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Published on: July 8, 2021
Structure, composition and anisotropic swelling of the bovine acetabular labrum
Stephanie Huber1, Matthias X T Santschi1, Jemima Schadow1
1ETH Zurich, Institute for Biomechanics, Zurich, Switzerland.
Abstract:
The fibro-cartilaginous labrum surrounds the acetabular rim and is important for hip joint stability and sealing. Sealing may be enhanced by swelling pressure within the normal labrum. Swelling of the degenerated or torn labrum might occur and potentially contribute to the development of osteoarthritis, through altered load transmission. This study aimed to characterize the three-dimensional swelling behaviour, the collagen fiber orientation and spatial proteoglycan distribution of the bovine acetabular labrum. Specimens were harvested from bovine donors (192-652 days, male, n = 6 donors). Structure was analyzed by scanning electron microscopy, histology, and dimethylmethylene blue assay. Specimen dimensions were measured before and after incubation in phosphate buffered saline to assess the swelling. Results showed that the articulating surface is composed of a collagen mesh network. Collagen fiber bundles showed a low degree of alignment close to the surface and were circumferentially aligned in the deep tissue. Proteoglycans were identified clustered between the collagen bundles. Glycosaminoglycan content was 10 x lower than that of cartilage (23.1 ± 6.4 compared to 299.5 ± 19.1 μg/mg dry weight) with minor regional differences. Specimens swelled significantly more in the orthogonal direction (swelling ratio 124.7 ± 10.2%) compared to the swelling parallel to the articulating surface (108.8 ± 6.1% and 102.8 ± 4.1%). In the deep tissue, swelling was also restricted in the main collagen fiber bundle direction (circumferentially), with a swelling ratio of 109.5 ± 4.0% in the main fiber bundle direction compared to 126.8 ± 7.3 % and 122.3 ± 5.8% radially. The findings demonstrate that the labrum shows anisotropic swelling properties, which reflect the anisotropy in the tissue structure and inter-fiber localisation of proteoglycans.
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