Femoroacetabular impingement (FAI) causes pain
and chondrolabral damage via mechanical overload during movement
of the hip. It is caused by many different types of pathoanatomy,
including the cam ‘bump’, decreased head–neck offset, acetabular
retroversion, global acetabular overcoverage, prominent anterior–inferior
iliac spine, slipped capital femoral epiphysis, and the sequelae
of childhood Perthes’ disease. Both evolutionary and developmental factors may cause FAI. Prevalence
studies show that anatomic variations that cause FAI are common
in the asymptomatic population. Young athletes may be predisposed
to FAI because of the stress on the physis during development. Other
factors, including the soft tissues, may also influence symptoms and
chondrolabral damage. FAI and the resultant chondrolabral pathology are often treated
arthroscopically. Although the results are favourable, morphologies
can be complex, patient expectations are high and the surgery is
challenging. The long-term outcomes of hip arthroscopy are still
forthcoming and it is unknown if treatment of FAI will prevent arthrosis.
As our understanding of hip function and disease improves, it is evident that the acetabular fossa has received little attention, despite it comprising over half of the acetabulum’s surface area and showing the first signs of degeneration. The fossa’s function is expected to be more than augmenting static stability with the ligamentum teres and being a templating landmark in arthroplasty. Indeed, the fossa, which is almost mature at 16 weeks of intrauterine development, plays a key role in
Aims. Femoroacetabular impingement (FAI) is a potential cause of hip osteoarthritis (OA). The purpose of this study was to investigate the expression profile of matrix metalloproteinases (MMPs) in the labral tissue with FAI pathology. Methods. In this study, labral tissues were collected from four FAI patients arthroscopically and from three normal hips of deceased donors. Proteins extracted from the FAI and normal labrums were separately applied for MMP array to screen the expression of seven MMPs and three tissue inhibitors of metalloproteinases (TIMPs). The expression of individual MMPs and TIMPs was quantified by densitometry and compared between the FAI and normal labral groups. The expression of selected MMPs and TIMPs was validated and localized in the labrum with immunohistochemistry. Results. On MMP arrays, most of the targeted MMPs and TIMPs were detected in the FAI and normal labral proteins. After data normalization, in comparison with the normal labral proteins, expression of MMP-1 and MMP-2 in the FAI group was increased and expression of TIMP-1 reduced. The histology of the FAI labrum showed disorderly cell distribution and altered composition of thick and thin collagen fibres. The labral cells expressing MMP-1 and MMP-2 were localized and their percentages were increased in the FAI labrum. Immunohistochemistry confirmed that the percentage of TIMP-1 positive cells was reduced in the FAI labrum. Conclusion. This study established an expression profile of MMPs and TIMPs in the FAI labrum. The increased expression of MMP-1 and MMP-2 and reduced expression of TIMP-1 in the FAI labrum are indicative of a pathogenic role of FAI in
