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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
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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 LangbeinDagger §, Michael A. Rogers, Hermelita Winter, Silke PraetzelDagger , and Jürgen Schweizer

From the Divisions of Dagger  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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