Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis
Phospholipids are a major class of lipids in epidermis, where they serve as a source of free fatty acids that are important for the maintenance of epidermal permeability barrier function. The phospholipid biosynthetic enzyme, 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT), catalyzes the acyl...
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Elsevier
2005-11-01
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Series: | Journal of Lipid Research |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520328832 |
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author | Biao Lu Yan J. Jiang Mao Q. Man Barbara Brown Peter M. Elias Kenneth R. Feingold |
author_facet | Biao Lu Yan J. Jiang Mao Q. Man Barbara Brown Peter M. Elias Kenneth R. Feingold |
author_sort | Biao Lu |
collection | DOAJ |
description | Phospholipids are a major class of lipids in epidermis, where they serve as a source of free fatty acids that are important for the maintenance of epidermal permeability barrier function. The phospholipid biosynthetic enzyme, 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT), catalyzes the acylation of lysophosphatidic acid to form phosphatidic acid, the major precursor of all glycerolipids. We identified an expression pattern of AGPAT isoforms that is unique to epidermis, with relatively high constitutive expression of mouse AGPAT (mAGPAT) 3, 4, and 5 but low constitutive expression of mAGPAT 1 and 2. Localization studies indicate that all five isoforms of AGPAT were expressed in all nucleated layers of epidermis. Furthermore, rat AGPAT 2 and 5 mRNAs increased in parallel with both an increase in enzyme activity and permeability barrier formation late in rat epidermal development. Moreover, after two methods of acute permeability barrier disruption, mAGPAT 1, 2, and 3 mRNA levels increased rapidly and were sustained for at least 24 h. In parallel with the increase in mRNA levels, an increase in AGPAT activity also occurred.Because upregulation of mAGPAT mRNAs after tape-stripping could be partially reversed by artificial barrier restoration by occlusion, these studies suggest that an increase in the expression of AGPATs is linked to barrier requirements. |
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spelling | doaj.art-02829b8ff0ce4bc1aedf124824ed1e5f2022-12-21T21:25:25ZengElsevierJournal of Lipid Research0022-22752005-11-01461124482457Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermisBiao Lu0Yan J. Jiang1Mao Q. Man2Barbara Brown3Peter M. Elias4Kenneth R. Feingold5Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121To whom correspondence should be addressed.; Dermatology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, CA 94121Phospholipids are a major class of lipids in epidermis, where they serve as a source of free fatty acids that are important for the maintenance of epidermal permeability barrier function. The phospholipid biosynthetic enzyme, 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT), catalyzes the acylation of lysophosphatidic acid to form phosphatidic acid, the major precursor of all glycerolipids. We identified an expression pattern of AGPAT isoforms that is unique to epidermis, with relatively high constitutive expression of mouse AGPAT (mAGPAT) 3, 4, and 5 but low constitutive expression of mAGPAT 1 and 2. Localization studies indicate that all five isoforms of AGPAT were expressed in all nucleated layers of epidermis. Furthermore, rat AGPAT 2 and 5 mRNAs increased in parallel with both an increase in enzyme activity and permeability barrier formation late in rat epidermal development. Moreover, after two methods of acute permeability barrier disruption, mAGPAT 1, 2, and 3 mRNA levels increased rapidly and were sustained for at least 24 h. In parallel with the increase in mRNA levels, an increase in AGPAT activity also occurred.Because upregulation of mAGPAT mRNAs after tape-stripping could be partially reversed by artificial barrier restoration by occlusion, these studies suggest that an increase in the expression of AGPATs is linked to barrier requirements.http://www.sciencedirect.com/science/article/pii/S0022227520328832lamellar bodyphospholipidsepidermal permeability barrier |
spellingShingle | Biao Lu Yan J. Jiang Mao Q. Man Barbara Brown Peter M. Elias Kenneth R. Feingold Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis Journal of Lipid Research lamellar body phospholipids epidermal permeability barrier |
title | Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis |
title_full | Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis |
title_fullStr | Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis |
title_full_unstemmed | Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis |
title_short | Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis |
title_sort | expression and regulation of 1 acyl sn glycerol 3 phosphate acyltransferases in the epidermis |
topic | lamellar body phospholipids epidermal permeability barrier |
url | http://www.sciencedirect.com/science/article/pii/S0022227520328832 |
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