Influence of posterior lateral femoral condyle geometry on patellar dislocation.

INTRODUCTION: Patellar instability is a condition with multifactorial aetiology, potentially involving soft tissue characteristics, the bony anatomy of the patella, femur and tibia, and alignment of the lower limb. The shape of the distal femur and patellofemoral joint has been frequently studied using plain orthogonal and skyline radiographs. We investigated a possible contribution of hypoplasia of the lateral femoral condyle in the axial plane to patellar instability. METHODS: The geometry of the distal femur and alignment of the lower limb on plain radiographs and MRI scans in 25 young adult patients with patellar instability was measured, and compared to a control group of 75 age-matched patients. Measurements were validated by intra-observer and inter-observer reliability studies, and multivariate analysis was used to compare the groups. Cases with and without high Beighton score or knee hyperextension were also compared. RESULTS: The anatomical posterior condylar angle, anterior condylar angle and sulcus angle on axial MRI scans showed insignificant differences between groups. The Blackburne-Peel ratio, anatomical femoro-tibial angle and femoral joint angle showed significant differences between groups, but not the tibial plateau angle. There was a significant correlation between posterior condylar angle and valgus knee alignment. In cases with joint hypermobility, femoral joint angle was significantly increased and posterior condylar angle was significantly decreased. CONCLUSIONS: Multiplanar hypoplasia of the lateral femoral condyle resulting in a valgus knee is a risk factor for patellar instability in young patients without osteoarthritis or joint hypermobility. Isolated posterior lateral condyle hypoplasia appears to be unrelated to patellar instability.

Structural basis for engagement by complement factor H of C3b on a self surface.

Complement factor H (FH) attenuates C3b molecules tethered by their thioester domains to self surfaces and thereby protects host tissues. Factor H is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d) corresponding to the thioester domain. We used NMR and X-ray crystallography to study the C3d-FH19-20 complex in atomic detail and identify glycosaminoglycan-binding residues in factor H module 20 of the C3d-FH19-20 complex. Mutagenesis justified the merging of the C3d-FH19-20 structure with an existing C3b-FH1-4 crystal structure. We concatenated the merged structure with the available FH6-8 crystal structure and new SAXS-derived FH1-4, FH8-15 and FH15-19 envelopes. The combined data are consistent with a bent-back factor H molecule that binds through its termini to two sites on one C3b molecule and simultaneously to adjacent polyanionic host-surface markers.