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Biochem Biophys Res Commun. 1993 Nov 15;196(3):1195-201.

Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome.

Author information

1
Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.

Abstract

A tripeptide aldehyde protease inhibitor, benzyloxycarbonyl(Z)-Leu-Leu-leucinal (ZLLLa1), initiates neurite outgrowth in PC12 cells at an optimal concentration of 30nM. This result suggests the existence of a protease which regulates neurite formation in PC12 cells. We report here an attempt to identify this target protease in bovine brain using Z-Leu-Leu-Leu-4-methylcoumaryl-7-amide (ZLLL-MCA), in which the aldehyde moiety of ZLLLa1 was changed to 4-methylcoumaryl-7-amide to serve as a substrate for the protease. As a result, we have purified a proteasome with a molecular weight of about 660 kDa as a ZLLL-MCA degrading protease. The activity of the proteasome was inhibited efficiently by ZLLLa1, and was different from known catalytic activities of proteasome in some aspects, suggesting it to be a novel one. Thus, the proteasome may be involved in the regulation of neurite formation in PC12 cells.

PMID:
8250877
DOI:
10.1006/bbrc.1993.2378
[Indexed for MEDLINE]

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