Worm Breeder's Gazette 7(1): 66
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
We have used pulse labelling and subsequent 2-D gel electrophoresis of newly labelled proteins to answer two questions about the spectrum of proteins synthesized at different times in the lifespan of the worm: Are there changes in the spectrum of proteins synthesized by old worms compared to those synthesized by young adults? Is there misincorporation of amino acids into newly synthesized proteins in old worms? No changes have been detected in the spectrum of proteins synthesized by old as compared to young worms. This finding is in contrast to previous findings (Johnson and Hirsh, 1979) of a large number of changes in the spectrum of proteins synthesized at various times during larval development. Therefore, by this criterion, there appear to be marked differences between the mechanisms operating in development and those that operate to cause aging. We also have found no evidence to suggest that there is an increase in translational errors in old worms. Such an increase might be expected if aging is primarily due to an 'error catastrophe event' somewhere in the information processing machinery of the worm. The generality of these findings is limited by the fact that only the 600-800 most prevalent proteins can be examined by this technique. Furthermore, old worms eat less than young worms, thus lowering the specific activity of the amino acid pool in old worms and consequently decreasing the sensitivity of the assay.