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.

Absence of Protein Changes in "Old" Worms

G. McCaffrey, T.E. Johnson

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 
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.