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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Main Authors: Biao Lu, Yan J. Jiang, Mao Q. Man, Barbara Brown, Peter M. Elias, Kenneth R. Feingold
Format: Article
Language:English
Published: Elsevier 2005-11-01
Series:Journal of Lipid Research
Subjects:
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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