PMID: 8602725Mar 22, 1996Paper

Proenkephalin-processing enzymes in chromaffin granules: model for neuropeptide biosynthesis

Annals of the New York Academy of Sciences
Vivian HookN Tezapsidis

Abstract

Our discovery of precursor preference of processing enzymes indicates possible development of future drugs that target specific proteases uniquely associated associated with processing of a particular prohormone. For example, selective processing of PE by the PTP suggests that future evaluation of modulation of PTP through central nervous system drug reagents may modify the endogenous analgesic effects of the enkephalins. With respect to blood pressure, neuropeptide Y (NPY) that is released from sympathetic nerve terminals is a strong vasoconstrictor. Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests that investigation of inhibitors of peripheral PTP in blood pressure regulation should be initiated. Overall, elucidation of the proteolytic components required in prohormone processing will provide insights into the molecular mechanisms of human disease.

References

Mar 16, 1990·Biochemical and Biophysical Research Communications·V Y HookH U Affolter
Jan 1, 1990·Methods in Enzymology·F W StudierJ W Dubendorff
Mar 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·R S FullerJ Thorner
Jan 1, 1982·Annual Review of Physiology·K Docherty, D F Steiner
Dec 1, 1994·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·V Y HookN Tezapsidis

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