A review of phosphatidate phosphatase assays
Phosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol and regulates the synthesis of membrane phospholipids. There is much interest in this enzyme because it controls the cellular levels of its substrate, phosphatidate (PA), and product, DAG; defects in t...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520600189 |
| _version_ | 1818592017936023552 |
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| author | Prabuddha Dey Gil-Soo Han George M. Carman |
| author_facet | Prabuddha Dey Gil-Soo Han George M. Carman |
| author_sort | Prabuddha Dey |
| collection | DOAJ |
| description | Phosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol and regulates the synthesis of membrane phospholipids. There is much interest in this enzyme because it controls the cellular levels of its substrate, phosphatidate (PA), and product, DAG; defects in the metabolism of these lipid intermediates are the basis for lipid-based diseases such as obesity, lipodystrophy, and inflammation. The measurement of PAP activity is required for studies aimed at understanding its mechanisms of action, how it is regulated, and for screening its activators and/or inhibitors. Enzyme activity is determined through the use of radioactive and nonradioactive assays that measure the product, DAG, or Pi. However, sensitivity and ease of use are variable across these methods. This review summarizes approaches to synthesize radioactive PA, to analyze radioactive and nonradioactive products, DAG and Pi, and discusses the advantages and disadvantages of each PAP assay. |
| first_indexed | 2024-12-16T10:21:39Z |
| format | Article |
| id | doaj.art-21fab71ec1164ab094efc00f42dc7172 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-16T10:21:39Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-21fab71ec1164ab094efc00f42dc71722022-12-21T22:35:17ZengElsevierJournal of Lipid Research0022-22752020-12-01611215561564A review of phosphatidate phosphatase assaysPrabuddha Dey0Gil-Soo Han1George M. Carman2Department of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, USADepartment of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, USADepartment of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, USA; For correspondence: George M. Carman; For correspondence: George M. CarmanPhosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol and regulates the synthesis of membrane phospholipids. There is much interest in this enzyme because it controls the cellular levels of its substrate, phosphatidate (PA), and product, DAG; defects in the metabolism of these lipid intermediates are the basis for lipid-based diseases such as obesity, lipodystrophy, and inflammation. The measurement of PAP activity is required for studies aimed at understanding its mechanisms of action, how it is regulated, and for screening its activators and/or inhibitors. Enzyme activity is determined through the use of radioactive and nonradioactive assays that measure the product, DAG, or Pi. However, sensitivity and ease of use are variable across these methods. This review summarizes approaches to synthesize radioactive PA, to analyze radioactive and nonradioactive products, DAG and Pi, and discusses the advantages and disadvantages of each PAP assay.http://www.sciencedirect.com/science/article/pii/S0022227520600189Pah1lipinenzyme assaysradioactive assaysnonradioactive assaysdiacylglycerol |
| spellingShingle | Prabuddha Dey Gil-Soo Han George M. Carman A review of phosphatidate phosphatase assays Journal of Lipid Research Pah1 lipin enzyme assays radioactive assays nonradioactive assays diacylglycerol |
| title | A review of phosphatidate phosphatase assays |
| title_full | A review of phosphatidate phosphatase assays |
| title_fullStr | A review of phosphatidate phosphatase assays |
| title_full_unstemmed | A review of phosphatidate phosphatase assays |
| title_short | A review of phosphatidate phosphatase assays |
| title_sort | review of phosphatidate phosphatase assays |
| topic | Pah1 lipin enzyme assays radioactive assays nonradioactive assays diacylglycerol |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520600189 |
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