Cellular control of ornithine decarboxylase activity by its antizyme

✍ Scribed by John S. Heller; Evangelos S. Canellakis

• Publisher: John Wiley and Sons
• Year: 1981
• Tongue: English
• Weight: 702 KB
• Volume: 107
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041070206

✦ Synopsis

Abstract

Conditions have been established under which the antizyme of ornithine decarboxylase (E.C. 4.1.1.17, L‐ornithine carboxy‐lyase, ODC) a noncompetitive protein inhibitor of ODC, can be detected in cells in response to as little as 10^−7^ M putrescine. The maintenance of intracellular antizyme activity depends upon the continued presence of putrescine in the medium. Removal of putrescine results in a rapid decline of antizyme activity. These phenomena are unaffected by the presence of cycloheximide and are comparable to the requirement of L‐asparagine for the maintenance of ODC activity.

The extent to which the antizyme level is increased is inversely related to the preexisting level of intracellular ODC at the time of addition of putrescine. The time of appearance of free antizyme is delayed in cells that have high levels of ODC; the amount of free antizyme that can be assayed for in these cells, at any particular time is correspondingly less. The converse is also true. In cells that have high levels of antizyme, the delay in appearance of ODC is greater and the amount of ODC that can be assayed for is correspondingly less than in cells with low levels of antizyme.

These experiments, as well as others, indicate that the ODC antizyme and ODC interact in vitro with each other to modify their respective activities.