Nov 28, 1988 - A transudate occurs when the mechanical factors influencing the forma- tion or reabsorption of pleural fluid are altered. The pleural surfaces ...
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BIOCHEMICAL SOCIETY TRANSACTIONS
in tension ( < 10% of the carbachol-induced contraction over this concentration range). Exogenous NKA in the concentra~ dose-related tracheal tion range lo-’ to 1 0 - 7 . induced contraction up to 80% of the carbachol-induced response. In the presence of peptide 4 ( M), contractions were significantb’ reducedl(Fig. 1. The mechanism Of this antagonism is as yet unclear and is under investigation. This study was funded by a grant from the N. Ireland Chest, Heart and Stroke Association.
Barnes, P. J. (1987)Am. Rev. Respir. Dis. 136, S77-S83 Kaiser, E. T., Colescott, R. L., Bossinger, C. D. & Cook, P. I. ( 1970) Biochem.
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595-598
Quirion, R. & Dam, T. V. ( 1 988) Re@. Peprides 22, 18-25
w, & Merrifie,d, R, B, (1983) Am, Chem, 6442-6455 Williams, B. J., Curtis, N. R., McKnight, A. T., Foster, A. & Tridget, R. ( 1988) Regul. Peprides 22, 189
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Received 28 November 1988
Determination of creatine kinase levels in pleural effusions SEDEF YENICE, GUL GUNER, MAKBULE GIN and ATILLA AKKOCLU Departments of Biochemistry and Chest Medicine, Dokut Eyliil University Faculty of Medicine, Izmir, Turkey Pleural effusions frequently cause diagnostic problems. A correct diagnosis of the underlying disease is essential to rational management. Despite employment of extensive diagnostic procedures, the cause remains elusive in 10-20% of all cases (Storey et al., 1976; Hirsch et al., 1979; Wordmann et al., 1984). A primary step in the diagnosis of pleural effusions is their classification as ‘transudates’ or ‘exudates’. A transudate occurs when the mechanical factors influencing the formation or reabsorption of pleural fluid are altered. The pleural surfaces are thought not to be involved in the primary pathological process (Agostini et al., 1957; Stead & Sproul, 1964). In contrast, an exudate results from inflammation or other disease of the pleural surface (such as tuberculosis, pneumonia with effusion, malignancy, pancreatitis, pulmonary infarction, or systemic lupus erythematosis). Pleural fluid protein levels (Hirsch e f al., 1979) and more recently lactate dehydrogenase (LDH) levels (Chanrasekhar et al., 1969) have been used to distinguish exudates and transudates. However, these parameters have consistently led to the misclassification of some effusions (Carr & Power, 1958; Light et al., 1972). Creatine kinase ( E C 2.7.3.2; CK) is an enzyme catalysing the reversible phosphorylation of creatine by ATP. Increased CK activity has been reported in serum or in cerebrospinal fluid CSF in a variety of pathologies, including primary or metastatic tumors (Kjeldsberg & .Krieg, 1984). However, no data have been found in the scientific literature concerning the activity of this enzyme in pleural effusions. This study was undertaken to assess the value of determining the level of creatine kinase in pleural effusions with different aetiology and to compare these results with those obtained with LDH and total protein levels. As the most frequent causes of pleural effusions are reported as ‘cancer’ and ‘tuberculous infection’, effusions due to these principal causes were investigated, along with transudates resulting from mechanical factors (Gunnels, 1978). This investigation was carried out on 74 patients admitted to the Department of Chest Medicine, Dokuz Eylul University Faculty of Medicine between September 1987 and August 1988. They were divided into three diagnostic groups: congestive heart failure, malignant disorders, and tuberculous pleurisy. The diagnostic laboratory tests performed were: pleural fluid pH, specific gravity, cell count, glucose concentration. cytological and bacteriological examination, including smear
and culture for Mycobacterium tuberculosis, serum and pleural fluid total protein, and LDH levels. When these tests did not establish the diagnosis, a thoracoscopy was performed and multiple pleural biopsies were taken for histological and bacteriological examination. Creatine kinase activity was measured at 340 nm using the method of Oliver (1955) and Rosalki (1967) (see The Committee on Enzymes of the Scandinavian Society for Clinical Chemistry and Clinical Physiology, 1979). Lactate dehydrogenase ( E C 1.I.1.27; LDH) levels were determined using L-lactate as substrate and NAD as coenzyme and by measuring the increase in absorbance at 340 nm. They were expressed in international units (i.u.) (Technicon kit) (Morgenstern et al., 1973). Total proteins were assayed using the Biuret method and results are given in g/dl (Bauer et al., 1968). All tests were performed by using Technicon RA1000 autoanalyser. The results of the different diagnostic groups were compared using the Student’s t-test. The total protein, LDH, and CK levels measured in sera and pleural fluids of the three diagnostic groups are represented in Table 1. Compared with the transudates, the mean CK activities in pleural fluids of the patients with malignant effusions and tuberculous pleurisy were found to be significantly higher ( P < 0.05). The mean serum CK activity in malignant effusions was determined to be significantly higher ( P C/inica/ Laboratory Methods, pp. 320-322,l h e C.V. Mosby Company, Saint Louis Carr, D. T. & Power, M. H. (1958)N. Engl. J . Med. 259.926-927 Chanrasekhar. A. J., Palatao, A,. Dubin, A. & Levine. H. (1969) Arch. Intern. Med. 128,48-50 Gunnels, J. J. ( 1 978)Chest 74,390 Hamm, H.,Brohan, M. D.. Bohmer. R. & Missmahl. H. P. ( 1 987) Chest 2,296-302 Hirsch, A., Ruffie, P., Nebut, M., Bignon, J. & Chretien, J./ ( 1 979) Thorax 34,106-112 Kjeldsberg, C. R. & Krieg, A. F. (1984)in Clinicul Diagnosis and Management by Laboratory Methods (Henry, J. B., ed.), pp. 473, W. B. Saunders Company, Philadelphia, London, Toronto, Mexico City, Rio de Janeiro, Sydney, Tokyo Light, R. W., Macgregor, M. I., Luchsinger, P. C. & Ball, W. C. ( 1 972) Ann. Int. Med. 77,507-513 Morgenstern, S., Rush, R. & Lehman, D. ( 1 973) in Advances in Automated Analysis, 1972 ltiternutionul C’ongress, p p . 27-3 I , Mediat. Inc., Tarrytown. New York Oliver,I.T.(1955)Biochern. J . 61,116-122 Rosalki, S.B. ( 1 967)J . Lab. C‘lin. Med. 69,695-705 The Committee on Enzymes of the Scandinavian Society for Clinical Chemistry and Clinical Physiology, ( 1979) Scund. J . Clin. Lab. Invest. 39,( 1 - 5 ) . Stead, W. W. & Sproul, J. M. ( 1964)DM. July, 1-48 Storey, D. D., Dines, D. E. & Coles, D. T. ( 1 976) JAMA 236,
2 183-2186 Wordmann, A. G., Bowen, M., Struthers, L. P. L., Cooke. N. J. ( I 984)Med. Pediatr. Oticol. 12,68-72
Received 22 December 1988
Effect of interferon inducers on carbon tetrachloride toxicity in congenic strains of mice MAHTA JAHANSHAHI and NlGEL J. GOODERHAM* Department of c‘litiicul I’hurtnucolo~y,R o y l I’osrgrudirute Medical School, Dir Curie Road, Lotidon WIZ ONN, U . K . Renton & Mannering (1976) reported that treatment of animals with interferon inducers depresses hepatic cytochrome P450-mediated drug metabolism, and that some cytochrome P-450 isoenzymes are depressed more than others. Recently, we demonstrated that the interferon inducer, polyriboinosinic acid. polyribocytidylic acid [poly(l).poly(C)],protects male Swiss Webster mice from the hepatotoxic effects of carbon tetrachloride. We proposed that the mechanism of this protection was depression of the levels of cytochrome 1’-450 isoenzymes which activate carbon tetrachloride to its toxic metabolites (Freeman et ul., 1988). Four genetic loci which influence the induction of interferon have been found in inbred strains of mice (DeMaeyer & DeMaeyer-Guignard, 1979). C,H/He and C,H/HeJ are congenic strains of mice, the C,H/HeJ strain Abbreviations used: poly( l).poly(C). polyriboinosinic acid-polyribocytidylic acid; LPS, lipopolysaccharide. *To whom correspondence should be addressed
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carrying the recessive allele for the production o f interferon at the interferon-1 locus. C,H/He is susceptible to the effects of lipopolysaccharide (LPS), whereas C,HeJ are resistant. One response to LPS is induction of interferon via the interferon-1 locus; thus this compound only induces interferon in the C,H/He strain. In contrast to LPS, poly(I).poly(C)produces interferon in both strains of mice by inducing through loci other than interferon-1 (Singh & Renton, 1981). We have attempted to investigate whether the single interferon gene locus difference between the two strains confers differing susceptibility to the hepatotoxicity of carbon tetrachloride, after treatment with poly(l).poly(C)or LPS. At the onset we postulated that treatment o f mice with either poly(l).poly(C)or LPS would depress cytochrome 1’-450mediated metabolism in the C,H/He strain, and thus may provide protection against the hepatotoxin carbon tetrachloride. Since C,H/HeJ mice are LPS non-responders, it seemed likely that LPS treatment would not lower hepatic cytochrome 11-450-mediated drug metabolism in this strain and therefore may not protect against carbon tetrachloride he patotoxicity. Male C,H/He and C,H/HeJ mice were injected with intraperitoneal doses o f either saline (0.9% w.v, NaCI).
