Abstract
Biochemical analyses, employing HPLC and electrochemical detection, have shown that the mutation adl-1, which causes muscle defects, also induces a temperature-sensitive defect in catecholamine metabolism. The pool sizes of N-acetyldopamine (NADA) and N-beta-alanyldopamine (NBAD) in mutant adults incubated at 29 degrees attain only a fraction, dependent on the length of incubation, of those in mutants incubated at 22 degrees or in controls. The differences are more striking in relevant hemizygotes. Notably, dopamine is unaffected. Concomitant examination of behavior revealed a correlation between decreases in NADA and NBAD and decreases in locomotor function. That these observations suggest a requirement for catecholamine metabolism in muscle function is discussed.
