scholarly journals Collagen–proteoglycan interactions. Localization of proteoglycans in tendon by electron microscopy

1980 ◽  
Vol 187 (3) ◽  
pp. 887-891 ◽  
Author(s):  
J E Scott

Proteoglycan in foetal- and adult-rat tail tendon and adult-rabbit achilles tendon was stained for electron microscopy with a cationic phthalocyanin-like dye, based on cinchomeronic acid, in a ‘critical electrolyte concentration’ method [Scott (1973) Biochem. Soc. Trans. 1, 787-806). Provided that the tissue was fixed with glutaraldehyde or formaldehyde, regular orthogonal perifibrillar arrays of filamentous material (proteoglycan) were observed, but no intra-fibrillar proteoglycan was seen. Specific proteoglycan-collagen interactions are inferred, and a model is proposed. Without fixation, the filamentous arrays disaggregated in the MgCl2 solutions (0.3 M) used during staining. End-to-end proteoglycan aggregation is implied. Tendon and cartilage are compared. Problems of electron-histochemical localization of extended space-filling polyanions by the use of cationic electron-dense precipitants are discussed, particularly polyanion-domain collapse, specificity of staining and fixation. A two-stage staining procedure that markedly enhances contrast is described, based on the multivalent nature of the dye, and the consequent anion-exchange properties of the dye-polyanion complex.

1981 ◽  
Vol 197 (1) ◽  
pp. 213-216 ◽  
Author(s):  
J E Scott ◽  
C R Orford

Rat tail tendon was stained with a cationic phthalocyanin dye, Cupromeronic Blue, in a ‘critical-electrolyte-concentration’ method [Scott (1980) Biochem. J. 187, 887-891] specifically to demonstrate proteoglycan by electron microscopy. Hyaluronidase digestion in the presence of proteinase inhibitors corroborated the results. Collagen was stained with uranyl acetate and/or phosphotungstic acid to demonstrate the banding pattern a-e in the D period. Proteoglycan was distributed about the collagen fibrils in an orthogonal array, the transverse elements of which were located almost exclusively at the d band, in the gap zone. The proteoglycan may inhibit (1) fibril radial growth by accretion of collagen molecules or fibril fusion, through interference with cross-linking, and (2) calcification by occupying the holes in the gap region later to be filled with hydroxyapatite.


1977 ◽  
Vol 195 (1120) ◽  
pp. 355-364 ◽  

Electron microscopy of positively stained elastoidin reveals a fine struc­ture apparently identical with that of the collagen of rat tail tendon. The negatively stained pattern is clearly related to that of the collagen but differs from it; it resembles that of artificially cross-linked collagens more. X-ray diffraction fails to find evidence of any long range lateral order in the arrangement of molecules within the elastoidin. The interest­ing splitting of the meridional pattern upon drying is re-reported and its possible origins discussed. Some discussion of fibrillogenesis is presented based on a comparison of rat tail tendon collagen and elastoidin.


1992 ◽  
Vol 23 (3) ◽  
pp. 260-261 ◽  
Author(s):  
C. Dell'Orbo ◽  
D. Quacci ◽  
M. Raspanti ◽  
A. Riva

1960 ◽  
Vol 235 (4) ◽  
pp. 989-994
Author(s):  
Alexander Kessler ◽  
Hyman Rosen ◽  
Stanley M. Levenson

1972 ◽  
Vol 11 (1) ◽  
pp. 249-260
Author(s):  
J. ALWEN ◽  
JENNIFER J. GALLHAI-ATCHARD

A method for preparing suspensions of adult rat hepatocytes suitable for maintenance in vitro is described. Cultures were established from the cell suspensions by the squash technique. Cells were examined by light and electron microscopy; histochemically for glycogen, bile, lipid and glucose-6-phosphatase; and by autoradiography for DNA, RNA and protein synthesis. Hepatocytes could be maintained in vitro for at least 3 days and began to aggregate after 1 day. Uridine and leucine were incorporated, but not thymidine. Cultures consisted mainly of hepatocytes, though reticulo-endothelial cells were sometimes present.


2002 ◽  
Vol 7 (2) ◽  
pp. 205 ◽  
Author(s):  
Patrick Stoller ◽  
Beop-Min Kim ◽  
Alexander M. Rubenchik ◽  
Karen M. Reiser ◽  
Luiz B. Da Silva

2001 ◽  
Vol 159 (2) ◽  
pp. 683-691 ◽  
Author(s):  
Rumi Maruyama ◽  
Genzou Takemura ◽  
Takuma Aoyama ◽  
Kenji Hayakawa ◽  
Masahiko Koda ◽  
...  

Author(s):  
Gerhard A. Holzapfel ◽  
Ray W. Ogden

We propose a mechanical model to account for progressive damage in collagen fibres within fibrous soft tissues. The model has a similar basis to the pseudoelastic model that describes the Mullins effect in rubber but it also accounts for the effect of cross-links between collagen fibres. We show that the model is able to capture experimental data obtained from rat tail tendon fibres, and the combined effect of damage and collagen cross-links is illustrated for a simple shear test. The proposed three-dimensional framework allows a straightforward implementation in finite-element codes, which are needed to analyse more complex boundary-value problems for soft tissues under supra-physiological loading or tissues weakened by disease.


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