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Purification and Characterization of an Endogenous Inhibitor Specific to the Z-Leu-Leu-Leu-MCA Degrading Activity in Proteasome and Its Identification as Heat-Shock Protein 90

Purification and Characterization of an Endogenous Inhibitor Specific to the Z-Leu-Leu-Leu-MCA Degrading Activity in Proteasome and Its Identification as Heat-Shock Protein 90

S Tsubuki, Y Saito, S Kawashima

FEBS Lett. 1994 May 16;344(2-3):229-33.

PMID: 8187890

Abstract:

We previously identified a benzyloxycarbonyl(Z)-Leu-Leu-Leu-4-methylcoumaryl-7-amide (ZLLL-MCA) degrading activity in proteasome as a candidate for the regulator of neurite outgrowth. As its counterpart, we purified a protein from bovine brain that specifically inhibits the ZLLL-MCA degrading activity in proteasome. This protein is heat stable and has no effect on the other catalytic activities in proteasome, or on the activities of trypsin, chymotrypsin, or m- and mu-calpains either. The molar ratio of inhibitor-to-proteasome that inhibits 50% of the ZLLL-MCA degrading activity of proteasome is 1:1. The inhibitory mechanism of the inhibitor against proteasome is non-competitive. Finally, the inhibitor was identified as heat-shock protein 90 (HSP90) by partial amino acid sequencing and immunodetection. The results suggest that HSP90 initiates neurite outgrowth through the inhibition of the ZLLL-MCA degrading activity in proteasome.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241043	Heat Shock Protein 90 from bovine brain			Price

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