Collagen Arrangement in Cartilages

Zambrano, N.Z.; Montes, G. S.; Shigihara, Kae; Sánchez, E.; Junqueira, L. C.

doi:10.1159/000145534

Cited by 75 publications

(46 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Usually, when G is 0n1-0n2 or less, the section practically represents an infinite 2-D section plane of the object and the bias is negligible (Weibel & Paumgartner, 1978). At the ultrastructural level, however, where section thickness varies between 30 and 80 nm and the diameter of collagen fibrils varies from 5-15 to 120 nm (Zambrano et al 1982 ;Hedlund et al 1993), the relative section thickness is high, varying from 0n25 to 16, and the stereological probe, instead of representing a 2-D section plane, is a 3-D ' thick ' section having a volume. In this case the bias caused by the overprojection of the fibrils, overlapping of the projected fibrils, and truncation, i.e.…”

Section: mentioning

confidence: 99%

Electron microscopic stereological study of collagen fibrils in bovine articular cartilage: volume and surface densities are best obtained indirectly (from length densities and diameters) using isotropic uniform random sampling

et al. 1999

View full text Add to dashboard Cite

Results obtained by the indirect zonal isotropic uniform random (IUR) estimation were compared with those obtained by the direct point and interception counting methods on vertical (VS) or IUR sections in a stereological study of bovine articular cartilage collagen fibrils at the ultrastructural level. Besides comparisons between the direct and indirect estimations (direct IUR vs indirect IUR estimations) and between different sampling methods (VS vs IUR sampling), simultaneous comparison of the 2 issues took place (direct VS vs indirect IUR estimation). Using the direct VS method, articular cartilage superficial zone collagen volume fraction (V v 41 %) was 67 % and fibril surface density (S v 0n030 nm#\nm$) 15 % higher (P 0n05) than values obtained by the indirect IUR method (V v 25 % and S v 0n026 nm#\nm$). The same was observed when the direct IUR method was used : collagen volume fraction (V v 40 %) was 63 % and fibril surface density (S v 0n032 nm#\nm$) 21 % higher (P 0n05) than those obtained by the indirect IUR technique. Similarly, in the deep zone of articular cartilage direct VS and direct IUR methods gave 50 and 55 % higher (P 0n05) collagen fibril volume fractions (V v 43 and 44 % vs 29 %) and the direct IUR method 25 % higher (P 0n05) fibril surface density values (S v 0n025 vs 0n020 nm#\nm$) than the indirect IUR estimation. On theoretical grounds, scrutiny calculations, as well as earlier reports, it is concluded that the direct VS and direct IUR methods systematically overestimated the V v and S v of collagen fibrils. This bias was due to the overprojection which derives from the high section thickness in relation to collagen fibril diameter. On the other hand, factors that during estimation tend to underestimate V v and S v , such as profile overlapping and truncation (' fuzzy ' profiles), seemed to cause less bias. As length density (L v ) and collagen fibril diameter are minimally biased by the high relative section thickness, the indirect IUR method, based on utilisation of these estimates, is here regarded as representing a ' gold standard '. The sensitivity of these 3 methods was also tested with cartilage from an in vitro loading experiment which caused tissue compression. In the superficial zone of articular cartilage V v and S v of collagen fibrils increased (P 0n05). This difference in the stereological estimates was only detected by the indirect IUR estimation but not by the direct VS or direct IUR methods. This indicated that the indirect IUR estimation was more sensitive than the direct VS or direct IUR estimations. On the basis of these observations, the indirect zonal IUR estimation can be regarded as the technique of choice in the electron microscopic stereology of cartilage collagen.

show abstract

Section: mentioning

confidence: 99%

Electron microscopic stereological study of collagen fibrils in bovine articular cartilage: volume and surface densities are best obtained indirectly (from length densities and diameters) using isotropic uniform random sampling

et al. 1999

View full text Add to dashboard Cite

show abstract

“…7, 8,11). Collagen type II, which is present in hyaline and elastic cartilages, does not form fibers and displays a weak birefringence of a variable color (ZAMBRANo et al, 1982) (Fig. 9).…”

Section: Histochemistrymentioning

confidence: 99%

“…The enhancement of birefringence in Picrosirius-stained sections studied by polarization microscopy has been shown to be specific for collagen. x 100 the interaction of collagen molecules with the ground substance (ZAMBRANO et al, 1982). It is thus evident that, in the 5 to 7 pm sections routinely used in histology, the different colors and intensities of birefringence displayed by collagen types I, II or III, are due to differences in their patterns of physical aggregation.…”

Section: Histochemistrymentioning

confidence: 99%

“…14). On the other hand, fibril diameters are larger and more variable in articular cartilages (resembling the collagen type I fibril diameters of fibrous cartilages, which suggests that collagen fibrils in cartilages that support high pressures such as articular and fibrous cartilages differ from the collagen fibrils of the hyaline and elastic cartilages not subjected to strong pressures) (ZAMBRANO et al, 1982).…”

Section: Collagen Type IImentioning

confidence: 99%

“…Thus, in the upper region collagen is disposed parallel to the articular surface, while the collagen in the deeper layers (lower region) shows a perpendicular orientation. A recent report (ZAMBRANO et al, 1982) has shown that the different types of cartilage present characteristic patterns of collagen arrangement which are related to their function. x 330.…”

Section: Collagen Type IIImentioning

confidence: 99%

See 2 more Smart Citations

Biology of collagen-proteoglycan interaction.

Junqueira

Montes

1983

Arch. Histol. Jap., Arch. Histol. Jpn

View full text Add to dashboard Cite

Amianthoid (Asbestoid) transformation: Electron microscopical studies on aging human costal cartilage

Mallinger¹,

Stockinger²

1988

Am. J. Anat.

View full text Add to dashboard Cite

The present study reports on the fine structure of human costal cartilage at different ages in order to obtain information on the morphogenesis of amianthoid fibers. Our results reveal an overall increase of collagen fibril diameter with increasing age, even in areas with no signs of amianthoid transformation. Ultrastructural evidence is presented that this increase in diameter is due to a gathering of the preexisting collagen fibrils. The age-related change in collagen fibril diameter is paralleled by changes in the composition and ultrastructural appearance of cartilage proteoglycans (as revealed by acridine orange staining). Acridine-orange-positive filaments indicative for proteoglycans are markedly reduced in size with advancing age in centrally located regions of costal cartilage. Treatment with testicular hyaluronidase previous to acridine-orange staining leaves these small proteoglycan filaments unaffected. By contrast, the filaments visible after acridine-orange staining in the extracellular matrix near to the perichondrium are susceptible to hyaluronidase treatment. Infrequently, a sharp increase in collagen fibril diameter can be observed in territorial matrix areas of degenerating chondrocytes. This observation is conspicuous at ages of 10 and 20 years. Amianthoid transformation is characterized by the appearance of collagen fibrils strictly arranged in parallel. These amianthoid fibers are embedded in a matrix rich in small acridine-orange-positive filaments similar to the proteoglycan filaments observed in centrally located matrix regions. It can be concluded that extensive remodelling not only of the collagen fibrils but also of the cartilage proteoglycans is involved in the development of amianthoid transformation.

show abstract

Collagen Arrangement in Cartilages

Cited by 75 publications

References 10 publications

Electron microscopic stereological study of collagen fibrils in bovine articular cartilage: volume and surface densities are best obtained indirectly (from length densities and diameters) using isotropic uniform random sampling

Electron microscopic stereological study of collagen fibrils in bovine articular cartilage: volume and surface densities are best obtained indirectly (from length densities and diameters) using isotropic uniform random sampling

Biology of collagen-proteoglycan interaction.

Amianthoid (Asbestoid) transformation: Electron microscopical studies on aging human costal cartilage

Contact Info

Product

Resources

About