Expression and regulation of mRNA for putative fatty acid transport related proteins and fatty acyl CoA synthase in murine epidermis and cultured human keratinocytes.
The epidermis has a requirement for fatty acids in order to synthesize cellular membranes and the extracellular lipid lamellar membranes in the stratum corneum. Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requirement. Fatty acid uptake by keratinocytes has been shown to be mediated by a transport system. In this study we determined in murine epidermis and human cultured keratinocytes the expression of three putative fatty acid transport related proteins and fatty acyl CoA synthase, an enzyme that facilitates the uptake of fatty acids by promoting their metabolism. In cultured human keratinocytes, mRNA for fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABP-pm), and fatty acyl CoA synthase (FACS) were detectable. Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an approximately 50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50%. Fatty acid translocase (FAT) mRNA was not detected in cultured human keratinocytes. In murine epidermis, FATP, FABP-pm, FACS, and FAT mRNA were all present. Barrier disruption by either tape stripping or acetone treatment increased FAT mRNA levels by approximately 2-fold without affecting FATP, FABP-pm, or FACS. Occlusion with an impermeable membrane immediately after barrier disruption completely blocked the increase in FAT mRNA levels, indicating that this increase is related to barrier disruption rather than a nonspecific injury effect. In summary, this study demonstrates that several putative fatty acid transport related proteins as well as fatty acyl CoA synthase are expressed in keratinocytes and epidermis, and that the expression of these proteins may be regulated by differentiation and/ or barrier disruption.
Harris
I R
IR
Department of Veterans Affairs Medical Center and Department of Dermatology, University of California, San Francisco 94121, USA.
Farrell
A M
AM
Memon
R A
RA
Grunfeld
C
C
Elias
P M
PM
Feingold
K R
KR
D000818:Animals; D018955:CD36 Antigens; D002352:Carrier Proteins / Q000235:genetics*; D002454:Cell Differentiation; D002463:Cell Membrane Permeability; D002478:Cells, Cultured; D003066:Coenzyme A Ligases / Q000235:genetics*; D050612:Fatty Acid Transport Proteins; D006801:Humans; D015603:Keratinocytes / Q000737:chemistry / Q000166:cytology / Q000378:metabolism*; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics*; D026901:Membrane Transport Proteins; D051379:Mice; D008812:Mice, Hairless; D027361:Organic Anion Transporters; D012333:RNA, Messenger / Q000378:metabolism*; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012867:Skin / Q000166:cytology / Q000378:metabolism*; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D018955:CD36 Antigens; D002352:Carrier Proteins; D050612:Fatty Acid Transport Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D027361:Organic Anion Transporters; D012333:RNA, Messenger; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; C493572:Slc27a4 protein, mouse; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase