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

Manjunath, C. K. ; Padmanaban, G. ; Cama, H. R. (1979) Characterization of mitochondrial neutral protease activity and the response of lysosomal enzymes to clofibrate feeding in rat liver Biochemical Pharmacology, 28 (19). pp. 2929-2934. ISSN 0006-2952

Full text not available from this repository.

Official URL: http://www.sciencedirect.com/science/article/pii/0...

Related URL: http://dx.doi.org/10.1016/0006-2952(79)90588-4

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:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:91978
Deposited On:25 May 2012 13:54
Last Modified:25 May 2012 13:54

Repository Staff Only: item control page