The induction of apoptosis in thymocytes by the glucocorticoid dexamethasone was used as a model system to investigate whether there are changes in 20 S and 26 S proteasome activities during apoptosis. We observed that thymocytes contain high concentrations of proteasomes and that following treatment with dexamethasone, cell extracts showed a decrease in proteasome chymotrypsin-like activity which correlated with the degree of apoptosis observed. The decrease in chymotrypsin-like activity of 20 S and 26S proteasomes was still apparent after these complexes had been partially purified from apoptotic thymocyte extracts and was therefore not due to competition resulting from a general increase in protein turnover.
View Article and Find Full Text PDFLobster skeletal muscles contain four Ca2+-dependent cysteine proteinases (CDPs I, IIa, IIb, and III) that degrade myofibrillar proteins. Lobster CDPs share many properties with calpains from vertebrate tissues, but differ in native mass and subunit composition. Recently, cDNAs encoding a calpain-like protein (Dm-calpain; 91.
View Article and Find Full Text PDFBiochem Biophys Res Commun
March 1994
The presence of calcium-dependent proteinase in plants was investigated using soluble proteins from Arabidopsis root cultures. Calcium increased the proteolytic activity by two to three fold. Calcium-stimulated proteolytic activity was inhibited by different protease inhibitors.
View Article and Find Full Text PDFMulticatalytic proteinase (MCP) is thought to play a central role in the processing and turnover of intracellular proteins in eukaryotic cells. Immunocytochemistry was used to determine the intracellular distribution of the MCP in the claw muscles of the land crab, Gecarcinus lateralis, and the claw and abdominal muscles of the American lobster, Homarus americanus. Cryosections were stained with an affinity-purified polyclonal antibody to lobster MCP that cross-reacted with the land crab enzyme.
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