Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism
Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence...
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Published in | M.S. Médecine sciences Vol. 26; no. 2; p. 177 |
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Main Authors | , |
Format | Journal Article |
Language | French |
Published |
France
01.02.2010
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Subjects | |
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Abstract | Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence genomics with as a main objective to yield insight into cellular physiology. Recently, an emerging group of genes coding for proteins bearing a common domain termed patatin (PNPLA domain) have been discovered. Members of this new enzymatic family displaying lipase and transacylase properties appeared to have major roles in the regulation of lipid metabolism. The aim of this review is to make an overview on the latest discoveries concerning this new family of proteins and their relationship with lipid metabolism, physiology of mammals and their potential involvement in human pathology. |
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AbstractList | Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence genomics with as a main objective to yield insight into cellular physiology. Recently, an emerging group of genes coding for proteins bearing a common domain termed patatin (PNPLA domain) have been discovered. Members of this new enzymatic family displaying lipase and transacylase properties appeared to have major roles in the regulation of lipid metabolism. The aim of this review is to make an overview on the latest discoveries concerning this new family of proteins and their relationship with lipid metabolism, physiology of mammals and their potential involvement in human pathology.Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence genomics with as a main objective to yield insight into cellular physiology. Recently, an emerging group of genes coding for proteins bearing a common domain termed patatin (PNPLA domain) have been discovered. Members of this new enzymatic family displaying lipase and transacylase properties appeared to have major roles in the regulation of lipid metabolism. The aim of this review is to make an overview on the latest discoveries concerning this new family of proteins and their relationship with lipid metabolism, physiology of mammals and their potential involvement in human pathology. Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence genomics with as a main objective to yield insight into cellular physiology. Recently, an emerging group of genes coding for proteins bearing a common domain termed patatin (PNPLA domain) have been discovered. Members of this new enzymatic family displaying lipase and transacylase properties appeared to have major roles in the regulation of lipid metabolism. The aim of this review is to make an overview on the latest discoveries concerning this new family of proteins and their relationship with lipid metabolism, physiology of mammals and their potential involvement in human pathology. |
Author | Baulande, Sylvain Langlois, Clotilde |
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References | 20188036 - Med Sci (Paris). 2010 Feb;26(2):128-30 |
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SubjectTerms | Amino Acid Sequence Animals Arabidopsis Proteins - chemistry Arabidopsis Proteins - physiology Caenorhabditis elegans Proteins - chemistry Caenorhabditis elegans Proteins - physiology Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - classification Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - physiology Catalytic Domain - genetics Conserved Sequence Drosophila Proteins - chemistry Drosophila Proteins - physiology Escherichia coli Proteins - chemistry Escherichia coli Proteins - physiology Humans Lipase - chemistry Lipase - physiology Lipid Metabolism - genetics Lipid Metabolism - physiology Lipolysis - genetics Mammals - metabolism Mice Molecular Sequence Data Multigene Family Phospholipases A2, Calcium-Independent - chemistry Phospholipases A2, Calcium-Independent - physiology Phylogeny Plant Proteins - chemistry Plant Proteins - physiology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - physiology Sequence Alignment Sequence Homology, Amino Acid Species Specificity |
Title | Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism |
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