Matrix metalloproteinase-13 is fully activated by neutrophil elastase and inactivates its serpin inhibitor, alpha-1 antitrypsin: Implications for osteoarthritis.

Matrix metalloproteinase-13 (MMP-13) is a uniquely important collagenase that promotes the irreversible destruction of cartilage collagen in osteoarthritis (OA). Collagenase activation is a key control point for cartilage breakdown to occur, yet our understanding of the proteinases involved in this process is limited. Neutrophil elastase (NE) is a well-described proteoglycan-degrading enzyme which is historically associated with inflammatory arthritis, but more recent evidence suggests a potential role in OA.

Serine proteinases in the turnover of the cartilage extracellular matrix in the joint: implications for therapeutics.

Cartilage destruction is a key characteristic of arthritic disease, a process now widely established to be mediated by metzincins such as MMPs. Despite showing promise in preclinical trials during the 1990s, MMP inhibitors for the blockade of extracellular matrix turnover in the treatment of cancer and arthritis failed clinically, primarily due to poor selectivity for target MMPs. In recent years, roles for serine proteinases in the proteolytic cascades leading to cartilage destruction have become increasingly apparent, renewing interest in the potential for new therapeutic strategies that utilize pharmacological inhibitors against this class of proteinases.

Relationship between Glycation and Polyphenol Content and the Bioactivity of Selected Commercial Soy Milks.

Soy milk is a health-promoting beverage of which consumption is steadily expanding. Different bioactivities have been associated with soy products such as antioxidant capacity, anti-inflammatory properties, or decrease of cancer development risk. These activities have been related to the presence of several compounds, including polyphenols and serine protease inhibitors, although factors influencing such activities have been scarcely studied.