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Vol. 12, Issue 6, 1557-1568, June 2001
and
*Institute of Genetics, University of Bonn, 53117 Bonn, Germany;
The expression of distinct keratin pairs during epidermal
differentiation is assumed to fulfill specific and essential
cytoskeletal functions. This is supported by a great variety of
genodermatoses exhibiting tissue fragility because of keratin
mutations. Here, we show that the loss of K10, the most prominent
epidermal protein, allowed the formation of a normal epidermis in
neonatal mice without signs of fragility or wound-healing response.
However, there were profound changes in the composition of suprabasal
keratin filaments. K5/14 persisted suprabasally at elevated protein
levels, whereas their mRNAs remained restricted to the basal
keratinocytes. This indicated a novel mechanism regulating keratin
turnover. Moreover, the amount of K1 was reduced. In the absence of its
natural partner we observed the formation of a minor amount of novel
K1/14/15 filaments as revealed by immunogold electron microscopy. We
suggest that these changes maintained epidermal integrity. Furthermore, suprabasal keratinocytes contained larger keratohyalin granules similar
to our previous K10T mice. A comparison of profilaggrin processing in
K10T and K10Institute of Anatomy, University Hospital of Bonn, 53115 Bonn, Germany; and Division of Cell Biology, German
Cancer Research Center, 69120 Heidelberg, Germany
/ mice revealed an accumulation
of filaggrin precursors in the former but not in the latter, suggesting
a requirement of intact keratin filaments for the processing. The mild
phenotype of K10/ mice suggests that there
is a considerable redundancy in the keratin gene family.
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