期刊
PHARMACOLOGICAL RESEARCH
卷 83, 期 -, 页码 3-9出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phrs.2014.04.002
关键词
Pharmacological chaperone; Proteostasis; Chaperone; ERAD; Protein misfolding disease; Lysosomal storage disease; GPCR; Ion channel
资金
- Research Start-up Fund from Case Western Reserve University School of Medicine, Epilepsy Foundation of America [225243]
- Clinical Translational Science Collaborative of Cleveland CTSA from the National Center for Research Resources [UL1RR024989]
- National Center for Advancing Translational Sciences of the National Institutes of Health
- National Heart, Lung and Blood Institute [T32 HL007567]
Normal organismal physiology depends on the maintenance of proteostasis in each cellular compartment to achieve a delicate balance between protein synthesis, folding, trafficking, and degradation while minimizing misfolding and aggregation. Defective proteostasis leads to numerous protein misfolding diseases. Pharmacological chaperones are cell-permeant small molecules that promote the proper folding and trafficking of a protein via direct binding to that protein. They stabilize their target protein in a protein-pharmacological chaperone state, increasing the natively folded protein population that can effectively engage trafficking machinery for transport to the final destination for function. Here, as regards the application of pharmacological chaperones, we focus on their capability to promote the folding and trafficking of lysosomal enzymes, G protein coupled receptors (GPCRs), and ion channels, each of which is presently an important drug target. Pharmacological chaperones hold great promise as potential therapeutics to ameliorate a variety of protein misfolding diseases. (C) 2014 Elsevier Ltd. All rights reserved.
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