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Elastase activity, uninhibited by α 1 ‐antitrypsin, in the periprosthetic connective matrix around loose total hip prostheses
Author(s) -
Takagi Michiaki,
Konttinen Yrjö T.,
Santavirta Seppo,
Kangaspunta Petri,
Sorsa Timo,
Yamakawa Mitsunori,
Suda Akio
Publication year - 1995
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100130218
Subject(s) - elastase , periprosthetic , connective tissue , chemistry , pancreatic elastase , proteinase inhibitor , prosthesis , immunohistochemistry , proteolytic enzymes , matrix metalloproteinase , pathology , enzyme , microbiology and biotechnology , anatomy , medicine , biochemistry , arthroplasty , biology , surgery
To clarify the proteolytic cascade in the loosening of total hip prostheses, the presence, tissue localization, and content of the serine proteinase, elastase, and its endogenous inhibitor, α 1 ‐antitrypsin, were studied in perioprosthetic tissues around 12 loose hip prostheses by immunohistochemistry, spectrophotometric enzyme assay, and immunoblot analysis, and the results were compared with those in control synovial tissue samples from eight knees. Increased numbers of elastase‐immunoreactive cells and elevated elastase activity, inhibited by the addition of native α 1 ‐antitrypsin, were observed both in the interface tissues between the bone and implants and in the pseudocapsular tissues from around loose hip prostheses. Elevated elastase activity, uninhibited by α 1 ‐antitrypsin in situ and inhibited by the addition of native inhibitor, suggests a proteinase‐inhibitor imbalance that contributes to the weakening of periprosthetic tissues and thus causes the loosening of hip prostheses.