Ultrastructural study of tension and pressure zones in a rabbit flexor tendon

Merrilees, Mervyn J.; Flint, Michael H.

doi:10.1002/aja.1001570109

Cited by 157 publications

(81 citation statements)

References 39 publications

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“…On the concave (pressure) side the GAG content is -2.3-3.5%, of which 60% is chondroitin sulphate, whilst the associated collagen fibrils have a mass-average diameter of -150nm; in the tensional parts of the tendon, the GAG content is -0.2% (70% being dermatan sulphate) and the fibrils have a mass-average diameter -200 nm [44]. It has also been found that if the tendon is translocated forward so that it is subjected only to tensional forces, profound biochemical and morphological changes occur [35,43,45].…”

Section: Discussionmentioning

confidence: 99%

A role for glycosaminoglycans in the development of collagen fibrils

et al. 1982

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Extensive data on the glycosaminoglycan (GAG) composition and the collagen fibril diameter distribution have been collected for a diverse range of connective tissues. It is shown that tissues with the smallest diameter collagen fibrils (mass-average diameter < 60 nm) have high concentrations of hyaluronic acid and that tissues with the largest diameter collagen fibrils (mass-average diameter -200nm) have high concentrations of dermatan sulphate. It is suggested that the lateral growth of fibrils beyond a diameter of about 60nm is inhibited by the presence of an excess of hyaluronic acid but that this inhibitory effect may be removed by an increasing concentration of chondroitin sulphate and/or dermatan sulphate. It is also postulated that high concentrations of chondroitin sulphate will inhibit fibril growth beyond a massaverage diameter of -150nm. Such an inhibition may in turn be removed by an increasing concentration of dermatan sulphate such that it becomes the dominant GAG present in the tissue. Glycosaminoglycan Collagen fibriI Fibrillogenesis Connective tissue development

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Section: Discussionmentioning

confidence: 99%

A role for glycosaminoglycans in the development of collagen fibrils

et al. 1982

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“…18 However, Type II collagen has been shown to be present in both medial meniscal attachments in the uncalcified fibrocartilage, calcified fibrocartilage, and the ligamentous zone 16 ; as well as aggrecan has been found in insertion sites of ligaments. 34 Inasmuch as this type of collagen, usually found where aggrecan is present, 27 is normally related with compression and shear forces, 29,32 we might speculate that both insertion sites in meniscal attachments are subjected to tensile and compressive load in the loaded knee joint. It should be noted that our GAG fraction analysis is only semi-quantitative, comparing only relative amounts of GAG between regions and zones based on staining intensity.…”

Section: Discussionmentioning

confidence: 99%

A Quantitative Study of the Microstructure and Biochemistry of the Medial Meniscal Horn Attachments

Villegas

Hansen

Liu³

et al. 2007

Ann Biomed Eng

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Abstract-Little quantitative data is available on the structure of meniscal attachments. Therefore, as an aid to designing meniscal replacements as well as a possible explanation for mechanical behavior, this study was designed to further the knowledge of the microstructure and biochemistry of native meniscal attachments. Bovine medial meniscal attachments (the external ligamentous portion as well as the transition zones at the bony insertion) were removed and prepared for microstructural evaluation. After embedding in paraffin, the samples were sliced on a microtome and stained for quantitative analysis. The anterior and posterior insertion sites are known to contain three zones: subchondral bone, calcified fibrocartilage, and uncalcified fibrocartilage. Additionally, others have shown that the anterior insertion site contains a ligamentous zone. The insertion zones were further divided into proximal, middle, and distal zones. The posterior attachment's insertion site had a significantly greater thickness of interdigitations, subchondral bone, uncalcified fibrocartilage, and calcified fibrocartilage zone thickness compared to the anterior attachment insertion. The anterior attachment's insertion had the greatest GAG fraction in each zone when compared to the posterior attachment's insertion. GAG fraction decreased from the meniscus to the subchondral bone. Both GAG fraction and normalized thickness varied within a given zone, decreasing from the distal to proximal regions in both the anterior and posterior attachments' insertion zones. Crimp frequency of the collagen fibrils in the external ligamentous portion of the tissue was homogeneous along the length. The findings from this study agree with previously published material property data on the medial meniscal attachments, and could be used in the future to design methods of attachment for tissue engineered replacement menisci.

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“…In general, tendon matrices are composed of collagen (mainly type I collagen) GAGs and PGs (19,25). Little alteration from the reaction of azan staining in the incubated tendon tissue blocks was found, suggesting that the amount of collagen fibrils in the tendon changed very little during the incubation period of 96 h. To understand the collagen turnover (synthesis and decomposition of collagen fibrils) in cultured tendon tissue blocks, we are currently carrying out an experiment to determine whether the blocks of tendon tissue have the ability to synthesis collagen fibrils during incubation.…”

Section: Discussionmentioning

confidence: 99%

Structure and component alteration of rabbit Achilles tendon in tissue culture

et al. 2005

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The aim of this study was to investigate alterations of cultured tendon tissues to determine whether tissue culture is a useful method for biological analyses of the tendon. Tendon tissues for tissue culture were isolated from Achilles tendons of rabbits. The tendon segments were placed one segment per well and incubated in growth medium consisting of Dullbecco's modified Eagle's medium supplemented with 5% fetal bovine serum at 37°C in a humidified atmosphere with 5% CO 2 for various periods. The alignment of collagen fibrils was preserved for 48 h, but tendon structure has disintegrated at 96 h. Alcian blue staining and gelatine zymography revealed that proteoglycan markedly diminished and that matrix metalloproteinase (MMPs) activity was upregulated sharply at 72 and 96 h. The ratio of collagen fibrils with large diameter had increased and the mean diameter and mass average diameter value had reached maximum at 48 h. The values then decreased and mean diameters at 72 and 96 h were significantly different from that at 48 h. At 96 h, the ratio of collagen fibrils with small diameters had increased and collagen fibrils with large diameters had disappeared. These findings indicate that structural alteration is possible to be induced by disintegration of collagen fibrils and disappearance of glycosaminoglycans from extracellular matrix (ECM), subsequent of upregulation of MMPs activity. Although the study period is limited, the tissue culture method is available for investigating cell-ECM interaction in tendons.Tendon, which is dense connective tissue, consist of type I collagen and elastin embedded in a proteoglycan (PG)-water matrix, with collagen accounting for 70% and a miniscle amount of elastin (11,18). These elements, extracellular matrices (ECMs), are produced, synthesized and digested by tenoblasts and tendinocytes (19). There is a very intimate relation between the cell and ECM.The best way to understand cell-and-ECM interaction in vitro is to carry out experiments under similar to in vivo conditions, such as tissue culture. The tissue culture method has its advantage to investigate and observe the cell-and-ECM interaction easily. Methods of tissue culture are well established and widely used for the study of blood vessels (34, 38), lungs (26), uterus (3), testis (24) and intestines (21), whereas only a few studies have been reported in tissue culture of tendon (20,23,32). In vitro study of tendon has been mainly demonstrated by cell cultures on plastic plates. If tissue culture method for tendon is established, it will be a useful tool for investigating interaction of cells and ECM in a tendon and alteration in tendon tissue during degen-

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Ultrastructural study of tension and pressure zones in a rabbit flexor tendon

Cited by 157 publications

References 39 publications

A role for glycosaminoglycans in the development of collagen fibrils

A role for glycosaminoglycans in the development of collagen fibrils

A Quantitative Study of the Microstructure and Biochemistry of the Medial Meniscal Horn Attachments

Structure and component alteration of rabbit Achilles tendon in tissue culture

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