muramidase and Pleurisy

Lung cancer remains the leading cause of cancer death over the world. Although new diagnostic methods have been discovered, new biomarkers of the cancer are still under studying. A human chitinolytic enzyme called chitotriosidase hydrolyzes chitin and chitotrioside substrates. It is specifically expressed by activating macrophages and seems to play a role in the defense against chitinous human pathogens. Recently it has been shown that chitotriosidase may also attend to the inflammatory process. The aim of the study was to determine chitotriosidase activity in serum of patients with lung cancer and patients with inflammatory exudate. We studied the usefulness of the above parameter determination in differentiation between lung cancer and inflammation. In addition, serum activity of lysozyme and cathepsin H was determined.. The study included 17 patients with inflammatory pleural exudate--group 1., 40 lung cancer patients with malignant pleural effusion--group 2. and 37 healthy subjects. All the patients of group 2. were divided into 2 subgroups: 2A without metastases (n = 23) and 2B with metastases (n = 17). Chitotriosidase and cathepsin H activity was determined in serum by a fluorometric methods. Serum lysozyme activity was measured by turbidimetric method with Micrococcus luteus as substrate.. We observed an increase of the chitotriosidase activity in serum patients of both studied group in comparison with the control. The activity of the chitotriosidase in lung cancer patients was significantly higher than in the control (36.7 vs 68.1 nmol/ml/h; p < 0.01). There were no significant differences in serum lysozyme and cathepsin H activity in patients in comparison to healthy subjects.. The results suggest that activity of the chitotriosidase can not be used to differentiation between inflammation and cancer in lung.

Topics: Aged; Biomarkers, Tumor; Cathepsin H; Cathepsins; Cysteine Endopeptidases; Diagnosis, Differential; Female; Hexosaminidases; Humans; Lung Neoplasms; Male; Muramidase; Pleural Effusion; Pleural Effusion, Malignant; Pleurisy

The anti-inflammatory effect of total phenolics from Laggera alata (TPLA) was evaluated with various in vivo models of both acute and chronic inflammations. In the acute inflammation tests, TPLA inhibited significantly xylene-induced mouse ear oedema, carrageenan-induced rat paw oedema and acetic acid-induced mouse vascular permeability. In the carrageenan-induced rat pleurisy model, TPLA significantly suppressed inflammatory exudate and leukocyte migration, reduced the serum levels of lysozyme (LZM) and malondialdehyde (MDA), increased the serum levels of superoxide dismutase (SOD) and glutathione peroxidase (GSH-PX), and also decreased the contents of total protein, nitric oxide (NO) and prostaglandin E(2) (PGE(2)) in the pleural exudates. In the chronic inflammation experiment, TPLA inhibited significantly cotton pellet-induced rat granuloma. These results indicated that TPLA possesses potent anti-inflammatory activity on acute and chronic inflammation models. Its anti-inflammatory mechanisms are probably associated with the inhibition of prostaglandin formation, the influence on the antioxidant systems, and the suppression of LZM release. Furthermore, the total phenolic content of Laggera alata and its main component type was quantified, and its principle components were isolated and authenticated. Acute toxicity studies revealed that TPLA up to an oral dose of 8.5 g/kg body weight was almost nontoxic in mice.

Topics: Acute Disease; Animals; Asteraceae; Capillary Permeability; Carrageenan; Chronic Disease; Dexamethasone; Ear, External; Edema; Glutathione Peroxidase; Inflammation; Male; Malondialdehyde; Mice; Mice, Inbred ICR; Muramidase; Nitric Oxide; Plant Extracts; Pleurisy; Quinic Acid; Rats; Rats, Sprague-Dawley; Superoxide Dismutase; Xylenes

Immunohistochemical phenotyping of 7 cases of histioeosinophilic granulomas of thymus and 4 cases of reactive eosinophilic pleuritis was performed. All 11 cases of these 2 entities reacted identically. This supports the view that these 2 lesions are similar in nature. Both lesions are reactions to the presence of insufflated gas and its resorption.

Topics: Antibodies, Monoclonal; Biomarkers; Eosinophilic Granuloma; Humans; Immunohistochemistry; Lymphatic Diseases; Muramidase; Myasthenia Gravis; Phenotype; Pleurisy; Receptors, Cholinergic; Thymus Gland

An immunoblotting technique was developed to detect human lysozyme and lysozyme complexes in body fluids. The unoccupied binding capacity of proteins was demonstrated by addition of surplus lysozyme. The sensitivity of immunoblotting to the free enzyme in human albumin solution was less than 5 ng. In serum and pleural fluid, part of exogenous lysozyme was bound to alpha 2-macroglobulin (alpha 2-M). At high concentrations of lysozyme in leukemic sera, part of the enzyme formed an endogenous alpha 2-M complex. On the other hand, the formation of alpha 2-M complexes with exogenous lysozyme was especially striking in sera from nephrotic patients with elevated alpha 2-M. The findings corroborate with previous reports on lysozyme binding to purified alpha 2-M in vitro and suggest that the binding is concentration-dependent with respect to both reaction partners. In vivo the mechanism may provide a pathway for extrarenal lysozyme catabolism medicated by reticuloendothelial cells. No other binding proteins were seen in the present study: lysozyme did not bind to serum immunoglobulins in 35 samples with an immunoglobulin paraprotein, three samples with polyclonally elevated gamma-globulins, 20 other patient sera and 10 normal sera. Neither did lysozyme bind to urinary proteins in five samples from patients with myeloic leukemias nor in 10 samples from myeloma patients with urinary excretion of a monoclonal immunoglobulin light chain.

Topics: alpha-Macroglobulins; Humans; Immunoblotting; Immunologic Deficiency Syndromes; Leukemia, Myeloid; Muramidase; Nephrosis; Pleura; Pleurisy

In pleural biopsy specimens and histological sections from the fibrin clots of pleural fluid aspirates it may be difficult to distinguish reactive mesothelial cells from malignant mesothelial cells and metastatic carcinoma. Reactive pleurisy with effusion is usually associated with loss of cohesion and exfoliation of mesothelial cells, which is consistent with the hypothesis that they act as facultative histiocytes. A series of biopsy specimens and sections of clots from benign and malignant pleural effusions have been stained by the immunoperoxidase technique for the histiocytic markers alpha 1-antitrypsin, alpha 1-antichymotrypsin, and lysozyme (muramidase). Eight cases of mesothelioma were included. Mesothelial cells when seen as a monolayer lining the pleural surface were negative. Reactive mesothelial cells, usually seen as exfoliated cells, were consistently strongly positive for alpha 1-antichymotrypsin and more variably for alpha 1-antitrypsin and lysozyme. Malignant cells, whether from carcinoma or from mesothelioma, were usually but not always negative. Consequently immunohistochemical staining for alpha 1-antichymotrypsin is often helpful in distinguishing reactive mesothelial cells from malignant cells.

Topics: alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Biopsy; Biopsy, Needle; Chymotrypsin; Humans; Immunoenzyme Techniques; Mesothelioma; Muramidase; Pleura; Pleural Effusion; Pleural Neoplasms; Pleurisy

Topics: Adolescent; Adult; Aged; Diagnosis, Differential; Female; Humans; Lung Neoplasms; Male; Middle Aged; Muramidase; Pleural Effusion; Pleurisy; Pneumonia; Tuberculosis, Pulmonary

Lysozyme content was measured in the plasma and pleural fluid of 110 patients with pleural effusions of various causes. The concentration of pleural fluid lysozyme was significantly higher (P less than .001) in patients with tuberculous pleurisy than in those with primary pulmonary carcinoma, metastatic carcinoma of the lung, connective tissue disease, nonspecific pleurisy, or congestive heart failure. Tuberculous patients also had a significantly higher (P less than .001) pleural fluid-to-plasma lysozyme ratio than did the other patients. Plasma lysozyme activity did not differ significantly among the various patient groups. Lysozyme was identified immunohistochemically in epithelioid cell granulomas in tuberculosis, in activated macrophages in lymph nodes adjacent to tuberculous lesions, and in granulocytes in pleural empyema. No lysozyme was detected in neoplastic cells in pulmonary carcinoma. The results show that the determination of pleural fluid lysozyme is a simple, fast method for obtaining corroborative information in the differential diagnosis of tuberculous pleurisy.

Topics: Adolescent; Adult; Clinical Enzyme Tests; Diagnosis, Differential; Female; Humans; Male; Middle Aged; Muramidase; Pleural Diseases; Pleural Effusion; Pleurisy; Tuberculosis, Pleural

Topics: Humans; Muramidase; Pleural Effusion; Pleurisy; Tuberculosis, Pleural