Characterization of mitochondrial neutral protease activity and the response of lysosomal enzymes to clofibrate feeding in rat liver

Manjunath, CK and Padmanaban, G and Cama, HR (1979) Characterization of mitochondrial neutral protease activity and the response of lysosomal enzymes to clofibrate feeding in rat liver. In: Biochemical Pharmacology, 28 (19). pp. 2929-2934.

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Abstract

The phosphate-inhibitable neutral protease activity of the heavy mitochondrial fraction of rat liver is of lysosomal origin. The activity is essentially due to the thiol proteinases of the lysosomes. Digitonin treatment of the mitochondrial fraction results in the release of about 85 per cent of the neutral protease activity and the residual activity has an alkaline pH optimum and is not inhibited by phosphate. Clofibrate feeding at 0.5 per cent level in the diet results in enhanced levels of lysosomal enzymes. The increase is however restricted to the lysosome-rich fraction such that the activities associated with the heavy mitochondrial fraction show a significant decrease. It is suggested that clofibrate inhibits engulfment of mitochondria by lysosomes and this results in enhanced mitochondrial protein content.

Item Type:	Journal Article
Publication:	Biochemical Pharmacology
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	23 Sep 2010 09:48
Last Modified:	23 Sep 2010 09:48
URI:	http://eprints.iisc.ac.in/id/eprint/32399

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