An immunohistochemical study of the extracellular matrix of entheses associated with the human pisiform bone.

The immunohistochemical labelling patterns of the extracellular matrix at the insertion of the flexor carpi ulnaris tendon and the entheses at both ends of the pisometacarpal and pisohamate ligaments were compared in order to relate the molecular composition of the attachment sites to their mechanical environment. Tissue was obtained from elderly dissecting room cadavers and labelled with a panel of monoclonal antibodies directed against collagens, glycosaminoglycans, proteoglycans and matrix proteins. All entheses were fibrocartilaginous and labelled positively for molecules typically associated with articular cartilage (type II collagen, chondroitin 6 sulphate, aggrecan and link protein). Labelling for type II collagen was most conspicuous at the attachment of the flexor carpi ulnaris tendon. In the ligaments, type II collagen labelling was always greater at the pisiform end. Matrilin 1 was universally present at all five entheses examined and fibromodulin labelling was most intense around the tidemark. Fibromodulin may thus be involved in anchorage and/or the control of mineralization at the hard-soft tissue interface of entheses. The greater prominence of fibrocartilage at the pisiform enthesis of the flexor carpi ulnaris tendon than at any ligament attachment may relate to the marked change in the tendon insertional angle that occurs with wrist movements. We also suggest that the more fibrocartilaginous character of the proximal compared with the distal ends of the ligaments relates to the fact that the pisiform is anchored in position and is thus at the centre of rotation of any movement of ligaments attached to it.