30 rats. The tendon defects were repaired with either 1) MSC-loaded mesh; or 2) surgical mesh only; or 3) routine surgical suture. Repaired tendons were harvested at days 6 and 14 for histology, which was scored on the bases of collagen organization, vascularity and cellularity, and immunohistochemisty of types I and III collagen.ResultsIn comparison with the other two repair types, at day 6, the MSC-loaded mesh significantly improved the quality of the repaired tendons with dense and parallel collagen bundles, reduced vascularity and increased type I collagen. At day 14, the MSC-loaded mesh repaired tendons had better collagen formation and organization.ConclusionThe MSC-loaded mesh enhanced early tendon healing, particularly the quality of collagen bundles. Application of the MSC-loaded mesh, as a new device and MSC delivery vehicle, may benefit to early functional recovery of the ruptured tendon.

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“…An emerging picture is that there is a spatiotemporal resemblance between expressions of collagen type I, collagen type II, and bIG-H3 mRNA during murine embryogenesis, indicating a physiologically important interaction. This possibility is underscored by the findings that in vitro, bIG-H3 binds collagens (Hashimoto et al 1997) which are primary components of MTJs and also of cartilage and bone (Williams et al 1980;Cheah et al 1991;Birk and Mayne 1997). Ultrastructural analysis revealed that bIG-H3 localized to regions where fibrils appear to intersect in the extracellular space.…”

Section: Results Show Values and Their Sdmentioning

confidence: 99%

The extracellular matrix protein ?IG-H3 is expressed at myotendinous junctions and supports muscle cell adhesion

Ferguson

Thoma

Mikesh

et al. 2003

Cell and Tissue Research

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Molecules of the extracellular matrix (ECM) play important roles in the development and maintenance of myotendinous junctions (MTJs), specialized regions of muscle to bone union. In this report we provide evidence that skeletal muscle cells synthesize the collagen- and fibronectin-binding ECM protein betaIG-H3 and that betaIG-H3 is localized to MTJs. In situ hybridization experiments revealed that during E16.5-E18.5 of murine development, betaIG-H3 RNA transcripts were expressed where developing skeletal muscle fibers contact primordial cartilage and bone. Immunohistochemical analysis verified that the betaIG-H3 protein itself localized distinctively at MTJs, and ultrastructural analysis suggested that betaIG-H3 associates with extracellular fibers and the surface of cells. In vitro, recombinant betaIG-H3 functioned as an adhesion substratum for skeletal muscle cells. Adhesion was significantly reduced by anti-integrin alpha7 and beta1 antibodies, suggesting that betaIG-H3 binds to skeletal muscle cells via alpha7beta1 integrin. Localization of betaIG-H3 to the termini of skeletal muscle fibers and the binding of betaIG-H3 to cells and to molecules of the ECM suggests that betaIG-H3 may play an organizational and structural role in developing MTJs, linking skeletal muscle to components of the ECM.

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Cell morphology and collagen types in equine tendon scar

Cited by 110 publications

References 21 publications

Graded Arrangement of Collagen Fibrils in the Equine Superficial Digital Flexor Tendon

Graded Arrangement of Collagen Fibrils in the Equine Superficial Digital Flexor Tendon

Efficacy of a mesenchymal stem cell loaded surgical mesh for tendon repair in rats

The extracellular matrix protein ?IG-H3 is expressed at myotendinous junctions and supports muscle cell adhesion

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