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A peptide derived from G0/G1 switch gene 2 acts as noncompetitive inhibitor of adipose triglyceride lipase.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2014 Nov 21; Vol. 289 (47), pp. 32559-70. Date of Electronic Publication: 2014 Sep 25. - Publication Year :
- 2014
-
Abstract
- The protein G0/G1 switch gene 2 (G0S2) is a small basic protein that functions as an endogenous inhibitor of adipose triglyceride lipase (ATGL), a key enzyme in intracellular lipolysis. In this study, we identified a short sequence covering residues Lys-20 to Ala-52 in G0S2 that is still fully capable of inhibiting mouse and human ATGL. We found that a synthetic peptide corresponding to this region inhibits ATGL in a noncompetitive manner in the nanomolar range. This peptide is highly selective for ATGL and does not inhibit other lipases, including hormone-sensitive lipase, monoacylglycerol lipase, lipoprotein lipase, and patatin domain-containing phospholipases 6 and 7. Because increased lipolysis is linked to the development of metabolic disorders, the inhibition of ATGL by G0S2-derived peptides may represent a novel therapeutic tool to modulate lipolysis.<br /> (© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.)
- Subjects :
- 1-Acylglycerol-3-Phosphate O-Acyltransferase antagonists & inhibitors
1-Acylglycerol-3-Phosphate O-Acyltransferase genetics
1-Acylglycerol-3-Phosphate O-Acyltransferase metabolism
Amino Acid Sequence
Animals
COS Cells
Cell Cycle Proteins chemistry
Cell Cycle Proteins genetics
Chlorocebus aethiops
Dose-Response Relationship, Drug
Humans
Lipase genetics
Lipase metabolism
Mice, Knockout
Molecular Sequence Data
Peptides genetics
Recombinant Proteins chemistry
Cell Cycle Proteins metabolism
Lipase antagonists & inhibitors
Peptides pharmacology
Recombinant Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 289
- Issue :
- 47
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 25258314
- Full Text :
- https://doi.org/10.1074/jbc.M114.602599