Developmental Regulation of Proteolytic Activities and Subunit Pattern of 20 S Proteasome in Chick Embryonic Muscle

J Y Ahn, S O Hong, K B Kwak, S S Kang, K Tanaka, A Ichihara, D B Ha, C H Chung

J Biol Chem. 1991 Aug 25;266(24):15746-9.

PMID: 1874733

Abstract:

The proteolytic activities of the 20 S proteasome were found to change in their levels during the development of chick embryonic muscle. The peptide-cleaving activities against N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and N-benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide gradually decreased with the time of development. On the other hand, the casein-degrading activity in the presence of poly-L-lysine markedly increased from embryonic day 11 and reached a maximal level by day 17. These changes appeared to be tissue-specific because little or no change in any of the proteolytic activities was observed with developing embryonic brain, while dramatic alterations occurred in the extents of the peptide hydrolyses in liver. Furthermore, a number, but not all, of the proteasome subunits in embryonic muscle were changed in their amounts during the development. These results suggest that the alterations in the proteasome activities and subunit pattern are developmentally regulated and may be correlated.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP94367212	N-Succinyl-Leu-Leu-Val-Tyr-7-Amido-4-Methylcoumarin		94367-21-2	Price