Non-invasive ventilation corrects alveolar hypoventilation during spinal anesthesia.

Purpose: To document and explain the beneficial effects of non-invasive ventilation in correcting hypoxemia and hypoventilation in severe chronic obstructive pulmonary disease, during spinal anesthesia in the lithotomy position.

Clinical Features: A morbidly obese patient with severe chronic obstructive pulmonary disease underwent prostate surgery in the lithotomy position under spinal anesthesia. Hypoxemia was encountered during surgery, and a profound decrease of forced vital capacity associated with alveolar hypoventilation and ventilation/perfusion mismatching were observed.

Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids.

Background Information: Chronic inflammation and tissue remodelling result from an imbalance between proteolytic enzymes and their inhibitors in the lungs in favour of proteolysis. While many studies have examined serine proteases (e.g.

Cysteine cathepsins in human silicotic bronchoalveolar lavage fluids.

Mature, active cysteine cathepsins (CPs) were identified in human inflammatory bronchoalveolar lavage fluid (BALF) supernatants from patients suffering from silicosis by both western blot and surface plasmon resonance analyses. BALFs are not a reservoir of activatable proforms, since no autocatalytic maturation at acidic pH occurs. Cathepsin H is the most profuse among studied CPs (median value: 36.

Competition between elastase and related proteases from human neutrophil for binding to alpha1-protease inhibitor.

The protease-antiprotease imbalance that is characteristic of most inflammatory lung disorders depends on the spatial-temporal regulation of active inhibitor and protease concentrations in lung secretions. We have studied the competition between the three main serine proteases from human neutrophil primary granules in their binding to alpha1-Pi, the main serine proteases inhibitor in lung secretions. Elastase was the only target of alpha1-Pi when identical molar amounts of purified inhibitor and the three proteases were tested together.

Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates.

Human neutrophil elastase (HNE) has long been linked to the pathology of a variety of inflammatory diseases and therefore is a potential target for therapeutic intervention. At least two other serine proteases, proteinase 3 (Pr3) and cathepsin G, are stored within the same neutrophil primary granules as HNE and are released from the cell at the same time at inflammatory sites. HNE and Pr3 are structurally and functionally very similar, and no substrate is currently available that is preferentially cleaved by Pr3 rather than HNE.

Measurement of free and membrane-bound cathepsin G in human neutrophils using new sensitive fluorogenic substrates.

Activated human polymorphonuclear neutrophils at inflammatory sites release the chymotrypsin-like protease cathepsin G, together with elastase and proteinase 3 (myeloblastin), from their azurophil granules. The low activity of cathepsin G on synthetic substrates seriously impairs studies designed to clarify its role in tissue inflammation. We have solved this problem by producing new peptide substrates with intramolecularly quenched fluorescence.