The biosynthesis of human epidermal prekeratin [Abstract]

Bladon, P. T., Bowden, Paul Edward, Wood, E. J. and Cunliffe, W. J. 1981. The biosynthesis of human epidermal prekeratin [Abstract]. British Journal of Dermatology 105 (3) , pp. 345-346. 10.1111/j.1365-2133.1981.tb01295.x

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Abstract

The formation of keratin filaments is a prerequisite for normal keratinization, the initial stages of which include the biosynthesis and post-translational modifications of prekeratin polypeptides in living epidermal cells. It is possible to translate messenger RNA (mRNA) from human epidermis in a cell-free system and to isolate the initial gene products by precipitation with antiserum to prekeratin (Bowden et al., 1980). We have now investigated the next stage of keratin formation, the biochemical processing of the initial gene products, by comparing native prekeratin with the products of in vitro incubation and cell-free biosynthesis. Slices of scalp epidermis were incubated with labelled amino acids and processed prekeratin isolated either by immunoprecipitation with anti-prekeratin IgG bound to protein A-sepharose or by isoelectric precipitation (Skerrow, 1977). Native epidermal prekeratin was prepared and was labelled with ['*C]-formaldehyde (Rice & Means, 1971). The products of mRNA-directed cell-free translation were isolated by immunoprecipitation and the labelled proteins compared by SDS-PAGE (Bowden & Cunliffe, 1980) and fluorography. Human scalp epidermis incorporated labelled amino acids into prekeratin, which had similar electrophoretic behaviour to native prekaratin. However, the products of mRNA-directed biosynthesis contained fewer polypeptide chains than prekeratin synthesized by incubation of epidermal tissue. As the translation of mRNA in the reticulocyte lysate system yields essentially unprocessed polypeptide chains, it is possible that the more complex polypeptide chain composition of native and in vitro hiosynthesized prekeratin is due to post-translational modification. The exact molecular nature of this mechanism is presently under investigation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Subjects:	R Medicine > R Medicine (General) R Medicine > RL Dermatology
Additional Information:	Society Proceedings - BAD Investigative Group Meeting, Cardiff, January 1981.
Publisher:	Wiley-Blackwell
ISSN:	0007-0963
Last Modified:	12 Jun 2019 02:24
URI:	https://orca.cardiff.ac.uk/id/eprint/57811

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