Antizyme Activation in Chemotherapy and Chemoprevention
Abstract
Antizyme is a small, labile protein important in the regulation of polyamines and a likely candidate to mediate polyamine depletion as cancer therapy. Once thought of as a single protein, antizyme has been found to actually consist of at least four different forms in cells. These forms are distinct in their molecular weight, stability and response to osmotic stress. To determine what forms originate from the first start site of AZ-1 and what post-translational modifications occur, Antizyme constructs with the second start site mutated were made and transfected into rat hepatoma (HTC) and Chinese hamster ovary (CHO) cells. Western blot analysis showed that the mutated antizyme gene, when expressed in cells, produces two proteins distinct in molecular weight. Only one band was expected, and when expressed in a cell-free system only one band was seen. The second, smaller band found in cells can only be explained by post-translational modification. These forms of antizyme behave as native antizyme with respect to activity in binding to and inhibiting ODC as well as cellular localization based on cellular fractionation experiments. These results suggests that native antizyme is post-translationally modified and this modification may play a role in the regulation of antizyme activity.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 2002
- Accession Number
- ADA405302
Entities
People
- Sandra L. Moore
Organizations
- Northern Illinois University