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Fibrous extracellular matrix of tendon is considered to be an inextensible anatomical structure consisting of type I collagen fibrils arranged in parallel bundles. Under polarized light microscopy the collagen fibre bundles appear crimped with alternating dark and light transverse bands. This study describes the ultrastructure of the collagen fibrils in crimps of both relaxed and in vivo stretched rat Achilles tendon. Under polarized light microscopy crimps of relaxed Achilles tendons appear as isosceles or scalene triangles of different size. Tendon crimps observed via SEM and TEM show the single collagen fibrils that suddenly change their direction containing knots. The fibrils appear partially squeezed in the knots, bent on the same plane like bayonets, or twisted and bent. Moreover some of them lose their D-period, revealing their microfibrillar component. These particular aspects of collagen fibrils inside each tendon crimp have been termed 'fibrillar crimps' and may fulfil the same functional role. When tendon is physiologically stretched in vivo the tendon crimps decrease in number (46.7%) ( P < 0.01) and appear more flattened with an increase in the crimp top angle (165 ° in stretched tendons vs. 148 ° in relaxed tendons, P < 0.005). Under SEM and TEM, the 'fibrillar crimps' are still present, never losing their structural identity in straightened collagen fibril bundles of stretched tendons even where tendon crimps are not detectable. These data suggest that the 'fibrillar crimp' may be the true structural component of the tendon crimp acting as a shock absorber during physiological stretching of Achilles tendon.

This work analyzes the effects of storage by fresh-freezing at -80 degrees C on the histological, structural and biomechanical properties of the human posterior tibial tendon (PTT), used for ACL reconstruction. Twenty-two PTTs were harvested from eleven donors. For each donor one tendon was frozen at -80 degrees C and thawed in physiological solution at 37 degrees C, and the other was tested without freezing (control). Transmission electron microscopy (TEM), differential scanning calorimetry (DSC) and biomechanical analysis were performed. We found the following mean changes in frozen-thawed tendons compared to controls: TEM showed an increase in the mean diameter of collagen fibrils and in fibril non-occupation mean ratio, while the mean number of fibrils decreased; DSC showed a decrease in mean denaturation temperature and denaturation enthalpy. Biomechanical analysis showed a decrease in ultimate load and ultimate stress, an increase in stiffness and a decrease in ultimate strain of tendons. In conclusion fresh-freezing brings about significant changes in the biomechanical and structural properties of the human PTT. A high variability exists in the biophysical properties of tendons among individuals and in the effects of storage on tendons. Therefore, when choosing an allograft tendon, particular care is needed to choose a biomechanically suitable graft.

We have used an InGaAs/InP single-photon avalanche diode detector module in conjunction with a time-of-flight depth imager operating at a wavelength of 1550 nm, to acquire centimeter resolution depth images of low signature objects at stand-off distances of up to one kilometer. The scenes of interest were scanned by the transceiver system using pulsed laser illumination with an average optical power of less than 600 µW and per-pixel acquisition times of between 0.5 ms and 20 ms. The fiber-pigtailed InGaAs/InP detector was Peltier-cooled and operated at a temperature of 230 K. This detector was used in electrically gated mode with a single-photon detection efficiency of about 26% at a dark count rate of 16 kilocounts per second. The system's overall instrumental temporal response was 144 ps full width at half maximum. Measurements made in daylight on a number of target types at ranges of 325 m, 910 m, and 4.5 km are presented, along with an analysis of the depth resolution achieved.