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Enzymatic adaptation in ligaments during immobilization

Division of Orthopaedic Surgery, Department of Surgery, Stanford University School of Medicine, Palo Alto, California

Charles C. Edwards, MD

Division of Orthopaedic Surgery,University of Maryland School of Medicine, Baltimore, Maryland

Stephen R. Max, PhD

Department of Neurology, University of Maryland School of Medicine, Baltimore, Maryland

Ligaments are a composite of fibroblasts and collagen in a proteoglycan matrix. Seventy-five percent of the organic solid is collagen and 23% is proteoglycan. Fibroblasts are responsible for the overall composition of the ligament, that is the synthesis and the degrada tion of macromolecular components. Like muscle and bone, ligaments are dynamic, undergoing hypertrophy with exercise and atrophy with immobilization. This paper reviews the structure and composition of liga ments and discusses the cellular events responsible for atrophy of ligaments with immobilization. As an exper imental model, one knee of New Zealand White rabbits was immobilized with a pin. After 2, 4, and 8 weeks of immobility, the medial collateral ligaments were isolated and enzyme analysis was performed. Gross and micro scopic changes were apparent after 2 weeks. As for enzyme changes, lactic dehydrogenase and malic de hydrogenase decreased in activity. The lysosomal hy drolases responsible for glycosaminoglycan degrada tion increased in activity, suggesting that enzymatic adaptations mediate the physical and chemical changes in the ligament. The cells switch from an anabolic synthetic state to a catabolic, degradative state during immobility. It would seem from the biochemical view point that, whenever possible, cast-bracing and func tional splints may be preferable to rigid plasters in many sports-related ligamentous injuries.

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