The acyl-CoA binding protein is required for normal epidermal barrier function in mice

M. BLOKSGAARD; S. BEK; MARCHER AB; NEESS D; J. BREWER; HANNIBAL-BACH HK; HELLEDIE T; FENGER C; DUE M; BERZINA Z; NEUBERT R,; CHEMNITZ J; FINSEN B; CLEMMENSEN A; WILBERTZ J; SAXTORPH H; KNUDSEN J; LUIS A. BAGATOLLI; S. MANDRUP

JLR PAPERS IN PRESS

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Lugar: Bethesda, Maryland; Año: 2012 vol. 53 p. 2162 - 2162

0022-2275

div class="">The acyl-CoA binding protein (ACBP) is a 10 kDa intracellular protein expressed in all eukaryotic species. Mice with targeted disruption of Acbp (ACBP(-/-) mice) are viable and fertile but present a visible skin and fur phenotype characterized by greasy fur and development of alopecia and scaling with age. Morphology and development of skin and appendages are normal in ACBP(-/-) mice; however, the stratum corneum display altered biophysical properties with reduced proton activity and decreased water content. Mass spectrometry analyses of lipids from epidermis and stratum corneum of ACBP(+/+) and ACBP(-/-) mice showed very similar composition, except for a significant and specific decrease in the very long chain free fatty acids (VLC-FFA) in stratum corneum of ACBP(-/-) mice. This finding indicates that ACBP is critically involved in the processes that lead to production of stratum corneum VLC-FFAs via complex phospholipids in the lamellar bodies. Importantly, we show t