scholarly journals Tendon collagen fibrils ‐ Continuity and mechanical properties

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Rene Brüggebusch Svensson ◽  
Andreas Herchenhan ◽  
Vuokko Kovanen ◽  
Klaus Qvortrup ◽  
S. Peter Magnusson
Author(s):  
Rene B. Svensson ◽  
Christian S. Eriksen ◽  
Peter H.T. Tran ◽  
Michael Kjaer ◽  
S. Peter Magnusson

Nanoscale ◽  
2021 ◽  
Author(s):  
Weijian Fang ◽  
Hang Ping ◽  
Wolfgang Wagermaier ◽  
Shenbao Jin ◽  
Shahrouz Amini ◽  
...  

Collagen fibrils present periodic structures, which provide space for intrafibrillar growth of oriented hydroxyapatite nanocrystals in bone and contribute to the good mechanical properties of bone. However, there are not...


2008 ◽  
Vol 94 (6) ◽  
pp. 2204-2211 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Carel F.C. Fitié ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  

1990 ◽  
Vol 38 (10) ◽  
pp. 1405-1411 ◽  
Author(s):  
G A Pringle ◽  
C M Dodd

Two monoclonal antibodies, 6D6 and 7B1, previously shown to recognize different epitopes on different regions of the protein core of decorin were used to localize the protein core in relation to the positively stained bands in the D period of bovine tendon collagen fibrils. Peroxidase-antiperoxidase staining revealed that the antigen is associated with the surface of all fibrils and suggested that the axial distance between antigens is D-periodic. Immunoferritin labeling with each antibody produced a distribution of ferritin particles that showed that both epitopes of the protein core are localized near the d and e bands in the D period. The data indicate that the decorin protein core binding site(s) on tendon collagen fibrils is/are located near these bands, axially, within the D period.


1987 ◽  
Vol 72 (3) ◽  
pp. 359-363 ◽  
Author(s):  
Pr J. E. Scott ◽  
Marion Haigh ◽  
Geok-Eng Neo ◽  
Sarah Gibson

1. Voluntary muscle activity in chick embryos was paralysed by administration in ovo of tubocurarine hydrochloride, administered in single or multiple doses, from day 9 to day 13 after fertilization. Control eggs were given saline instead of tubocurarine or were simply incubated without operative interference. Embryos were killed at 9, 13, 14, 16 and 19 days after fertilization. Flexor digitorum tendons were removed, fixed in glutaraldehyde, embedded in plastic, sectioned, and stained with phosphotungstic acid for electron microscopy. The diameters of the tendon collagen fibrils were measured, on electron micrographs, using a Magiscan Mk II programme. 2. Tendon collagen fibril expansion was not inhibited by tubocurarine treatment. It is concluded that the rapid increase of collagen fibril diameters, which coincides in the normal embryo with the first onset of use of the associated muscle, is not dependent on muscle activity. There remains a possibility that other ways of producing tension in the tendon could provide sufficient stimulus to fibril expansion.


1978 ◽  
Vol 33 (5-6) ◽  
pp. 346-358 ◽  
Author(s):  
H. Wesch ◽  
R. Jonak ◽  
H. Nemetschek-Gansler ◽  
H. Riedl ◽  
Th. Nemetschek

Abstract The content of trace elements in several organs of rats under the influence of D-penicillamine (D-PA) was investigated by the neutronactivation-analysis. It could be shown an diminution of Cu, and Co under D-PA-treatment, the content of Fe, Mn, Rb and Zn was not influenced. The investigat­ ed organs didn’t show any submicroscopic alterations under D-PA. On isolated collagen fibrils of tail tendon was seen a significantly diminuition of E-moduls. In accordance with Siegel the principal effect of D-PA is thought to block the synthesis of functional groups from Schiff-base crosslink precursors but not to inhibit lysyloxidase by loss of Cu-ions of connective tissue. The thermostability of D-PA influenced fibrils is changed in stretched state only and will be due to the lack of crosslink Schiff-bases; where as the shrinking point of not stretched fibrils shows only aging dependent changes.


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