Impact of experimental diabetes on phenylalanine hydroxylase expression in rat liver

Abstract

627th MEETING, NOTTINGHAM 1057 activation is lower than that found in lysosomes (Ohkuma & Poole, 1978) our results suggest that the activation in vivo may depend on components or structures that induce conformational changes at less acidic pH values. This may involve membrane interactions since hydrophilic/hydrophobic interactions appear to be important. Internal cleavages in the precursor must occur after transport to the lysosome since no change in M , was observed after reduction with dithiothreitol. The K , and k,,, values obtained for the degradation of Z-Phe-Arg-7-(4-methyI)coumarylamide (NHMec) of the activated precursors suggest that cathepsin L may be potentially more active in vivo than in vitro. The glycosyl residues did not alter the conditions required for activation and only slightly altered the kinetic parameters.

The effect of streptozotocin-induced diabetes on phenylalanine hydroxylase expression in rat liver

“…The present paper seeks to clarify the mechanisms underlying the changes in phenylalanine hydroxylase expression which occur after the onset of streptozotocininduced diabetes in rats. Portions of this work have appeared in preliminary form (Taylor et al, 1988).…”