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PMID: 19029121 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions.

Journal of lipid research ·Vol. 50 Suppl ·2009-04-00 ·Pages S63-8

Kienesberger PC, Oberer M, Lass A, Zechner R

Abstract

The human genome expresses nine patatin-like phospholipase domain containing proteins (PNPLA1-9). Members of this family share a protein domain discovered initially in patatin, the most abundant protein of the potato tuber. Patatin is a lipid hydrolase with an unusual folding topology that differs from classical lipases. Mammalian PNPLAs include lipid hydrolases with specificities for diverse substrates such as triacylglycerols, phospholipids, and retinol esters. Analysis of induced mutant mouse models and the clinical phenotype of patients with mutations revealed important insights into the physiological role of several members of the PNPLA family. This review aims to summarize current knowledge of PNPLA proteins and to document their emerging importance in lipid and energy homeostasis.

MeSH Terms
Animals Biological Phenomena Humans Keratinocytes/enzymology Lipase/chemistry,classification,genetics,metabolism Lipolysis Mammals/classification,genetics,metabolism Triglycerides/metabolism
Chemicals
Triglycerides Lipase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kienesberger Petra C
Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Oberer Monika
Lass Achim
Zechner Rudolf
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Article Info
Journal
Journal of lipid research
Abbr.
J Lipid Res
ISSN
0022-2275
Published
2009-04-00
Epub
2008-00-23
Pages
S63-8
Language
English
Region
United States
NLM ID
0376606
PMCID
PMC2674697
Subset
IM
Grants
Austrian Science Fund FWF · F 3002 · Austria
Austrian Science Fund FWF · W 901 · Austria
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