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5132092 
Journal Article 
Review 
Glucuronide Conjugation in the Lung 
Aitio, A 
1976 
1 
Agents and Actions
ISSN: 0065-4299 
6 
4 
531-533 
English 
60876 
WOS:A1976BY33400069 
A review of literature on the biotransformation of agents by the lungs is presented. Several recent studies have confirmed the existence of a low level of the enzyme, uridine-diphosphate-glucuronosyltransferase (UDPGT), in the lungs of laboratory animals. UDPGT activity towards a number of agents has been detected in the lungs. The activity of UDPGT in the lungs has been found to be only one third that of the hepatic enzyme. The response of the pulmonary UDPGT to various treatments of the microsomes is distinctly different from that of the liver. The pulmonary enzyme more closely resembles that of the gastrointestinal tract mucosa and of the placenta. The UDPGT of the lung, like that of the liver, kidney and gastrointestinal mucosa, can be induced by such agents as those listed: cinchophen (132605), 3,4-benzpyrene (50328) and 3-methylcholanthrene (56495); phenobarbital (50066) fails to cause induction of pulmonary UDPGT. The lungs also contain a high activity of beta-glucuronidase, which could significantly alter the measured UDPGT activity. The authors conclude that the effect of the pulmonary glucuronide synthesis on the overall pharmacokinetics of drugs and toxins is probably minimal, but has significance when small amounts of toxins enter the body via the lungs, or when they are accumulated in the lungs.