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J Biol Chem, Vol. 273, Issue 28, 17763-17770, July 10, 1998
From the Laboratory of Skin Biology, NIAMS, National Institutes of
Health, Bethesda, Maryland 20892-2752
An important component of barrier function in
human epidermis is contributed by ceramides that are bound by ester
linkages to undefined proteins of the cornified cell envelope (CE). In this paper, we have examined the protein targets for the ceramide attachment. By partial saponification of isolated foreskin epidermal CEs followed by limited proteolysis, we have recovered several lipopeptides. Biochemical and mass spectroscopic characterization revealed that all contained near stoichiometric amounts of ceramides of
masses ranging from about 690 to 890 atomic mass units, of which six
quantitatively major species were common. The array of ceramides was
similar to that obtained from pig skin, the composition of which is
known, thereby providing strong indirect data for their fatty acid and
sphingosine compositions. The recovered peptides accounted for about
20% of the total foreskin CE ceramides. By amino acid sequencing,
about 35% of the peptides were derived from ancestral
glutamine-glutamate-rich regions of involucrin, an important CE
structural protein. Another 18% derived from rod domain sequences of
periplakin and envoplakin, which are also known or suspected CE
proteins. Other peptides were too short for unequivocal identification.
Together, these data indicate that involucrin, envoplakin, periplakin,
and possibly other structural proteins serve as substrates for the
attachment of ceramides by ester linkages to the CE for barrier
function in human epidermis.
Ceramides Are Bound to Structural Proteins of the Human Foreskin
Epidermal Cornified Cell Envelope
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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