Hydration Effects on Tensile Properties of the Corneal Stroma

2013 ◽  
Author(s):  
Abdolrasol Rahimi ◽  
Hamed Hatami-Marbini
Keyword(s):  
Tensile Properties ◽  
Dermatan Sulfate ◽  
Lattice Structure ◽  
Corneal Thickness ◽  
Corneal Stroma ◽  
Swelling Pressure ◽  
Keratan Sulfate ◽  
Empty Space ◽  
Collagen Fibrils ◽  
Healthy Human

The mechanical behavior of the cornea is mainly governed by the microstructure and composition of the stroma. The stroma is a highly ordered extracellular matrix and constitutes about 90% of the corneal thickness. From the mechanics point of view, the corneal stroma can be considered as a polyelectrolyte gel which is composed of collagen fibrils embedded in an aqueous matrix. The collagen fibrils compose about 70% of cornea’s dry mass and are arranged in a regular lattice structure [2]. Previous studies have shown that while the collagen fibrils are primarily located parallel to the surface, they are not distributed uniformly in all directions and their preferred orientation is not same in different species. For example, collagen fibrils are almost equally distributed in the nasal-temporal and inferior-superior directions in healthy human corneas [4] and they are mainly aligned in the inferior-superior direction in bovine corneas[2]. The differences in the orientations of the collagen fibrils have seen to have important implications on the mechanical properties of the cornea. In addition to this observation, the relative distance between the collagen fibrils is expected to play a role in defining the mechanics of the tissue. It is well-documented that the proteoglycans bind collagen fibrils at regular sites and control their relative position. The main proteoglycan in the corneal stroma is decorin. Decorin is the simplest small leucine-rich proteoglycan with a single glycosaminoglycan side chain. Chondroitin sulfate, dermatan sulfate, and keratan sulfate are among the prevalent glycosaminoglycans found in the cornea. Under physiological conditions, these linear carbohydrate polymers are ionized and carry negative charges. Therefore, a hydrated gel is formed in the empty space between collagen fibrils by attracting water. It is known that the interaction of these negatively charged glycosaminoglycans with themselves and with the free ions contribute to the corneal swelling pressure and subsequently to its compressive stiffness. Nevertheless, their possible influence on the corneal tensile properties is yet to be determined. In this work, we experimentally characterized the tensile properties of the bovine corneal stroma in different bathing solutions. Furthermore, a quasi-linear viscoelastic (QLV) model was used to examine the effect of bathing fluids and corneal hydration on mechanical parameter of the cornea.

On Unconfined Compression Response of the Porcine Corneal Stroma

2013 ◽  
Author(s):  
Ebitimi Etebu ◽  
Hamed Hatami-Marbini
Keyword(s):  
Mechanical Properties ◽  
Lattice Structure ◽  
Research Work ◽  
Corneal Stroma ◽  
Swelling Pressure ◽  
Transversely Isotropic ◽  
Collagen Fibrils ◽  
Mechanical Parameters ◽  
Unconfined Compression ◽  
Biphasic Model

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.

Characterizing Swelling Pressure and Hydration Relationship for Porcine Corneal Stroma

2013 ◽  
Author(s):  
Hamed Hatami-Marbini ◽  
Ebitimi Etebu ◽  
Abdolrasol Rahimi
Keyword(s):  
Extracellular Matrix ◽  
Core Protein ◽  
Lattice Structure ◽  
Incident Light ◽  
Corneal Stroma ◽  
Swelling Pressure ◽  
Collagen Fibrils ◽  
Bathing Solution ◽  
Swelling Properties ◽  
Knock Out

The mechanical properties and structure of connective tissues such as the cornea and articular cartilage are derived from the functions and properties of their extracellular matrix, which is a polyelectrolyte gel composed of collagenous fibers embedded in an aqueous matrix. The collagen fibrils in the extracellular matrix of the corneal stroma are arranged in a regular lattice structure, which is necessary for corneal transparency and transmitting the incident light to the back of the eye. This regular pseudo hexagonal arrangement is attributed to the interaction of collagen fibrils with the proteoglycans; these regularities are lost in proteoglycan knock-out mice [1]. Proteoglycans are heavily glycosylated glycoproteins consisting of a core protein to which glycosaminoglycan chains are covalently attached. The main proteoglycan in the corneal stroma is decorin. Decorin is the simplest small leucine-rich proteoglycan with only a single glycosaminoglycan side chain. It has a horse shape core protein and binds collagen fibrils at regular sites. Under normal physiological conditions, these linear carbohydrate polymers are ionized and carry negative charges due to the presence of negatively charged carboxylate and sulfate groups. The presence of these fixed charges creates an imbalance of charge density within the stroma and its surrounding aqueous domain. Therefore, the tissue has a tendency to swell when immersed in a bathing solution. In order to create mathematical models for the corneal mechanics, a proper experimental characterization of the swelling properties of the tissue is necessary.

Influence of Ionic Concentration on Swelling Behavior and Shear Properties of the Bovine Cornea

2012 ◽  
Author(s):  
Hamed Hatami-Marbini ◽  
Ebitimi Etebu
Keyword(s):  
Extracellular Matrix ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Incident Light ◽  
Corneal Stroma ◽  
Ionic Concentration ◽  
Collagen Fibers ◽  
Collagen Fibrils ◽  
Knock Out ◽  
Free Ions

The mechanical properties and structure of connective tissues such as the cornea and the cartilage are derived from the functions and properties of their extracellular matrix, a polyelectrolyte gel composed of collagenous fibers embedded in an aqueous matrix. The collagen fibers in the extracellular matrix of the corneal stroma are arranged in regular lattice structures, which is necessary for corneal transparency and transmitting the incident light to the back of the eye. This regular pseudo hexagonal arrangement is attributed to the interaction of collagen fibers with the proteoglycans as these regularities are lost in knock-out mice [i]. Proteoglycans (PGs) are heavily glycosylated glycoproteins. They consist of a core protein to which is glycosaminoglycan chains are covalently attached. The main PG in the corneal stroma is the proteoglycan decorin. Decorin is the simplest small leucine-rich PG and only has a single glycosaminoglycan side chain. It has a horse shape core protein and binds collagen fibrils at regular sites. Chondroitin sulfate (CS), dermatan sulfate (DS), keratan sulfate (KS) are among the prevalent glycosaminoglycans found in the cornea. Under physiological conditions, these linear carbohydrate polymers are ionized and carry negative charges due to the presence of negatively charged carboxylate and sulfate groups. Therefore, a hydrated gel is formed in the empty space between collagen fibrils by attracting water. The interaction of negatively charged glycosaminoglycans with themselves and their interaction with the free ions contribute to the corneal swelling pressure and subsequently to its compressive stiffness. From structural view point, the corneal stroma is a composite polyelectrolyte system in which the observed regular spacings of the collagens are suggested to exist because of the structural interaction of collagens, negatively charged glycosaminoglycans, and the free ions in the interfibrillar space.

Material Properties of Porcine Corneal Stroma in Unconfined Compression

2013 ◽  
Author(s):  
Hamed Hatami-Marbini ◽  
Ebitimi Etebu
Keyword(s):  
Extracellular Matrix ◽  
Corneal Stroma ◽  
Swelling Pressure ◽  
Empty Space ◽  
Collagen Fibers ◽  
Necessary Condition ◽  
Internal Stresses ◽  
Connective Tissues ◽  
Polyelectrolyte Gel ◽  
Hexagonal Arrangement

The tensile properties of the cornea have been extensively studied while there are fewer studies on its compressive stiffness. The mechanical properties and structure of the cornea like many other connective tissues are derived from the function and properties of their extracellular matrix. The corneal extracellular matrix, stroma, is a polyelectrolyte gel composed of collagenous fibers embedded in an aqueous matrix. The cornea has two different functions: optical and mechanical. It is the main refractive component of the visual system and it is an effective barrier resisting the deformation caused by external and internal stresses. A necessary condition for corneal optical properties and transparency is the maintenance of a pseudo hexagonal arrangement of the collagen fibers inside the extracellular matrix. This regular arrangement is attributed to the interaction of collagen fibers with the proteoglycans. Under physiological conditions, the proteoglycans are ionized and form a hydrated gel in the empty space between the collagen fibrils by attracting the water and solutes. The interaction of the negatively fixed charges of the proteoglycans with themselves and with the free ions inside the interstitial fluid contributes to the corneal swelling pressure and subsequently to its compressive properties.

scholarly journals Extracellular Matrix Deposition and Remodeling after Corneal Alkali Burn in Mice

2021 ◽  
Vol 22 (11) ◽  
pp. 5708
Author(s):  
Kazadi N. Mutoji ◽  
Mingxia Sun ◽  
Garrett Elliott ◽  
Isabel Y. Moreno ◽  
Clare Hughes ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Dermatan Sulfate ◽  
Temporal Distribution ◽  
Keratan Sulfate ◽  
Collagen Fibrils ◽  
Type I ◽  
Chemical Injury ◽  
Matrix Deposition ◽  
Alkali Burn ◽  
Extracellular Matrix Deposition

Corneal transparency relies on the precise arrangement and orientation of collagen fibrils, made of mostly Type I and V collagen fibrils and proteoglycans (PGs). PGs are essential for correct collagen fibrillogenesis and maintaining corneal homeostasis. We investigated the spatial and temporal distribution of glycosaminoglycans (GAGs) and PGs after a chemical injury. The chemical composition of chondroitin sulfate (CS)/dermatan sulfate (DS) and heparan sulfate (HS) were characterized in mouse corneas 5 and 14 days after alkali burn (AB), and compared to uninjured corneas. The expression profile and corneal distribution of CS/DSPGs and keratan sulfate (KS) PGs were also analyzed. We found a significant overall increase in CS after AB, with an increase in sulfated forms of CS and a decrease in lesser sulfated forms of CS. Expression of the CSPGs biglycan and versican was increased after AB, while decorin expression was decreased. We also found an increase in KS expression 14 days after AB, with an increase in lumican and mimecan expression, and a decrease in keratocan expression. No significant changes in HS composition were noted after AB. Taken together, our study reveals significant changes in the composition of the extracellular matrix following a corneal chemical injury.

A Triphasic Analysis of Corneal Swelling and Hydration Control

1998 ◽  
Vol 120 (3) ◽  
pp. 370-381 ◽  
Author(s):  
M. R. Bryant ◽  
P. J. McDonnell
Keyword(s):  
Ion Transport ◽  
Corneal Endothelium ◽  
Corneal Thickness ◽  
Corneal Stroma ◽  
Swelling Pressure ◽  
Confined Compression ◽  
Cylindrical Coordinates ◽  
Flux Boundary Condition ◽  
Corneal Hydration ◽  
Active Ion Transport

Physiological studies strongly support the view that hydration control in the cornea is dependent on active ion transport at the corneal endothelium. However, the mechanism by which endothelial ion transport regulates corneal thickness has not been elaborated in detail. In this study, the corneal stroma is modeled as a triphasic material under steady-state conditions. An ion flux boundary condition is developed to represent active transport at the endothelium. The equations are solved in cylindrical coordinates for confined compression and in spherical coordinates to represent an intact cornea. The model provides a mechanism by which active ion transport at the endothelium regulates corneal hydration and provides a basis for explaining the origin of the “imbibition pressure” and stromal “swelling pressure.” The model encapsulates the Donnan view of corneal swelling as well as the “pump-leak hypothesis.”

scholarly journals A cornealis sebgyógyulás és az extracelluláris mátrix

2016 ◽  
Vol 157 (25) ◽  
pp. 995-999
Author(s):  
Gréta Varkoly ◽  
János Bencze ◽  
Tibor Hortobágyi ◽  
László Módis
Keyword(s):  
Extracellular Matrix ◽  
Growth Factors ◽  
Dermatan Sulfate ◽  
Keratan Sulfate ◽  
Scar Tissue ◽  
Collagen Fibrils ◽  
Proteoglycan Synthesis ◽  
Abnormal Structure ◽  
Fibrillar Collagens ◽  
Corneal Scar

The cornea is the first refractive element of the eye. The transparency of the cornea results from the regularly arranged collagen fibrils, forming lamellar structure and the leucin rich proteoglycans, which make interactions between the fibrils. The adult cornea consists mainly of fibril-forming collagens. The cornea has less amount of fibril associated and non-fibrillar collagens. The main proteoglycans of the cornea are keratan-sulfate proteoglycans and it also contains dermatan-sulfate proteoglycans. Disorders of the proteoglycan synthesis lead to the disruption of the unique pattern and result in thicker collagen fibrils. The abnormal structure of the extracellular matrix can generate corneal disorders and the loss of corneal transparency. Furthermore, proteoglycans and collagens have an important role in wound healing. In injury the keratocytes produce higher amounts of collagens and proteoglycans mediated by growth factors. Depending on the ratio of the cells and growth factors the extracellular matrix returns to normal or corneal scar tissue develops. Orv. Hetil., 2016, 157(25), 995–999.

beta-D xyloside alters dermatan sulfate proteoglycan synthesis and the organization of the developing avian corneal stroma

Development ◽  
1992 ◽  
Vol 115 (2) ◽  
pp. 383-393
Author(s):  
R.A. Hahn ◽  
D.E. Birk
Keyword(s):  
Collagen Fibril ◽  
Dermatan Sulfate ◽  
Corneal Stroma ◽  
Small Diameter ◽  
Keratan Sulfate ◽  
Proteoglycan Synthesis ◽  
Sulfate Proteoglycan ◽  
In Ovo ◽  
Dermatan Sulfate Proteoglycan ◽  
Fibril Diameter

Corneal transparency is dependent upon the development of an organized extracellular matrix containing small diameter collagen fibrils with regular spacing, organized as orthogonal lamellae. Proteoglycan-collagen interactions have been implicated in the regulation of collagen fibrillogenesis and matrix assembly. To determine the role of dermatan sulfate proteoglycan in the development and organization of the secondary corneal stroma, its synthesis was disrupted using beta-D xyloside. The secondary corneal stroma contains two different proteoglycans, dermatan sulfate and keratan sulfate proteoglycan. beta-D xyloside interferes with xylose-mediated O-linked proteoglycan synthesis, and thus disrupts dermatan sulfate proteoglycan synthesis. Corneal keratan sulfate proteoglycan, a mannose-mediated N-linked proteoglycan, should not be altered. Biochemical analysis of corneas treated both in vitro and in ovo revealed a reduced synthesis of normally glycosylated dermatan sulfate proteoglycans and an increased synthesis of free xyloside-dermatan sulfate glycosaminoglycans. Keratan sulfate proteoglycan synthesis was unaltered in both cases. Corneal stromas were studied using histochemistry and electron microscopy after in ovo treatment with beta-D xyloside. The observed biochemical alterations in dermatan sulfate proteoglycans translated into disruptions in the organization of beta-D xyloside-treated stromas. There was a reduction in the histochemical staining of proteoglycans, but no alteration in collagen fibril diameter. In addition, focal alterations in collagen fibril packing, and a disruption of lamellar organization were observed in beta-D xyloside-treated corneas. These data suggest that dermatan sulfate proteoglycans are not involved in the regulation of corneal collagen fibril diameter, but are important in the fibril-fibril spacing as well as in lamellar organization, and cohesiveness.

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