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Journal of Lipid Research, Vol 33, 1201-1209, Copyright © 1992 by Lipid Research, Inc.
beta-Glucocerebrosidase activity in murine epidermis: characterization and localization in relation to differentiation
WM Holleran, Y Takagi, G Imokawa, S Jackson, JM Lee and PM Elias
Department of Dermatology, University of California School of Medicine, San Francisco.
The intercellular lipids of the stratum corneum, which are highly enriched
in ceramides, are critical for the mammalian epidermal permeability
barrier. During the terminal stages of epidermal differentiation, the
glucosylceramide content is dramatically reduced, while the content of free
ceramides increases. To investigate whether beta-glucocerebrosidase
(beta-GlcCer'ase) could be responsible for this change in lipid content, we
characterized its activity in murine epidermis, compared enzyme activity to
other murine tissues, and localized beta-GlcCer'ase activity within the
epidermis. Epidermal extracts demonstrated linear
4-methylumbelliferyl-beta-D-glucose hydrolysis (to 3 h) with protein
concentrations between 1 and 250 micrograms/ml. Whole epidermis contained
comparable beta-glucosidase activity (9.1 +/- 0.4 nmol/min per mg DNA) to
murine brain and liver, and 5-fold higher activity than spleen. Epidermal
beta-glucosidase activity was stimulated greater than 15-fold by sodium
taurocholate at pH 5.6, and inhibited at acidic pH (3.5-4.0).
Bromoconduritol B epoxide (greater than or equal to 1.0 microM), inhibited
epidermal enzyme activity by greater than 75%, while activity in brain,
liver, and spleen was only inhibited by 6, 17, and 14%, respectively.
Moreover, beta-GlcCer'ase mRNA expression in murine epidermis exceeded
levels in liver, brain, and spleen. Finally, beta-GlcCer'ase activity was
highest in the outer, more differentiated epidermal cell layers including
the stratum corneum. In summary, mammalian epidermis contains an usually
high percentage (approximately 75%) of beta-glucocerebrosidase activity,
and the concentration of activity in the more differentiated cell layers
may account for the replacement of glucosylceramide by ceramides in the
outer epidermis.

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Copyright © 1992 by the American Society for Biochemistry and Molecular Biology.
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