DIFFERENCES IN CATALYTIC ACTIVITIES AND SUBUNIT PATTERN OF MULTICATALYTIC PROTEINASE COMPLEXES (PROTEASOMES) ISOLATED FROM BOVINE PITUITARY, LUNG, AND LIVER - CHANGES IN LMP7 AND THE COMPONENT NECESSARY FOR EXPRESSION OF THE CHYMOTRYPSIN-LIKE ACTIVITY

被引:32
作者
CARDOZO, C
ELEUTERI, AM
ORLOWSKI, M
机构
[1] CUNY MT SINAI SCH MED,DEPT PHARMACOL,NEW YORK,NY 10029
[2] CUNY MT SINAI SCH MED,DEPT MED,NEW YORK,NY 10029
[3] UNIV CAMERINO,I-62032 CAMERINO,ITALY
关键词
D O I
10.1074/jbc.270.38.22645
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Polyacrylamide gel electrophoresis and high performance liquid chromatography of multicatalytic proteinase complexes (MPC) isolated from bovine pituitary, lung and liver showed marked differences in the pattern of subunits, The concentrations of LMP7 in the lung and liver were 10 and 5 times, respectively, greater than those in the pituitary, whereas the chymotrypsin-like activity and the amount of a subunit (BO2), necessary for its expression, were markedly decreased in the lung and moderately decreased in the liver, Lower trypsinlike, small neutral amino acid preferring, and peptidyl-glutamyl-peptide hydrolyzing activities were also found in the lung and liver. The activity of the branched chain amino acid preferring component (BrAAP), predominantly latent in the pituitary, was highly activated in the lung and liver, as evidenced by a greatly decreased IT, and a 20-fold increase of the specificity constant V-max/K-m, indicating facilitated substrate access to its active site and increased affinity toward substrates with branched chain amino acids in the P-1 position, It is suggested that overexpression of LMP7 in the lung is related to increased exposure of the airways to foreign antigens, The possible association between amounts of LMP7 and the activation of the BrAAP component needs further examination.
引用
收藏
页码:22645 / 22651
页数:7
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