1 Biochemical changes in male, Wistar rats, treated with different doses of 1,2-dichloropropane (50-500 mg kg-1 body weight), were investigated at the end of a 4-week treatment and after a 4-week recovery period.
2 The behaviour of Phase I and Phase II metabolic steps and of the angiotensin converting enzyme activity of the renal proximal tubule brush border were determined.
3 Phase II is more affected by the solvent than Phase I metabolism, and liver metabolism is more affected than the kidney.
4 Angiotensin converting enzyme activity from the proximal tubule brush border appears to be the most sensitive parameter of kidney involvement during treatment.
5 After a 4-week recovery period all the metabolic indices together with angiotensin converting enzyme activity have returned to normal. Only liver reduced glutathione content shows a slight, but significant, increase for the highest dose (500 mg kg -1 body weight).
6 The results show that the biochemical changes induced in liver and kidney by 1,2-dichloropropane are reversible.
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References
1.
' Trevisan A., Rizzi E., Scapinello A., Gioffré F. & Chiesura P.Liver toxicity due to 1,2-dichloropropane in the rat. Archives of Toxicology1989; 63: 445-9.
2.
Highman B. & Heppel LAToxicology of 1,2-dichloropropane (propylene dichloride). III. Pathologic changes produced by a short series of daily exposures. Archives ofPathology1946; 42: 525-34.
3.
Bruckner JV, MacKenzie WF, Ramanathan R. et al. Oral toxicity of 1,2-dichloropropane: acute, short-term, and long-term studies in rats. Fundamental and Applied Toxicology1989; 12: 713-30.
4.
Trevisan A., Rizzi E., Bungaro A. et al. Proximal tubule brush border angiotensin converting enzyme behaviour and nephrotoxicity due to 1,2-dichloropropane. Archives of Toxicology1988: suppl. 12: 190-2.
5.
Sedlak J. & Lindsay RHEstimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Analytical Biochemistry1969; 25: 192-205.
6.
Habig WH, Pabst MJ & Jacoby WBGlutathione S-transferases. The first enzymatic step in mercapturic acid formation . The Journal of Biological Chemistry1974 ; 249: 7130-9.
7.
Imai Y., Ito A. & Sato R.Evidence for biochemically different types of vesicles in the hepatic microsomal fraction. The Journal of Biochemistry1966 ; 60: 417-28.
8.
McLean Aem & Day PAThe use of new methods to measure: the effect of diet and inducers of microsomal enzyme synthesis on cytochrome P450 in liver homogenates, and on metabolism of dimethyl nitrosamine. Biochemical Pharmacology1974; 23: 1173-80.
9.
Omura T. & Sato R.The carbon monoxide binding pigment of liver microsomes. The Journal of Biological Chemistry1964; 239: 2370-8.
10.
Booth AG & Kenny AJA rapid method for the preparation of microvilli from rabbit kidney. The Biochemical Journal1974; 142: 575-81.
11.
Summary JJThe spectrophotometric determination of human serum carboxypolypeptidase with angiotensin converting enzyme-like activity. Clinical Science and Molecular Medicine1976; 50: 321-7.
12.
Miller GLProtein determination for large numbers of samples. Analytical Chemistry1959; 31: 964.
