Molecular electromechanics of cartilaginous tissues and polyelectrolyte gels

Berkenblit, Scott I.; Quinn, Thomas M.; Grodzinsky, Alan J.

doi:10.1016/0304-3886(95)98192-m

Cited by 9 publications

(5 citation statements)

References 33 publications

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“…Likewise, fixed and free ions, particularly the fixed negative charges of proteoglycans, as well as glycosaminoglycans and proteins may also participate in redox reactions. Disruption to the internal stability of this liquid environment in cartilage that constitutes 70 to 80% of its wet weight may cause many mechanical changes [15]. In particular, such reactions may produce stress relaxation in the tissue, facilitating shape change and alteration of cartilage mechanical properties [9].…”

Section: Discussionmentioning

confidence: 99%

“…Altered through redox reactions as well, pH and ion concentrations change the fixed charge distribution which profoundly modifies the mechanical properties of cartilage tissue [13,[16][17][18]. Individually, pH determines the net charge of collagen, normally neutral at physiological pH, while ionic concentration also impacts the osmotic pressure of cartilage, which in turn affects tensile stress in the tissue's collagen network [15,17,18]. While pH changes may induce dramatic mechanical changes in cartilage, such alterations are often reversible [19,20].…”

Section: Discussionmentioning

confidence: 99%

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Changes in the Tangent Modulus of Rabbit Septal and Auricular Cartilage Following Electromechanical Reshaping

Lim

Protsenko

Wong

2011

Journal of Biomechanical Engineering

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Transforming decades' old methodology, electromechanical reshaping (EMR) may someday replace traditionally destructive surgical techniques with a less invasive means of cartilage reshaping for reconstructive and esthetic facial surgery. Electromechanical reshaping is essentially accomplished through the application of voltage to a mechanically deformed cartilage specimen. While the capacity of the method for effective reshaping has been consistently shown, its associated effects on cartilage mechanical properties are not fully comprehended. To begin to explore the mechanical effect of EMR on cartilage, the tangent moduli of EMR-treated rabbit septal and auricular cartilage were calculated and compared to matched control values. Between the two main EMR parameters, voltage and application time, the former was varied from 2-8 V and the latter held constant at 2 min for septal cartilage, 3 min for auricular cartilage. Flat platinum electrodes were used to apply voltage, maintaining the flatness of the specimens for more precise mechanical testing through a uniaxial tension test of constant strain rate 0.01 mm/s. Above 2 V, both septal and auricular cartilage demonstrated a slight reduction in stiffness, quantified by the tangent modulus. A thermal effect was observed above 5 V, a newly identified EMR application threshold to avoid the dangers associated with thermoforming cartilage. Optimizing EMR application parameters and understanding various side effects bridge the gap between EMR laboratory research and clinical use, and the knowledge acquired through this mechanical study may be one additional support for that bridge.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Changes in the Tangent Modulus of Rabbit Septal and Auricular Cartilage Following Electromechanical Reshaping

Lim

Protsenko

Wong

2011

Journal of Biomechanical Engineering

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“…At the macroscopic scale, the organization of collagen fibrils varies drastically from one tissue to another to comply with their physiological functions. In this article, we study the collagenous structure of cartilage that is formed at the nanoscale of a hydrated aggrecan gel reinforced by a three-dimensional collagen type II meshwork (5). At the macroscopic level, the collagen fibrils are arranged in closely linked leaves that are perpendicular to the surface deep in the cartilage and rapidly curve to become parallel to the surface in the superficial layers (6).…”

Section: Introductionmentioning

confidence: 99%

The Impact of Collagen Fibril Polarity on Second Harmonic Generation Microscopy

Couture

Bancelin

Kolk

et al. 2015

Biophysical Journal

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In this work, we report the implementation of interferometric second harmonic generation (SHG) microscopy with femtosecond pulses. As a proof of concept, we imaged the phase distribution of SHG signal from the complex collagen architecture of juvenile equine growth cartilage. The results are analyzed in respect to numerical simulations to extract the relative orientation of collagen fibrils within the tissue. Our results reveal large domains of constant phase together with regions of quasi-random phase, which are correlated to respectively high- and low-intensity regions in the standard SHG images. A comparison with polarization-resolved SHG highlights the crucial role of relative fibril polarity in determining the SHG signal intensity. Indeed, it appears that even a well-organized noncentrosymmetric structure emits low SHG signal intensity if it has no predominant local polarity. This work illustrates how the complex architecture of noncentrosymmetric scatterers at the nanoscale governs the coherent building of SHG signal within the focal volume and is a key advance toward a complete understanding of the structural origin of SHG signals from tissues.

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“…C: Pyridinium crosslinks interconnect single molecules of collagen type II, typically arranged as a triple helix [Fig. 1A adapted fromBerkenblit et al, 1995].…”

mentioning

confidence: 99%

Collagen in tissue-engineered cartilage: Types, structure, and crosslinks

et al. 1998

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The function of articular cartilage as a weight-bearing tissue depends on the specific arrangement of collagen types II and IX into a three-dimensional organized collagen network that can balance the swelling pressure of the proteoglycan/water gel. To determine whether cartilage engineered in vitro contains a functional collagen network, chondrocyte-polymer constructs were cultured for up to 6 weeks and analyzed with respect to the composition and ultrastructure of collagen by using biochemical and immunochemical methods and scanning electron microscopy. Total collagen content and the concentration of pyridinium crosslinks were significantly (57% and 70%, respectively) lower in tissue-engineered cartilage that in bovine calf articular cartilage. However, the fractions of collagen types II, IX, and X and the collagen network organization, density, and fibril diameter in engineered cartilage were not significantly different from those in natural articular cartilage. The implications of these findings for the field of tissue engineering are that differentiated chondrocytes are capable of forming a complex structure of collagen matrix in vitro, producing a tissue similar to natural articular cartilage on an ultrastructural scale.

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Molecular electromechanics of cartilaginous tissues and polyelectrolyte gels

Cited by 9 publications

References 33 publications

Changes in the Tangent Modulus of Rabbit Septal and Auricular Cartilage Following Electromechanical Reshaping

Changes in the Tangent Modulus of Rabbit Septal and Auricular Cartilage Following Electromechanical Reshaping

The Impact of Collagen Fibril Polarity on Second Harmonic Generation Microscopy

Collagen in tissue-engineered cartilage: Types, structure, and crosslinks

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