Immunohistological detection of relaxin binding to anterior cruciate ligaments.

Relaxin, a member of the insulin-like growth factor family, alters collagen metabolism in fibroblasts. It was hypothesized that relaxin interacts with the anterior cruciate ligament (ACL), contributing to its elasticity. Twelve ACL specimens were collected from reconstruction surgeries, sectioned, rinsed, and exposed to rh-relaxin overnight. Polyclonal antirelaxin antibodies, in conjunction with HRP-AEC, localized areas of tissue binding. Controls were used to infer binding specificity. Staining was present in the positive control and all 12 ACL specimens; little or no staining occurred in the negative controls. These data suggest that relaxin binding to the ACL is specific, indicative of a receptor-mediated event.