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J Biol Chem, Vol. 273, Issue 52, 35176-35184, December 25, 1998
From the Keratins (K), the cytoplasmic intermediate
filament (IF) proteins of epithelial cells, are encoded by a multigene
family and expressed in a tissue- and differentiation-specific manner.
In human skin, keratinocytes of the basal layer of epidermis and the
outer root sheath of hair follicles express K5 and K14 as their main
keratins. A small subpopulation of basal cells exhibiting stem-cell
like characteristics express, in addition, K19. At 40 kDa, this keratin
is the smallest IF protein due to an exceptionally short
carboxyl-terminal domain. We examined the assembly properties of K19
and contrasted them to K14 in vitro and in
vivo. Relative to K5-K14, we find that K5-K19 form less stable
tetramers that polymerize into shorter and narrower IFs in
vitro. When transiently co-expressed in cultured baby hamster
kidney cells, the K5 and K19 combination fails to form a filamentous
array, whereas the K5-K14 and K8-K19 ones readily do so. Transient
expression of K19 in the epithelial cell lines T51B-Ni and A431 results
in its integration into the endogenous keratin network with minimal if any perturbation. Collectively, these results indicate that K19 possesses assembly properties that are distinct from those of K14 and
suggest that it may impart unique properties to the basal cells
expressing it in skin epithelia.
The Type I Keratin 19 Possesses Distinct and
Context-dependent Assembly Properties
,,
, and
Laboratoire de Recherche des Grands
Brûlés/LOEX, Hôpital du Saint-Sacrement,
Québec G1S 4L8, the Department of Surgery, Université
Laval, Sainte-Foy, Québec, Canada, and the Departments of
Biological Chemistry and Dermatology, The Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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