Atomic Force Microscopy for High Resolution Imaging of Collagen Fibrils—A New Technique to Investigate Collagen Structure in Historic Bone Tissues

Thalhammer, Stefan; Heckl, Wolfgang M.; Zink, Albert; Nerlich, Andreas

doi:10.1006/jasc.2000.0644

Cited by 22 publications

(15 citation statements)

References 22 publications

(18 reference statements)

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“…It has also been found that the different types of collagen have different structures and that type I collagen typically forms thicker fibrils than type III collagen [29]. This result, however, is tissue or substrate dependent.…”

Section: Introductionmentioning

confidence: 97%

Collagen adsorption and structure on polymer surfaces observed by atomic force microscopy

Woodcock

Johnson

Chen

2005

Journal of Colloid and Interface Science

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Section: Introductionmentioning

confidence: 97%

Collagen adsorption and structure on polymer surfaces observed by atomic force microscopy

Woodcock

Johnson

Chen

2005

Journal of Colloid and Interface Science

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“…Moreover, AFM probes the surface of materials, and can thus provide only 2D information on the organization of the ultrastructure. This is why AFM's numerous applications in bone research [253,254] have been mainly focused on the study of its mechanical properties at a tissue [255][256][257] and single fibril level [258][259][260], while very few studies have investigated the organization of the mineralized collagen fibrils [261,262] ( figure 15). However, similarly to TEM, AFM has been extensively used to examine bone features at the nanometre scale, such as the size of mineral platelets [13,264], collagen fibril characteristics (e.g.…”

Section: Other Imaging Techniques 2341 Atomic Force Microscopymentioning

confidence: 99%

Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Georgiadis

Müller

Schneider

2016

J. R. Soc. Interface.

113

100

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Bone's remarkable mechanical properties are a result of its hierarchical structure. The mineralized collagen fibrils, made up of collagen fibrils and crystal platelets, are bone's building blocks at an ultrastructural level. The organization of bone's ultrastructure with respect to the orientation and arrangement of mineralized collagen fibrils has been the matter of numerous studies based on a variety of imaging techniques in the past decades. These techniques either exploit physical principles, such as polarization, diffraction or scattering to examine bone ultrastructure orientation and arrangement, or directly image the fibrils at the sub-micrometre scale. They make use of diverse probes such as visible light, X-rays and electrons at different scales, from centimetres down to nanometres. They allow imaging of bone sections or surfaces in two dimensions or investigating bone tissue truly in three dimensions, in vivo or ex vivo, and sometimes in combination with in situ mechanical experiments. The purpose of this review is to summarize and discuss this broad range of imaging techniques and the different modalities of their use, in order to discuss their advantages and limitations for the assessment of bone ultrastructure organization with respect to the orientation and arrangement of mineralized collagen fibrils.

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“…Surprisingly, collagen fibers of deep layers of elephant knee joint cartilage were generally thicker (230 nm) than expected for collagen type II (100 nm, see Thalhammer et al 2001) which is the major collagen type in cartilage (Alberts et al, 2004). On the other hand, increasing fiber diameter from the articular surface to bone tissue, as it was found in the elephant, is well known in other mammals (Zambrano et al, 1982).…”

Section: Adaptation Of the Knee Joint Cartilage Of The African Elephamentioning

confidence: 92%

Articular cartilage in the knee joint of the African elephant, Loxodonta africana, Blumenbach 1797

Egger

Witter

Weissengruber

et al. 2007

Journal of Morphology

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Knee joints of one adult and three juvenile African elephants were dissected. The specific features of the articular cartilage with particular reference to matrix components were studied by light and electron microscopy and immunohistochemistry. The elephant knee joint cartilage contains an unusually low concentration of proteoglycans resulting in rather eosinophilic staining properties of the matrix. The very thick collagen fibers of the cartilage possibly represent collagen I. Except for the different thickness of cartilage at the weight-bearing surfaces of femur (approximately 6.7 mm) and tibia (approximately 11.2 mm) in juvenile elephants, light and electron microscopy did not reveal distinct topographical differences in cartilage structure, perhaps because of the high congruency of the articulating surfaces and resulting uniform load distribution in the knee. The number of cell profiles per section area of both femoral (approximately 950 cell profiles/mm(2)) and tibial cartilage (approximately 898 cell profiles/mm(2)) was low, indicating excessive matrix production by the chondrocytes during cartilage development. These unique properties could be a result of the enormous compressive load resting on the elephant knee. Maintenance of the equilibrium between biological function and resistance to compression seems to be crucial in the elephant knee joint cartilage. Any disturbance that interferes with this equilibrium appears to lead to arthrotic alterations, as particularly seen in captive elephants.

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Atomic Force Microscopy for High Resolution Imaging of Collagen Fibrils—A New Technique to Investigate Collagen Structure in Historic Bone Tissues

Cited by 22 publications

References 22 publications

Collagen adsorption and structure on polymer surfaces observed by atomic force microscopy

Collagen adsorption and structure on polymer surfaces observed by atomic force microscopy

Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Articular cartilage in the knee joint of the African elephant, Loxodonta africana, Blumenbach 1797

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