期刊
JOURNAL OF NEUROCHEMISTRY
卷 141, 期 3, 页码 330-340出版社
WILEY
DOI: 10.1111/jnc.13993
关键词
active prodomains; biosynthetic pathway; pBDNF; precursor cleavage peptides; proBDNF; Val66Met polymorphism
资金
- International Society for Neurochemistry (ISN)
- International Brain Research Organization (IBRO) Return Home Fellowships
- Brain & Behavior Research Foundation
- Argentinean Ministry of Science and Technology (MINCyT)
- Committee for Aid and Education in Neurochemistry (CAEN) Return Home Award
Most growth factors and hormones are synthesized as pre-pro-proteins which are processed to the biologically active mature protein. The pre- and prodomains are cleaved from the precursor protein in the secretory pathway or, in some cases, extracellularly. The canonical functions of these prodomains are to assist in folding and stabilization of the mature domain, to direct intra and extracellular localization, to facilitate storage, and to regulate bioavailability of their mature counterpart. Recently, exciting evidence has revealed that prodomains of certain growth factors, after cleaved from the precursor pro-protein, can act as independent active signaling molecules. In this review, we discuss the various classical functions of prodomains, and the biological consequences of these pro-peptides acting as ligands. We will focus our attention on the brain-derived neurotrophic factor prodomain (pBDNF), which has been recently described as a novel secreted ligand influencing neuronal morphology and physiology.
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