Organization of Collagen Fibrils in the Corneal Stroma in Relation to Mechanical Properties and Surgical Practice

1999 ◽  
Vol 15 (6) ◽  
pp. 695-699 ◽  
Author(s):  
Keith M Meek ◽  
Richard H Newton
Author(s):  
Ebitimi Etebu ◽  
Hamed Hatami-Marbini

The corneal stroma constitutes about 90% of the corneal total thickness and is mainly responsible for its mechanical properties. The stroma is a highly ordered structure composed of mostly parallel to the surface stacks of 2 μm thick collagenous lamellae. The collagen fibrils have an almost uniform diameter and are arranged in a pseudohexagonal lattice structure. Under normal physiological conditions, the collagen fibrils are responsible for carrying the membrane tensile stresses caused by the intraocular pressure. It is believed that the interaction between the collagen fibrils and hydrophilic negatively charged proteoglycans are responsible for the stromal architecture as well as the compressive properties of the tissue. Up to date uniaxial strip testing method and biaxial pressure inflation experiments have widely been used to determine the mechanical parameters of the cornea. These experimental measurements often provide the necessary information for characterizing the tissue behavior in tension [1] [2, 3]. Nevertheless, the mechanical parameters of the cornea in compression have received less attention in the literature. Most of the previous studies are focused on describing the swelling pressure and hydration relations [4]. In this research work, we used unconfined compression experiments along with a biphasic model to measure the corneal parameters in compression. This method has been extensively used to explore the mechanical properties of similar hydrated tissues such as the articular cartilage [5]. Due to specific microstructure of the cornea, a transversely isotropic model was used to curve-fit the experimental data and to derive the in-plane modulus of the cornea. The predicted in-plane modulus was compared to the values reported in literature.


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...


2021 ◽  
pp. 2100972
Author(s):  
Nello Formisano ◽  
Cas Putten ◽  
Rhiannon Grant ◽  
Gozde Sahin ◽  
Roman K. Truckenmüller ◽  
...  

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 ◽  
...  

2004 ◽  
Vol 78 (3) ◽  
pp. 493-501 ◽  
Author(s):  
Linda J. Müller ◽  
Elizabeth Pels ◽  
Lucas R.H.M. Schurmans ◽  
Gijs F.J.M. Vrensen

1985 ◽  
Vol 5 (9) ◽  
pp. 765-774 ◽  
Author(s):  
J. E. Scott ◽  
M. Haigh

l. Proteoglycans (PGs) in rabbit corneal stroma and mouse sclera have been stained for electron microscopy with Cupromeronic blue in a critical electrolyte concentration (CEC) mode, with and without prior digestion of the tissue by keratanase or chondroitinase ABC to remove the keratan sulphate (KS) or chondroitin-dermatan sulphates (CS or DS) respectively.2. Two classes of PGs, located orthogonally to the corneal collagen fibrils at either the ‘step’ (band ‘a’ or ‘c’) or gap zone (band ‘d’ or ‘e’) are shown to be KS-PGs or DS-PGs respectively. Four separate and specific PG binding sites on Type I collagen fibrils have thus been identified.3. Rabbit corneal KS and DS PGs each contain two kinds of PG (Gregory JD, Coster L & Damle SP (1982) J. Biol. Chem.257, 6965–6970). We propose that each ‘small’ protein-rich PG is associated with a specific binding site on the collagen fibril.


2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Alfredo Vega-Estrada ◽  
Joaquin Silvestre-Albero ◽  
Alejandra E. Rodriguez ◽  
Francisco Rodriguez-Reinoso ◽  
Jose A. Gomez-Tejedor ◽  
...  

Corneal ectatic disorders are characterized by a progressive weakening of the tissue due to biomechanical alterations of the corneal collagen fibers. Carbon nanostructures, mainly carbon nanotubes (CNTs) and graphene, are nanomaterials that offer extraordinary mechanical properties and are used to increase the rigidity of different materials and biomolecules such as collagen fibers. We conducted an experimental investigation where New Zealand rabbits were treated with a composition of CNTs suspended in balanced saline solution which was applied in the corneal tissue. Biocompatibility of the composition was assessed by means of histopathology analysis and mechanical properties by stress-strain measurements. Histopathology samples stained with blue Alcian showed that there were no fibrous scaring and no alterations in the mucopolysaccharides of the stroma. It also showed that there were no signs of active inflammation. These were confirmed when Masson trichrome staining was performed. Biomechanical evaluation assessed by means of tensile test showed that there is a trend to obtain higher levels of rigidity in those corneas implanted with CNTs, although these changes are not statistically significant (p>0.05). Implanting CNTs is biocompatible and safe procedure for the corneal stroma which can lead to an increase in the rigidity of the collagen fibers.


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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