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Science 30 June 1978:
Vol. 200. no. 4349, pp. 1491 - 1493
DOI: 10.1126/science.566466
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Articles

Science, Vol 200, Issue 4349, 1491-1493
Copyright © 1978 by American Association for the Advancement of Science

articles

Biochemical evidence for keratinization by mouse epidermal cells in culture

P Steinert and SH Yuspa

More than 70 percent of the urea-extractable proteins from mouse stratum corneum or from differentiated cells of mouse epidermis grown in culture are two proteins of molecular weight 68,000 (keratin I) and 60,000 (kerae are two proteins of molecular weight 68,000 (keratin 1) and 60,000 (keratin 2), which are present in equimolar amounts on polyacrylamide gels. These proteins are the subunits of the keratin filaments, because when isolated from stratum corneum or cells grown in culture they form native-type epidermal keratin filaments in vitro. These observations provide biochemical evidence that epidermal cells grown in culture synthesize the major differentiation products of the epidermis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Protein composition of cornified cell envelopes of epidermal keratinocytes.
A. Steven and P. Steinert (1994)
J. Cell Sci. 107, 693-700
   Abstract »    PDF »
Actin in Human Corneal Epithelium.
H. K. Soong and J. A. Fairley (1985)
Arch Ophthalmol 103, 565-568
   Abstract »    PDF »
Heterogeneity of Intermediate Filaments Assembled In Vitro.
P. Steinert, W. Idler, M. Aynardi-Whitman, R. Zackroff, and R. D. Goldman (1982)
Cold Spring Harb Symp Quant Biol 46, 465-474
   Abstract »    PDF »


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