1982
DOI: 10.1073/pnas.79.8.2451
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Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation.

Abstract: Cathepsin M, which catalyzes inactivation of both rabbit liver fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) and rabbit liver fructose 1,6-bisphosphatase (Fru-P2ase; EC 3.1.3.11), has been characterized as a peptidyl peptidase. Modification of the COOH terminus of aldolase by cathepsin M or by Fru-P2ase converting enzyme 2 abolishes its ability to bind to phosphocellulose P11 and to form the complex with Fru-P2ase. On the other hand, modification ofthe COOH terminus of Fru-P2ase does not affect its interact… Show more

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Cited by 8 publications
(4 citation statements)
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“…It is presumed that the transition from the disengaged to the engaged state of the loop causes a development of a relatively homogeneous, positively charged cavity in the central region of an FBPase tetramer, which may facilitate the interaction between FBPase and the negatively charged C-terminal region of the aldolase subunit (Figure 9). Such a mode of interaction between aldolase and FBPase seems to be supported by the discovery of a new allosteric pocket located near the center of FBPase (52), as well as by the finding that limited proteolysis of the COOH terminus of liver aldolase abolishes its ability to form the complex with liver FBPase (53).…”
Section: Discussionmentioning
confidence: 97%
“…It is presumed that the transition from the disengaged to the engaged state of the loop causes a development of a relatively homogeneous, positively charged cavity in the central region of an FBPase tetramer, which may facilitate the interaction between FBPase and the negatively charged C-terminal region of the aldolase subunit (Figure 9). Such a mode of interaction between aldolase and FBPase seems to be supported by the discovery of a new allosteric pocket located near the center of FBPase (52), as well as by the finding that limited proteolysis of the COOH terminus of liver aldolase abolishes its ability to form the complex with liver FBPase (53).…”
Section: Discussionmentioning
confidence: 97%
“…47,92,93 ALDOC proteolysis by calpain or cathepsin produces a 38 kD ALDOC fragment on later post-injury days. [94][95][96] In contrast, GFAP proteolysis by calpains or caspases produces massive enzymatic degradation into several fragments that are reported in CSF from patients with various neurodegenerative diseases. [97][98][99][100][101] Thus, our data show that protein-specific breakdown contributes to different temporal biomarker profiles.…”
Section: Astroglial Neurotrauma Biomarkers Have Kinetic Diversitymentioning
confidence: 99%
“…Aldolase was isolated from the liver homogenates (5) and assayed (6) as described. Digestion of the purified enzyme with subtilisin and analysis of the acid-soluble peptides for tyrosine was carried out with dialyzed solutions of the purified aldolase (4). For the evaluation of release of lysosomal proteinases, the rate of hydrolysis of benzoyl-L-arginyl-2-naphthylamide (BANA) was determined.…”
Section: Methodsmentioning
confidence: 99%
“…We now show that the loss of activity is due to proteolytic modification of the COOH terminus and provide evidence that this modification is not the result of proteolysis during the isolation ofthe enzyme from the homogenates. The loss ofpeptides from the COOH terminus can be attributed to the action ofa recently identified lysosomal proteinase, designated cathepsin M (3), which was shown to catalyze a similar modification ofrabbit liver aldolase in vitro (4). The present results, which establish that this modification occurs during fasting in vivo, also support the concept that in the living cell some lysosomal proteinases may be accessible to the cytosol, accounting for at -least partial proteolysis of cytosolic enzymes without their entry into the lysosomes.…”
mentioning
confidence: 99%