This Article Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Sathyamoorthy, P. Articles by Frostick, S.P. Search for Related Content PubMed Articles by Sathyamoorthy, P. Articles by Frostick, S.P.

GELATINASE MMPS IN ASEPTIC LOOSENING OF SHOULDER PROSTHESES

Departmen of Musculoskeletal Science, The Royal Liverpool University Hospital, Prescot Street, Liverpool

The role of matrix metalloproteinases (MMPs) in the aseptic loosening of hip prostheses is well established. Gelatinase MMPs have been identified in the interface membranes and the pseudosynovial tissues in the hips. Little data are available on gelatinase MMPs and their major regulators, including specific tissue inhibitors of matrix metalloproteinases (TIMPs) in the loosening of shoulder prostheses. The objectives of this study were to determine whether A) gelatinase MMPs and their regulators (MMP14, TIMP-1,-2) are produced by periprosthetic tissues in cases of aseptic loosening of shoulder prostheses, and, B) to identify which cell types, in both interface and synovial tissues, localize the enzymes.

Interface tissues and synovial tissues were obtained during revision surgery for loose shoulder implants. In 9 patients (6-Total Shoulder Replacement, 3-Hemiarthro-plasty (Bipolar), 9 samples of interface tissues and 8 samples of synovial tissues were obtained. Of the interface tissues 2 were from the interface of the bipolar and the unresurfaced glenoid. Formalin-fixed paraffin embedded sections were stained using primary antibodies for MMP2 (Neomarkers), MMP9 (Oncogene Ltd), TIMP1, TIMP2 & MMP14 (Chemicon Ltd). Antigen retrieval required pressure cooker treatment for MMP2 and MMP9 and trypsin for TIMP1. Visualisation used a standard DAB chromagen technique (Envision, Dako Ltd.). Appropriate control sections ensured reproducibility of the staining. The antibodies selected bind to both active and inactive forms of the MMPs.

Both HDPE and metal debris were seen in both the synovial and interface tissues. Transformation of macrophages to giant cells was associated with PE debris, and was not observed with metal debris alone.

The presence of gelatinase MMPs in both interface and synovial tissues in aseptic loosening of shoulder prostheses was demonstrated. Differences between the MMP content of macrophages and giant cells between the tissues was detected, positivity was associated with the presence of metallic and/or HDPE debris. Activation of endothelial MMP2 by both MMP14 and low levels of TIMP2 would support the development of a vascular network.

Abstracts prepared by Dr P E Watkins, Hodgkin Building, Guys Campus, King’s College London.