PROTEOLYTIC ACTIVITY OF 26S PROTEASOMES ISOLATED FROM MUSCLES OF THE TOBACCO HORNWORM, MANDUCA SEXTA: DIFFERENCES BETWEEN SURVIVING MUSCLES AND THOSE UNDERGOING DEVELOPMENTALLY PROGRAMMED CELL DEATH

Reynolds, S. E. and Löw, P. and Sass, M. (2001) PROTEOLYTIC ACTIVITY OF 26S PROTEASOMES ISOLATED FROM MUSCLES OF THE TOBACCO HORNWORM, MANDUCA SEXTA: DIFFERENCES BETWEEN SURVIVING MUSCLES AND THOSE UNDERGOING DEVELOPMENTALLY PROGRAMMED CELL DEATH. Acta Biologica Hungarica, 52 (4). pp. 435-442. ISSN 0236-5383

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Abstract

The intersegmental muscles (ISMs) of tobacco hornworm, Manduca sexta are a well-characterised model system for examining the biochemical changes that accompany programmed cell death during develop- ment. When the ISMs become committed to die, there are dramatic increases in both the ubiquitin- expression, and ubiquitin-dependent proteolysis. Since the 26S proteasome is responsible for ATP/ubiq- uitin-dependent proteolysis in cells, we examined its enzymatic properties. Specific chymotrypsin-like proteolytic activity of 26S proteasomes isolated from ISM is four times higher than that of surviving flight muscle (FM). However, specific activity does not change between developmental stages within ISM or FM. The difference between proteolytic capacity of the two kinds of muscles is even higher when the ISM become committed to die because 26S proteasome content of ISM increases just before cell death. These observations underline the role of 26S proteasome in programmed cell death.

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