alpha-chymotrypsin and Bacterial-Infections

Binding of 125I-labelled types I and IV collagen, fibronectin and laminin to Aeromonas cells is a common characteristic among Aeromonas strains isolated from diseased fish and human infections. The proportion of Aeromonas strains which bind to the various proteins were significantly greater for A. hydrophila than for A. sobria or A. caviae. The binding property was specific since it was inhibited by unlabelled homologous proteins. Bacterial cells incubated with proteolytic enzymes lose the ability of binding to 125I-labelled collagen type I and IV, fibronectin, laminin and vitronectin. A bacterial cell surface protein extract, containing active receptors competes with intact cells for 125I-extracellular matrix protein binding. Culture conditions greatly influence the expression of A. hydrophila cell surface binding structures for extracellular matrix proteins. The presence of calcium ions in the growth medium seems to be an important enhancer of the expression of extracellular matrix protein cell surface receptors.

Topics: Aeromonas; Animals; Bacterial Infections; Bacterial Outer Membrane Proteins; Binding, Competitive; Calcium; Chymotrypsin; Collagen; Extracellular Matrix Proteins; Fibronectins; Fish Diseases; Fishes; Humans; Laminin; Radioligand Assay

The investigation concerned 33 systemic lupus erythematosus (SLE) patients assigned to three groups representing mild SLE, more severe extra renal SLE, and SLE with significant renal involvement. In patients with extrarenal disease, the inflammatory plasma protein response was often pronounced during exacerbation, as evidenced by markedly increased concentrations of C-reactive protein (CRP), alpha 1-antichymotrypsin, alpha 1-antitrypsin, and orosomucoid. CRP responses were rare in patients with renal involvement, despite the increased concentrations of other acute-phase reactants in some of these patients. Superimposed bacterial infections were not clearly distinguished by raised CRP concentrations. The classical pathway of complement was activated in all patients during exacerbation, as indicated by increased concentrations of C1r-C1s-C1 inactivator complexes and C2a fragments. C1, C2, and probably also C3 activation varied according to the amounts of circulating C1q-binding immune complexes, as measured by solid-phase assay. Manifest hypocomplementemia was usually associated with glomerulonephritis. Participation of complement components in the inflammatory plasma protein response apparently counteracted the development of hypocomplementemia in many patients with extrarenal SLE. Circulating C3d was detected in all patients during exacerbation of renal disease and in most patients with severe extrarenal manifestations. Inverse relationships were found between immunochemical C2 concentrations and the percentage of cleaved C2 and between C3 and C3d. There was no appreciable consumption of factors B and D and properdin of the alternative pathway in the patients. High concentrations of factor D, a low molecular weight protein, were exclusively found in patients with renal involvement and could be ascribed to retention due to reduced glomerular filtration.

Topics: alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Antigen-Antibody Complex; Bacterial Infections; C-Reactive Protein; Chymotrypsin; Complement Activating Enzymes; Complement Activation; Complement C1; Complement C1q; Complement C1r; Complement C3; Complement C4; Complement System Proteins; Humans; Lupus Erythematosus, Systemic; Orosomucoid

The intraneutrophilic concentrations of lactoferrin, myeloperoxidase, collagenase and chymotrypsin-like cationic proteins were measured sequentially during acute bacterial infection. The serum levels of lactoferrin and myeloperoxidase were also followed as well as the 'eosinophil' cationic protein as a marker for eosinophil leucocytes. During the early course of infection there was a profound but reversible decrease of intraneutrophilic lactoferrin. The levels of cellular collagenase and chymotrypsin-like cationic proteins also tended to decrease reversibly during day 2-8 in most cases; myeloperoxidase levels were normal except for two cases. Serum myeloperoxidase and lactoferrin correlated with blood neutrophil counts. In spite of the absence of peripheral eosinophils the 'eosinophil' cationic proteins of serum were increased on the first day of infection, which may reflect increased eosinophil turnover.

Topics: Bacterial Infections; Blood Proteins; Chymotrypsin; Eosinophils; Granulocytes; Humans; Lactoferrin; Leukocyte Count; Leukocytes; Microbial Collagenase; Neutrophils; Peroxidase

Topics: Animals; Antigens, Neoplasm; Bacterial Infections; Benzopyrenes; Cell Migration Inhibition; Chromatography, Gel; Chymotrypsin; Fibrosarcoma; Intradermal Tests; Leukocytes; Lymphocytes; Male; Molecular Weight; Rats; Rats, Inbred WF; Spleen; T-Lymphocytes; Thoracic Duct

When a tissue is injured, its vessels exhibit a marked increase in vascular permeability. Blood proteins, including fibrinogen, traverse the vessel walls and lead to the development of a surface coagulum. This inflammatory response continues until primary closure of the wound edges is accomplished. The thickness of the surface coagulum is roughly proportional to the time interval between wounding and closure. This coagulum encompasses the surface contaminants, preventing contact with either topical or systemic antibiotics. The presence of this surface coagulum limits the time in which antibiotic prophylaxis is effective. At three hours after injury, antimicrobial prophylaxis of contaminated wounds has no therapeutic value. Hydrolysis of the protein coagulum by proteolytic enzymes enhances the activity of the antibiotic in experimental wounds. The success of proteolytic enzymes as adjuncts to delayed antibiotic treatment can be correlated with the clot lysis activity of the enzymes in vitro. Travase, the most potent fibrinolytic enzyme, is the most effective adjunct to delayed antibiotic therapy of contaminated wounds. In contrast, the active enzymes found in Elase, which exhibit no significant clot lysis activity in vitro, do not potentiate the activity of antibiotics in wounds subjected to a delay in treatment. Travase prolongs the period of effective topical antibiotic action for at least eight hours in experimental contaminated wounds. The therapeutic merit of Travase is also apparent when the antibiotic is administered systemically. Travase shows promise as an adjunct to a variety of antibiotics that are effective against both gram-positive and gram-negative organisms. The results of these experimental studies support our belief that clinical studies support our belief that clinical studies should now be initiated to test the therapeutic value of Travase as an adjunct to antibiotics in heavily contaminated wounds subjected to an unavoidable delay in treatment.

Topics: Animals; Anti-Bacterial Agents; Bacillus subtilis; Bacteria; Bacterial Infections; Blood Coagulation; Bromelains; Chymotrypsin; Deoxyribonucleases; Drug Synergism; Fibrinolysin; Guinea Pigs; Hydrolysis; Papain; Peptide Hydrolases; Protein Denaturation; Streptodornase and Streptokinase; Subtilisins; Surgical Wound Infection; Time Factors; Trypsin

Topics: Bacterial Infections; Chymotrypsin; Drug Therapy, Combination; Focal Infection, Dental; Humans; Jaw Diseases; Tetracycline; Trypsin