PATHOMECHANICS OF SPRAINS AND STRAINS: CHANGES IN MOLECULAR STATE DUE TO COLLAGEN FIBRE OVEREXTENSION

Abstract

Sprains and strains result from collagen fibre overextension. This study investigated changes in the molecular state of collagen due to overextension damage, thereby gaining insight into tissue degeneration and cellular detection of damage. Overextension results in intermolecular and intrafibrillar sliding, detected with x-ray diffraction. Tendon rupture results in increased susceptibility to proteolytic enzymes. These observations and contemporary theory concerning collagen fibre stability lead to the hypothesis that sub-rupture overextension should result in reduced thermal stability of fibrous collagen.

Tendons were harvested from steer tails. Each provided a specimen for control and for overextension. Sub-rupture overextension at 1%/s strain rate was accomplished on a mechanical testing system, under the control of custom software, until the slope of the force-deformation curve was approximately zero (before complete failure). Two loading treatments were tested: one-cycle and five-cycles. Two specimen types were tested: native tendons ± NaBH4 crosslink stabilization. Tendons in each of the four groups (2x2) were paired by originating tail. Thermal stability was assessed in terms of denaturation temperature (Td) using hydrothermal isometric tension testing. Specimens were held at constant length and heated from ambient temperature to 90degC. Td was defined as the temperature where load suddenly increased due to molecular unraveling and attempted shrinkage.

Overextension of native specimens reduced the thermal stability of the collagen (p< 0.0001) and five-cycles had a still greater effect (p=0.03). Td of controls was 64.5±1.0degC (mean±SD). After one-cycle, Td dropped to 63.2±1.0degC and, after five-cycles, Td dropped to 61.8±2.0degC. For stabilised tendons, the effect of multiple cycles was lost (p=0.08) but overstretching decreased Td by ~2degC (p< 0.0001).

This study confirms that the molecular state of collagen is altered by overextension damage, reducing Td by up to 10% of the expected range (37–65degC) in our experiments. This is thought to occur due to intermolecular sliding that liberates specific domains on the molecules, lowering the activation energy for uncoiling. These domains may also be key targets in degeneration and cell-collagen signaling.