Fibrocartilage in the transverse ligament of the human acetabulum.
Biomechanical experiments on isolated hip joints have suggested that the transverse ligament acts as a bridle for the lunate articular surface of the acetabulum during load bearing, but there are inherent limitations in such studies because the specimens are fixed artificially to testing devices and there are no modifying influences of muscle pull. Further evidence is thus needed to substantiate the theory. Here we argue that if the horns of the lunate surface are forced apart under load, the ligament would straighten and become compressed against the femoral head. It would thus be expected to share some of the features of tendons and ligaments that wrap around bony pulleys and yet previous work has suggested that the transverse ligament is purely fibrous. Transverse ligaments were removed from 8 cadavers (aged 17-39 y) and fixed in 90% methanol. Cryosections were immunolabelled with antibodies against collagens (types I, II, III, VI), glycosaminoglycans (chondroitins 4 and 6 sulphate, dermatan sulphate, keratan sulphate) and proteoglycans (aggrecan, link protein, versican, tenascin). A small sesamoid fibrocartilage was consistently present in the centre of each transverse ligament, near its inner surface at the site where it faced the femoral head. Additionally, a more prominent enthesis fibrocartilage was found at both bony attachments. All fibrocartilage regions, in at least some specimens, labelled for type II collagen, chondroitin 6 sulphate, aggrecan and link protein, molecules more typically associated with articular cartilage. The results suggest that the ligament should be classed as containing a 'moderately cartilaginous' sesamoid fibrocartilage, adapted to withstanding compression. This supports the inferences that can be drawn from previous biomechanical studies. We cannot give any quantitative estimate of the levels of compression experienced. All that can be said is that the ligament occupies an intermediate position in the spectrum of fibrocartilaginous tissues. It is more cartilaginous than some wrap-around tendons at the wrist, but less cartilaginous than certain other wrap-around ligaments, e.g. the transverse ligament of the atlas.
Anatomische Anstalt, Ludwig-Maximilians-Universität, München, Germany. stefan.milz@anat.med.uni-muenchen.de
S
S
Milz
G
G
Valassis
A
A
Büttner
M
M
Maier
R
R
Putz
J R
JR
Ralphs
M
M
Benjamin
D000077:Acetabulum; D000293:Adolescent; D000328:Adult; D053674:Aggrecans; D002356:Cartilage / Q000737:chemistry*; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis; D002809:Chondroitin Sulfates / Q000032:analysis; D003094:Collagen / Q000032:analysis*; D003871:Dermatan Sulfate / Q000032:analysis; D016326:Extracellular Matrix Proteins; D005260:Female; D006025:Glycosaminoglycans / Q000032:analysis*; D006801:Humans; D007150:Immunohistochemistry; D007632:Keratan Sulfate / Q000032:analysis; D037181:Lectins, C-Type; D008297:Male; D011506:Proteins / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis*; D053675:Versicans; D000099249:Proteoglycan Link Protein
D053674:Aggrecans; D011508:Chondroitin Sulfate Proteoglycans; D002809:Chondroitin Sulfates; D003094:Collagen; D003871:Dermatan Sulfate; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D007632:Keratan Sulfate; D037181:Lectins, C-Type; D011506:Proteins; D011509:Proteoglycans; D053675:Versicans; D000099249:Proteoglycan Link Protein; C508322:VCAN protein, human