4-corner arthrodesis and proximal row carpectomy: a biomechanical comparison of wrist motion and tendon forces.

PURPOSE: Controversy exists as to whether a proximal row carpectomy (PRC) is a better procedure than scaphoid excision with 4-corner arthrodesis for preserving motion in the painful posttraumatic arthritic wrist. The purpose of this study was to determine how the kinematics and tendon forces of the wrist are altered after PRC and 4-corner arthrodesis. METHODS: We tested 6 fresh cadaver forearms for the extremes of wrist motion and then used a wrist simulator to move them through 4 cyclic dynamic wrist motions, during which time we continuously recorded the tendon forces. We repeated the extremes of wrist motion measurements and the dynamic motions after scaphoid excision with 4-corner arthrodesis, and then again after PRC. We analyzed extremes of wrist motion and the peak tendon forces required for each dynamic motion using a repeated measures analysis of variance. RESULTS: Wrist extremes of motion significantly decreased after both the PRC and 4-corner arthrodesis compared with the intact wrist. Wrist flexion decreased on average 13° after 4-corner arthrodesis and 12° after PRC. Extension decreased 20° after 4-corner arthrodesis and 12° after PRC. Four-corner arthrodesis significantly decreased wrist ulnar deviation from the intact wrist. Four-corner arthrodesis allowed more radial deviation but less ulnar deviation than the PRC. The average peak tendon force was significantly greater after 4-corner arthrodesis than after PRC for the extensor carpi ulnaris during wrist flexion-extension, circumduction, and dart throw motions. The peak forces were significantly greater after 4-corner arthrodesis than in the intact wrist for the extensor carpi ulnaris during the dart throw motion and for the flexor carpi ulnaris during the circumduction motion. The peak extensor carpi radialis brevis force after PRC was significantly less than in the intact wrist. CONCLUSIONS: The measured wrist extremes of motion decreased after both 4-corner arthrodesis and PRC. Larger peak tendon forces were required to achieve identical wrist motions with the 4-corner arthrodesis compared with the intact wrist. We observed smaller forces for the PRC. CLINICAL RELEVANCE: These results may help explain why PRC shows early clinical improvement, yet may lead to degenerative arthritis.

The role of the specificity-determining loop of the integrin beta subunit I-like domain in autonomous expression, association with the alpha subunit, and ligand binding.

Integrin beta subunits contain a highly conserved I-like domain that is known to be important for ligand binding. Unlike integrin I domains, the I-like domain requires integrin alpha and beta subunit association for optimal folding. Pactolus is a novel gene product that is highly homologous to integrin beta subunits but lacks associating alpha subunits [Chen, Y., Garrison, S., Weis, J. J., and Weis, J. H. (1998) J. Biol. Chem. 273, 8711-8718] and a approximately 30 amino acid segment corresponding to the specificity-determining loop (SDL) in the I-like domain. We find that the SDL is responsible for the defects in integrin beta subunit expression and folding in the absence of alpha subunits. When transfected in the absence of alpha subunits into cells, extracellular domains of mutant beta subunits lacking SDL, but not wild-type beta subunits, were well secreted and contained immunoreactive I-like domains. The purified recombinant soluble beta1 subunit with the SDL deletion showed an elongated shape in electron microscopy, consistent with its structure in alphabeta complexes. The SDL segment is not required for formation of alpha5beta1, alpha4beta1, alphaVbeta3, and alpha6beta4 heterodimers, but is essential for fomation of alpha6beta1, alphaVbeta1, and alphaLbeta2 heterodimers, suggesting that usage of subunit interface residues is variable among integrins. The beta1 SDL is required for ligand binding and for the formation of the epitope for the alpha5 monoclonal antibody 16 that maps to loop segments connecting blades 2 and 3 of beta-propeller domain of alpha5, but is not essential for nearby beta-propeller epitopes.