Characterization of the human patatin-like phospholipase family s⃞
Journal of Lipid Research, ISSN: 0022-2275, Vol: 47, Issue: 9, Page: 1940-1949
2006
- 237Citations
- 156Captures
- 9Mentions
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Metrics Details
- Citations237
- Citation Indexes237
- 237
- CrossRef197
- Captures156
- Readers156
- 156
- Mentions9
- References9
- Wikipedia9
Article Description
Several publications have described biological roles for human patatin-like phospholipases (PNPLAs) in the regulation of adipocyte differentiation. Here, we report on the characterization and expression profiling of 10 human PNPLAs. A variety of bioinformatics approaches were used to identify and characterize all PNPLAs encoded by the human genome. The genes described represent a divergent family, most with a highly conserved ortholog in several mammalian species. In silico characterization predicts that two of the genes function as integral membrane proteins and are regulated by cAMP/cGMP. A structurally guided protein alignment of the patatin-like domain identifies a number of conserved residues in all family members. Quantitative PCR was used to determine the expression profile of each family member. Affymetrix-based profiling of a human preadipocyte cell line identified several members that are differentially regulated during cell differentiation. Cumulative data suggest that patatin-like genes normally expressed at very low levels are induced in response to environmental signals. Given the observed conservation of the patatin fold and lipase motif in all human PNPLAs, a single nomenclature to describe the PNPLA family is proposed.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0022227520434601; http://dx.doi.org/10.1194/jlr.m600185-jlr200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33748745960&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/16799181; https://linkinghub.elsevier.com/retrieve/pii/S0022227520434601; http://www.jlr.org/lookup/doi/10.1194/jlr.M600185-JLR200; https://syndication.highwire.org/content/doi/10.1194/jlr.M600185-JLR200; https://dx.doi.org/10.1194/jlr.m600185-jlr200
Elsevier BV
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