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Originally published In Press as doi:10.1074/jbc.M103305200 on July 9, 2001
J. Biol. Chem., Vol. 276, Issue 37, 35123-35132, September 14, 2001
The Catalog of Human Hair Keratins
II. EXPRESSION OF THE SIX TYPE II MEMBERS IN THE HAIR FOLLICLE
AND THE COMBINED CATALOG OF HUMAN TYPE I AND II KERATINS*
Lutz
Langbein §,
Michael A.
Rogers¶,
Hermelita
Winter¶,
Silke
Praetzel , and
Jürgen
Schweizer¶
From the Divisions of Cell Biology and
¶ Tumor Cell Regulation, German Cancer Research Center,
Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
The human type II hair keratin subfamily consists
of six individual members and can be divided into two groups. The group A members hHb1, hHb3, and hHb6 are structurally related, whereas group
C members hHb2, hHb4, and hHb5 are rather distinct. Specific antisera
against the individual hair keratins were used to establish the
two-dimensional catalog of human type II hair keratins. In this
catalog, hHb5 showed up as a series of isoelectric variants, well
separated from a lower, more acidic, and complex protein streak
containing isoelectric variants of hair keratins hHb1, hHb2, hHb3, and
hHb6. Both in situ hybridization and immunohistochemistry on anagen hair follicles showed that hHb5 and hHb2 defined early stages
of hair differentiation in the matrix (hHb5) and cuticle (hHb5 and
hHb2), respectively. Although cuticular differentiation proceeded
without the expression of further type II hair keratins, cortex cells
simultaneously expressed hHb1, hHb3, and hHb6 at an advanced stage of
differentiation. In contrast, hHb4, which is undetectable in hair
follicle extracts and sections, could be identified as the largest and
most alkaline member of this subfamily in cytoskeletal extracts of
dorsal tongue. This hair keratin was localized in the posterior
compartment of the tongue filiform papillae. Comparative
analysis of type II with the previously published type I hair keratin
expression profiles suggested specific, but more likely, random
keratin-pairing principles during trichocyte differentiation.
Finally, by combining the previously published type I hair keratin
catalog with the type II hair keratin catalog and integrating both into
the existing catalog of human epithelial keratins, we present a
two-dimensional compilation of the presently known human keratins.
*
This work was supported in part by Deutsche
Forschungsgemeinschaft Grant Schw 539/4-1. This is Paper II in the
series "Catalog of Human Hair Keratins." Ref. 46 is Paper I in the
series.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
§
To whom correspondence should be addressed: German Cancer Research
Center, Division of Cell Biology, A0100, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany. Tel.: 49-6221-42-3436; Fax:
49-6221-42-3404; E-mail: Langbein@dkfz.de.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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