Background and purpose

It is controversial whether the transverse acetabular ligament (TAL) is a reliable guide for determining the cup orientation during total hip arthroplasty (THA). We investigated the variations in TAL anatomy and the TAL-guided cup orientation.

Methods

80 hips with osteoarthritis secondary to hip dysplasia (OA) and 80 hips with osteonecrosis of the femoral head (ON) were examined. We compared the anatomical anteversion of TAL and the TAL-guided cup orientation in relation to both disease and gender using 3D reconstruction of computed tomography (CT) images.

Results

Mean TAL anteversion was 11° (SD 10, range –12 to 35). The OA group (least-square mean 16°, 95% confidence interval (CI): 14–18) had larger anteversion than the ON group (least-square mean 6.2°, CI: 3.8 – 7.5). Females (least-square mean 20°, CI: 17–23) had larger anteversion than males (least-square mean 7.0°, CI: 4.6–9.3) in the OA group, while there were no differences between the sexes in the ON group. When TAL was used for anteversion guidance with the radiographic cup inclination fixed at 40°, 39% of OA hips and 9% of ON hips had more than 10° variance from the target anteversion, which was 15°.

Interpretation

In ON hips, TAL is a good guide for determining cup orientation during THA, although it is not a reliable guide in hips with OA secondary to dysplasia. This is because TAL orientation has large individual variation and is influenced by disease and gender.

Tg(PG14) mice express a prion protein (PrP) with a nine-octapeptide insertion associated with a human familial prion disease. These animals spontaneously develop a fatal neurodegenerative disorder characterized by ataxia, neuronal apoptosis, and accumulation in the brain of an aggregated and weakly protease-resistant form of mutant PrP (designated PG14spon). Brain homogenates from Tg(PG14) mice fail to transmit disease after intracerebral inoculation into recipient mice, indicating that PG14spon, although pathogenic, is distinct from PrPSc, the infectious form of PrP. In contrast, inoculation of Tg(PG14) mice with exogenous prions of the RML strain induces accumulation of PG14RML, a PrPSc form of the mutant protein that is infectious and highly protease resistant. Like PrPSc, both PG14spon and PG14RML display conformationally masked epitopes in the central and octapeptide repeat regions. However, these two forms differ profoundly in their oligomeric states, with PG14RML aggregates being much larger and more resistant to dissociation. Our analysis provides new molecular insight into an emerging puzzle in prion biology, the discrepancy between the infectious and neurotoxic properties of PrP.