The molecular composition of the extracellular matrix of the human iliolumbar ligament

The human iliolumbar ligament connects the transverse process of L5 to the iliac crest and contributes to lumbosacral stability and has been associated with low back pain. However, different opinions exist regarding the functional relevance of the ligament.

In the present study, we analyze the regional molecular composition of the ligament extracellular matrix.

Special attention is given to the attachment sites, to determine whether the ligament is subjected to a certain mechanical environment.

Iliolumbar ligament samples, extending from one enthesis to the other, were removed from 11 cadavers and fixed in methanol. Cryosections were immunolabeled with a panel of antibodies directed against collagens, glycosaminoglycans, proteoglycans, matrix proteins, and neurofilament.

The mid-substance of the ligament labeled for all the molecules normally found in dense fibrous connective tissue including types I, III, and VI collagen, versican, dermatan -, chondroitin 4 -, and keratan sulfate. However, both entheses were fibrocartilaginous and labeled for type II collagen, aggrecan, and chondroitin 6- sulfate. A common feature was fat between the fiber bundles near the entheses. Occasionally this fat contained nerve fibers.

The existence of fibrocartilaginous entheses suggests that the insertion sites of the ligament are subject to both tensile and compressive loading-probably because of insertional angle changes between ligament and bone during loading. Our findings support the suggestion that the iliolumbar ligament might play an important role in the stabilization of the lumbosacral junction.