THIOREDOXIN-LINKED PLANT AND ANIMAL PROCESSES - THE NEW-GENERATION

The renaissance in the study of thioredoxin in heterotrophic cells tha t began just prior to this decade has provided new insight into the fu nction and significance of this ubiquitous regulatory disulfide protei n. Thioredoxin, reduced enzymically with NADPH via NADP-thioredoxin re ductase, has been found to regulate a range of biochemical processes i n plants as well as animals. In so doing, thioredoxin targets intramol ecular disulfide bonds of proteins such as enzyme inhibitors, seed sto rage proteins and enzymes. As may be seen, the target proteins have no t been identified for a number of thioredoxin functions uncovered in c omplex systems, such as those involving transcription factors or gene inactivation. In a series of ongoing studies stemming from the fundame ntal work, thioredoxin has emerged as a new tool in technology and med icine. It now seems clear that we stand at a frontier in which the rap idly expanding knowledge of thioredoxin will lead to applications in i ndustry and health.