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2 results on '"GS2-like"'

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

Author

Petra C. Kienesberger, Monika Oberer, Achim Lass, and Rudolf Zechner

Subjects
PNPLA, ATGL, adiponutrin, GS2, GS2-like, NTE, Biochemistry, QD415-436
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.

Published
2009
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2. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions

Author

Monika Oberer, Rudolf Zechner, Achim Lass, and Petra C. Kienesberger

Subjects
Keratinocytes, Lipolysis, Mutant, QD415-436, Phospholipase, Biology, Biochemistry, Energy homeostasis, GS2-like, ATGL, Endocrinology, Hydrolase, Animals, Humans, Adiponutrin, education, Triglycerides, Biological Phenomena, Mammals, Genetics, education.field_of_study, PNPLA, food and beverages, Lipase, Cell Biology, NTE, Patatin-like phospholipase, adiponutrin, Enzymology, GS2, lipids (amino acids, peptides, and proteins), Human genome, Patatin
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.

Published
2009
Full Text
View/download PDF

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