title: An immunohistochemical study of the triangular fibrocartilage complex of the wrist: regional variations in cartilage phenotype.
abstract: The triangular fibrocartilage complex (TFCC) transmits load from the wrist to the ulna and stabilizes the distal radioulnar joint. Damage to it is a major cause of wrist pain. Although its basic structure is well established, little is known of its molecular composition. We have analysed the immunohistochemical labelling pattern of the extracellular matrix of the articular disc and the meniscal homologue of the TFCC in nine elderly individuals (age range 69-96 years), using a panel of monoclonal antibodies directed against collagens, glycosaminoglycans, proteoglycans and cartilage oligomeric matrix protein (COMP). Although many of the molecules (types I, III and VI collagen, chondroitin 4 sulphate, dermatan sulphate and keratan sulphate, the oversulphated epitope of chondroitin 6 sulphate, versican and COMP) were found in all parts of the TFCC, aggrecan, link protein and type II collagen were restricted to the articular disc and to entheses. They were thus not a feature of the meniscal homologue. The shift in tissue phenotype within the TFCC, from a fibrocartilaginous articular disc to a more fibrous meniscal homologue, correlates with biomechanical data suggesting that the radial region is stiff and subject to considerable stress concentration. The presence of aggrecan, link protein and type II collagen in the articular disc could explain why the TFCC is destroyed in rheumatoid arthritis, given that it has been suggested that autoimmunity to these antigens results in the destruction of articular cartilage. The differential distribution of aggrecan within the TFCC is likely to be reflected by regional differences in water content and mobility on the radial and ulnar side. This needs to be taken into account in the design of improved MRI protocols for visualizing this ulnocarpal complex of the wrist.
authors.affiliation: AO Research Institute, AO Foundation, Davos, Switzerland. stefan.milz@aofoundation.org
authors.forename: S
authors.initials: S
authors.lastname: Milz
authors.forename: B
authors.initials: B
authors.lastname: Sicking
authors.forename: C M
authors.initials: CM
authors.lastname: Sprecher
authors.forename: R
authors.initials: R
authors.lastname: Putz
authors.forename: M
authors.initials: M
authors.lastname: Benjamin
mesh_terms: D000368:Aged; D000369:Aged, 80 and over; D053674:Aggrecans / Q000032:analysis; D015415:Biomarkers / Q000032:analysis; D024042:Collagen Type I / Q000032:analysis; D024061:Collagen Type III / Q000032:analysis; D024142:Collagen Type VI / Q000032:analysis; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005260:Female; D006025:Glycosaminoglycans / Q000032:analysis; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D011509:Proteoglycans / Q000032:analysis; D011884:Radius; D019063:Tenascin / Q000032:analysis; D051478:Triangular Fibrocartilage / Q000737:chemistry* / Q000648:ultrastructure; D014457:Ulna; D053675:Versicans / Q000032:analysis; D000099249:Proteoglycan Link Protein
chemical_list: D053674:Aggrecans; D015415:Biomarkers; D024042:Collagen Type I; D024061:Collagen Type III; D024142:Collagen Type VI; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D011509:Proteoglycans; D019063:Tenascin; D053675:Versicans; D000099249:Proteoglycan Link Protein