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(Received for publication, June 28, 1996, and in revised form, August 27, 1996)
From the Laboratory of Skin Biology, NIAMS, National Institutes of
Health, Bethesda, Maryland 20892-2752
Involucrin was the first protein to be identified
as a likely constituent of the insoluble cornified cell envelope (CE)
of stratified squamous epithelia. However, to date, direct isolation from CEs of involucrin cross-linked by way of the
transglutaminase-induced isopeptide bond has not been reported. We have
treated human foreskin CEs with methanol/KOH (saponification) to
hydrolyze off much of the lipids. By immunogold electron microscopy,
this exposed large amounts of involucrin epitopes as well as of
desmoplakin, a desmosomal structural protein. About 20% of the total
CE protein could be solubilized by proteolytic digestion after
saponification, of which involucrin was the most abundant. Subsequent
amino acid sequencing revealed many peptides involving involucrin
cross-linked either to itself or to a variety of other known CE protein
components, including cystatin
Volume 272, Number 3,
Issue of January 17, 1997
pp. 2021-2030
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
, desmoplakin, elafin, keratins,
members of the small proline-rich superfamily, loricrin, and unknown
proteins related to the desmoplakin family. Specific glutamines or
lysines of involucrin were used to cross-link the different proteins, such as glutamines 495 and 496 to desmoplakin, glutamine 288 to keratins, and lysines 468, 485, and 508 and glutamines 465 and 489 for
interchain involucrin cross-links. Many identical peptides were
obtained from immature CEs isolated from the inner living cell layers
of foreskin epidermis. The multiple cross-linked partners of involucrin
provide experimental confirmation that involucrin is an important early
scaffold protein in the CE. Further, these data suggest that there is
significant redundancy in the structural organization of the CE.
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