Proteolytic and lysosomal enzymes in acute trauma-induced lung injury in sheep. 1989

S Andreasson, and L Smith, and A O Aasen, and O K Andersen, and B Risberg
Department of Anesthesia, University of Gothenburg, Sweden.

Surgical preparation of a lung lymph fistula in sheep was previously shown to induce temporary permeability disturbance of pulmonary microvessels. Flow and composition of lung lymph were compared in 19 sheep with acute, and 16 with chronic lymph fistula. Lymph and plasma were analyzed regarding activities of prothrombin, antithrombin III, prekallikrein, kallikrein, functional kallikrein inhibitors and 11 acid hydrolases of lysosomal origin. Levels of prothrombin and antithrombin III fell postoperatively in plasma and reached even lower values in lymph, indicating systemic activation of the coagulation system as well as local activation in the lung. The studied components of the plasma-kallikrein system were unchanged. Lysosomal enzymes were released in lung lymph, reflecting cell injury in the lung. Local activation of proteolytic enzyme systems thus occurs in the lung after trauma. Analysis of organ-specific lymph (= interstitial fluid) may contribute to better understanding of the pathophysiology of trauma.

UI MeSH Term Description Entries
D007610 Kallikreins Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77). Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007705 Kinins A generic term used to describe a group of polypeptides with related chemical structures and pharmacological properties that are widely distributed in nature. These peptides are AUTACOIDS that act locally to produce pain, vasodilatation, increased vascular permeability, and the synthesis of prostaglandins. Thus, they comprise a subset of the large number of mediators that contribute to the inflammatory response. (From Goodman and Gilman's The Pharmacologic Basis of Therapeutics, 8th ed, p588) Kinin
D008168 Lung Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood. Lungs
D008196 Lymph The interstitial fluid that is in the LYMPHATIC SYSTEM. Lymphs
D008198 Lymph Nodes They are oval or bean shaped bodies (1 - 30 mm in diameter) located along the lymphatic system. Lymph Node,Node, Lymph,Nodes, Lymph
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D001777 Blood Coagulation The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot. Blood Clotting,Coagulation, Blood,Blood Clottings,Clotting, Blood
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012756 Sheep Any of the ruminant mammals with curved horns in the genus Ovis, family Bovidae. They possess lachrymal grooves and interdigital glands, which are absent in GOATS. Ovis,Sheep, Dall,Dall Sheep,Ovis dalli

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