J. Lipid Res.
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A more recent version of this article appeared on November 1, 2005

Papers In Press, published online ahead of print September 8, 2005
J. Lipid Res., doi:10.1194/jlr.M500258-JLR200
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Submitted on June 20, 2005
Revised on July 28, 2005
Accepted on August 18, 2005

Expression and regulation of 1-acyl-sn-glycerol-3-phosphate acyltransferases in the epidermis

Biao Lu, Yan J. Jiang, Mao Q. Man, Barbara Brown, Peter M. Elias, and Kenneth R. Feingold

Dematology and Medicine Services, Veterans Administration Medical Center and University of California School of Medicine, San Francisco, San Francisco, CA 94121

Corresponding Author: lubiao{at}itsa.ucsf.edu

Phospholipids are a major class of lipids in epidermal lamellar bodies, 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. To date, at least five isoforms of this key enzyme have been identified in mice; i.e., mAGPAT 1-5, which are encoded by distinct genes. We identified an expression pattern of AGPAT isoforms that is unique to epidermis, with relatively high constitutive expression of 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. Further, rAGPAT 2 and 5 mRNAs increased in parallel with both an increase in enzyme activity, and permeability barrier formation late in fetal rat epidermal development. Moreover, following 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. Since up-regulation of mAGPAT mRNAs after tape-stripping could be partially reversed by artificially barrier restoration by occlusion, these studies suggest that an increase in the expression of AGPATs is linked to barrier requirements. Together, these studies reveal a unique pattern of AGPAT isoform expression in murine epidermis. The temporal regulation of AGPAT late in fetal epidermal development, and in response to altered barrier requirements, suggest that epidermal phospholipid synthesis is modulated to maintain epidermal permeability barrier homeostasis.


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K. R. Feingold
Thematic review series: Skin Lipids. The role of epidermal lipids in cutaneous permeability barrier homeostasis
J. Lipid Res., December 1, 2007; 48(12): 2531 - 2546.
[Abstract] [Full Text] [PDF]


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