Fibrocartilage in the extensor tendons of the human metacarpophalangeal joints.
The extensor tendons of the fingers cross both the metacarpophalangeal (MCP) and interphalangeal joints. Previous studies have shown that where the extensor tendons replace the capsule of the proximal interphalangeal (PIP) joint, they contain a sesamoid fibrocartilage that articulates with the proximal phalanx during flexion. The fibrocartilage labels immunohistochemically for a variety of glycosaminoglycans and collagens. In the current study, we investigate the molecular composition of the extensor tendons at the level of the MCP joints. This is of particular interest because the tendon has a greater moment arm at this location (and might thus be subject to greater compression), but is separated from the joint cavity by the capsule and peritendinous tissue. Six hands were removed from elderly cadavers (39-85 years of age) and the MCP joints were fixed in 90% methanol. The extensor tendons were dissected from all fingers, cryosectioned, and immunolabelled with a panel of monoclonal and polyclonal antibodies for types I, II, III, and VI collagens, chondroitin 4 and 6 sulphates, dermatan, and keratan sulphate and aggrecan. Antibody binding was detected with the Vectastain ABC 'Elite' avidin/biotin/peroxidase kit. The extensor tendons in all the fingers had a metachromatic sesamoid fibrocartilage on their deep surface which immunolabelled for types I, III, and VI collagens, and for all glycosaminoglycans and aggrecan. Labelling for type II collagen was also seen in some fibrocartilages and was a constant feature of all index fingers. This probably relates to the greater use of that digit and the higher loads to which its tendons are subject. Chondroitin 6 sulphate and type II collagen are the most consistent markers of the fibrocartilage phenotype and most of the chondroitin 6 sulphate is probably associated with aggrecan. It is concluded that the labelling profile of the tendon fibrocartilage in the different fingers at the MCP joints is broadly similar to that at the PIP joints. Thus, the potentially greater level of compression on the extensor tendons may be counterbalanced by the lack of fusion of the tendon with the joint capsule. It is suggested that the maintenance of a similar level of fibrocartilage differentiation at two different points along the length of the extensor tendon ensures that the tensile strength is the same in the two regions and that no weak link is present.
Milz
S
S
Anatomische Anstalt, Ludwig-Maximilians-Universität, D-80336 München, Germany. milz@anat.uni-muenchen.de
Putz
R
R
Ralphs
J R
JR
Benjamin
M
M
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D053674:Aggrecans; D002358:Cartilage, Articular / Q000033:anatomy & histology* / Q000378:metabolism; D002809:Chondroitin Sulfates / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D003871:Dermatan Sulfate / Q000378:metabolism; D016326:Extracellular Matrix Proteins; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D007632:Keratan Sulfate / Q000378:metabolism; D037181:Lectins, C-Type; D008297:Male; D008662:Metacarpophalangeal Joint / Q000033:anatomy & histology* / Q000378:metabolism; D008875:Middle Aged; D011509:Proteoglycans / Q000378:metabolism; D013710:Tendons / Q000033:anatomy & histology* / Q000378:metabolism
D053674:Aggrecans; D016326:Extracellular Matrix Proteins; D037181:Lectins, C-Type; D011509:Proteoglycans; D003871:Dermatan Sulfate; D002809:Chondroitin Sulfates; D003094:Collagen; D007632:Keratan Sulfate