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Neurotensin is an extremely potent inhibitor of protein degradation within the endoplasmic reticulum. The mechanism by which this process is inhibited is not known. The goal of this investigation was to identify the protein degradation pathway targeted by neurotensin. As a first step, we determined whether neurotensin also inhibits degradation of a non-endoplasmic reticulum-related substrate. V5-fusion proteins were expressed in Chinese hamster ovary cells and then the degradation of the proteins in the presence or absence of neurotensin (5-10 microM) was measured using a cycloheximide chase. The V5-protein fusions were either constructed in a mammalian expression vector driven by the constitutive cytomegalovirus promoter, or in the 5’UTR of a baculovirus vector. We found that neurotensin had no effect on the degradation of either the cytomegalovirus- or baculovirus-expressed proteins. We next determined whether a known component of the ubiquitin-proteasome pathway is involved in neurotensin-mediated inhibition of protein degradation. Activation of the proteasome by treating myocytes with proteasome inhibitors was not sufficient to suppress the effects of neurotensin on the degradation of V5-protein fusion. Further, we treated myocytes with proteasome inhibitors and then measured degradation of non-endoplasmic retic
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