Elasticity in extracellular matrix ‘shape modules’ of tendon, cartilage, etc. A sliding proteoglycan‐filament model

2003/11/27 by J. E. Scott · 26 citations
Materials Science · Biochemistry, Genetics and Molecular Biology · Medicine · #Collagen: Extraction and Characterization #Connective tissue disorders research #Tendon Structure and Treatment

paper · pdf · doi:10.1113/jphysiol.2003.050179

Abstract

Connective tissues (CTs), which define bodily shape, must respond quickly, robustly and reversibly to deformations caused by internal and external stresses. Fibrillar (elastin, collagen) elasticity under tension depends on molecular and supramolecular mechanisms. A second intra-/inter-molecular pair, involving proteoglycans (PGs), is proposed to cope with compressive stresses. PG interfibrillar bridges ('shape modules'), supramolecular structures ubiquitously distributed throughout CT extracellular matrices (ECMs), are examined for potential elastic properties. L-iduronate residues in shape module decoran PGs are suggested to be molecular springs, cycling through alternative conformations. On a larger scale, anionic glycosaminoglycan (AGAG) interfibrillar bridges in shape modules are postulated to take part in a sliding filament (dashpot-like) process, which converts local compressions into disseminated tensile strains. The elasticity of fibrils and AGAGs, manifest at molecular and larger-scale levels, provides a graduated and smooth response to stresses of varying degrees. NMR and rheo NMR, computer modelling, electron histochemical, biophysical and chemical morphological evidence for the proposals is reviewed.

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