Characterization of the human patatin-like phospholipase family

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 ch...

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Bibliographic Details
Published in:Journal of lipid research 2006-09, Vol.47 (9), p.1940-1949
Main Authors: Wilson, Paul A, Gardner, Scott D, Lambie, Natalie M, Commans, Stephane A, Crowther, Daniel J
Format: Article
Language:English
Subjects:
Adipocytes - enzymology
Adipocytes - metabolism
Amino Acid Sequence
Base Sequence
Cell Line
Female
Gene Expression Profiling
Humans
Isoenzymes - chemistry
Isoenzymes - genetics
Male
Molecular Sequence Data
Oligonucleotide Array Sequence Analysis
Phospholipases - chemistry
Phospholipases - genetics
Phylogeny
Protein Structure, Secondary
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0022-2275
1539-7262
DOI:10.1194/jlr.m600185-jlr200