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Molecular Neurobiology pp 259–291Cite as

Specificity of Prohormone Processing

The Promise of Molecular Biology

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Part of the book series: Current Topics in Neurobiology ((CTNB))

Abstract

Cells that use peptides as intercellular messengers employ a biosynthetic strategy that differs substantially from the biosynthesis of other chemical messengers. Most neuropeptides are initially synthesized as larger precursor proteins (prohormones) that are cleaved enzymatically to produce the bioactive peptides. The primary structures of many prohormones have been established in recent years, largely due to the advent of recombinant DNA technique (for review, see Douglas et al., 1984). In many prohormones, two or more bioactive domains will overlap, with a potential proteolytic processing site occurring within the sequence of a bioactive peptide. Differential cleavage of such internal sites can give rise to peptides with marked differences in both potency at a particular receptor and/or selectivity for various receptors, yielding products with substantial differences in biological function. Thus, a fundamental question of neuropeptide biosynthesis concerns the control of the specificity of cleavage of the precursor.

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Authors and Affiliations

  1. Molecular Pharmacology Department, Albert Einstein College of Medicine, Bronx, New York, 10461, USA

    Lloyd D. Fricker

  2. Institute for Advanced Biomedical Research, The Oregon Health Sciences University, Portland, Oregon, 97201, USA

    Dane Liston, Mark Grimes & Edward Herbert

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  1. Lloyd D. Fricker
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  2. Dane Liston
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  3. Mark Grimes
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  4. Edward Herbert
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  1. The Salk Institute, San Diego, California, USA

    Steve Heinemann  & James Patrick  & 

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© 1987 Plenum Press, New York

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Fricker, L.D., Liston, D., Grimes, M., Herbert, E. (1987). Specificity of Prohormone Processing. In: Heinemann, S., Patrick, J. (eds) Molecular Neurobiology. Current Topics in Neurobiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7488-0_8

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