Title

Prohormone thiol protease' (PTP) a novel cysteine protein for proenkephalin and prohormone processing" in Proteolytic and cellular mechanisms in prohormone and proprotein processing

Editors

Vivian Y. Hook

Document Type

Chapter

Publication Date

1998

Publication Title

Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing

Publisher

R.G. Landes Company

Publisher Location

Austin, TX

Edition

1

First page number:

89

Last page number:

104

Abstract

Production of peptide hormones and neurotransmitters requires several steps which involves transcription of the pro-hormone gene, translation of the corresponding mRNA, packaging of the prohormone into secretory vesicles, processing by proteolytic mechanisms, storage of mature neuropeptides in secretory vesicles, and regulated secretion of bioactive peptides. Among these steps, posttranslational processing is required for converting the inactive protein precursor into biologically active neuropeptides. Clearly, limited proteolysis is crticical for generating neuropeptides. Endoproteases and extoproteases are required for prohormone processing, which occurs in the regulated secretory pathway of neuroendocrine cells. These potent neuropeptides are stored and secreted from secretory vesicles. The released peptide hormones and neurotransmitters mediate cell-cell communication in neuroendocrine systems.

Keywords

Messenger RNA; Neuropeptides; Peptide hormones; Peptide hormones/metabolism; Peptide hormones/physiological transport; Post-translational modification; Preotein precursors; Proteolytic enzymesl; Proprotein convertases; Proteins--Metabolism

Disciplines

Life Sciences | Medical Sciences | Medicine and Health Sciences

Language

English


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