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The Laboratory for Soft Tissue Research, The Hospital for Special Surgery, affiliated with Cornell University Medical College, New York, New York
Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina
Presented at the interim meeting of the AOSSM, San Francisco, California, February 1997.
Address correspondence and reprint requests to Scott A. Rodeo, MD, The Hospital for Special Surgery, 535 East 70th Street, New York, NY 10021
This study examined collagen cross-links, collagen fibril diameter and density, amino acid composition, and elastic fibers in shoulder capsule and skin in four patient groups: 1) unidirectional anterior instability (N = 8); 2) multidirectional instability/primary surgery (N = 6); 3) multidirectional instability/revision sur-gery (N = 6); and 4) no history of instability (N = 5). Compared with normal capsule, capsule from groups 1 and 2 had more stable and reducible collagen cross-links, significantly greater mean collagen fibril diameter, more cysteine, and a higher density of elastin staining. Compared with shoulder capsule in groups 1 and 2, shoulder capsule from group 3 contained significantly more reducible cross-links, smaller-diameter collagen fibrils, decreased collagen fibril density, and an increased density of elastin staining. There were no significant differences in any parameters between groups 1 and 2. We hypothesized that repeated capsular deformation in patients with shoulder instability results in changes in the capsule that increase its strength and resistance to stretching. Skin analyses demonstrated a significantly smaller mean collagen fibril diameter in skin from group 2 compared with group 1, suggesting the possibility of an underlying connective tissue abnormality.
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