期刊
PEPTIDES
卷 29, 期 6, 页码 904-911出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2008.02.001
关键词
ghrelin structure; ghrelin phosphorylation; peptide-membrane binding; PKC substrate
资金
- NIDDK NIH HHS [R01 DK076037] Funding Source: Medline
- NIGMS NIH HHS [R01 GM031184, GM31184, R01 GM031184-21] Funding Source: Medline
The peptide hormone ghrelin requires Ser-3 acylation for receptor binding, orexigenic and anti-inflammatory effects. Functions of desacylghrelin are less well understood. In vitro kinase assays reveal that the evolutionarily conserved Ser-18 in the basic C-terminus is an excellent substrate for protein kinase C. Circular dichroism reveals that desacylghrelin is similar to 12% helical in aqueous solution and similar to 50% helical in trifluoroethanol. Ser-18-phosphorylation, Ser-18-Ala substitution, or Ser-3-acylation reduces the helical character in trifluoroethanol to similar to 24%. Both ghrelin and desacylghrelin bind to phosphatidylcholine:phosphatidylserine sucrose-loaded vesicles in a phosphatidylserine-dependent manner. Phosphoghrelin and phosphodesacylghrelin show greatly diminished phosphatidylserine-dependent binding. These results are consistent with binding of ghrelin and desacylghrelin to acidic lipids via the basic face of an amphipathic helix with Ser-18 phosphorylation disrupting both helical character and membrane binding. (C) 2008 Elsevier Inc. All rights reserved.
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