Prohormone thiol protease' (PTP) a novel cysteine protein for proenkephalin and prohormone processing" in Proteolytic and cellular mechanisms in prohormone and proprotein processing
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.
Messenger RNA; Neuropeptides; Peptide hormones; Peptide hormones/metabolism; Peptide hormones/physiological transport; Post-translational modification; Preotein precursors; Proteolytic enzymesl; Proprotein convertases; Proteins--Metabolism
Life Sciences | Medical Sciences | Medicine and Health Sciences
Hook, V. Y.,
Schiller, M. R.,
Johnston, J. M.,
Prohormone thiol protease' (PTP) a novel cysteine protein for proenkephalin and prohormone processing" in Proteolytic and cellular mechanisms in prohormone and proprotein processing. In Vivian Y. Hook,
Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing
Austin, TX: R.G. Landes Company.