Protein modifications during the keratinization of normal and psoriatic human epidermis

Skerrow, David; Hunter, Irene

doi:10.1016/0005-2795(78)90532-9

Cited by 91 publications

(53 citation statements)

References 15 publications

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“…For human epidermis, the commitment of basal cells (Fig. 2, track 2) to terminal differentiation and stratum corneum formation (track 1) seems to be correlated with increased synthesis of large keratins of Mr 63,000-67,000 (12,15,36 trastructural studies indicating that differentiation and stratum corneum formation in the epidermis of these mutant mice is less pronounced.…”

Section: Resultsmentioning

confidence: 99%

Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin.

Fuchs¹,

Marchuk²

1983

Proc. Natl. Acad. Sci. U.S.A.

136

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We have traced the evolutionary origins of keratin-like sequences to the genomes of lower eukaryotes. The proteins encoded by these genes have evolved to form the intermediate filaments that comprise the backbone of vertebrate skin cells. Two related but distinct types of keratins encoded by two separate multigene subfamilies are expressed in the epidermal keratinocytes of vertebrate species from fish to human. Both at the level of protein and at the level of DNA, these two classes of keratins are coordinately conserved throughout vertebrate evolution, indicating the central role that both types of keratins must play in the assembly and structure of the 8-nm filament.

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Section: Resultsmentioning

confidence: 99%

Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin.

Fuchs¹,

Marchuk²

1983

Proc. Natl. Acad. Sci. U.S.A.

136

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“…Changes in keratin synthesis have been observed for differentiating epidermis during embryonic development (2) and during the terminal differentiation of the adult epidermis (3)(4)(5)(6). Different keratin polypeptide patterns are also seen for keratinocytes in intact epidermis and keratinocytes growing in culture (6)(7)(8)(9).…”

mentioning

confidence: 88%

Keratin gene expression in mouse epidermis and cultured epidermal cells.

Roop¹,

Hawley‐Nelson²,

Cheng³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

159

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The major differentiation products ofmouse epidermis are keratins of40-70 kilodaltons (kDal). We have prepared a library of cDNA clones from total poly(A)+ RNA from newborn mouse epidermis. Clones corresponding to the major in vivo keratins of55, 59, and 67 kDal have been isolated and characterized.By RNA blot analysis of poly(A)" RNA from newborn mouse epidermis, we have identified RNA species that are approximately 1,600, 2,000, and 2,400 nucleotides in length and are complementary to the cDNAs for the 55-, 59-, and 67-kDal keratins, respectively. Analysis of RNA from primary cultures of newborn mouse epidermis by this same technique shows greatly reduced levels of these RNAs. Transcripts complementary to all three cloned cDNAs are abundant in 14-to 16-day embryonic and adult mouse skin. Thus, altered expression in culture does not appear to be due to induction of a developmentally programmed switch by placing the cells in culture but instead is due to factors modulating expression within the culture system. Because the 55-, 59-, and 67-kDal keratins are the major proteins in epidermis they probably represent keratin associated with terminal differentiation. The expression data suggest that cultured cells are blocked in expression ofdifferentiation keratins but instead synthesize other keratin family members probably related to cytoskeletal functions.Keratins constitute a family of at least 10 related a-helix-rich structural proteins of40-70 kilodaltons (kDal) and make up the subunits of the intermediate filaments (keratin filaments) present in large amounts in mammalian epidermis (1). Changes in keratin synthesis have been observed for differentiating epidermis during embryonic development (2) and during the ter-

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“…The large keratins are abundant only in differentiating epidermal cells and are probably associated with stratum corneum formation (7,13,15,35). The smaller keratins are present in conjunctival cells (16,41), the intestinal epithelium (10), mesothelial cells (46), and many simple and glandular epithelia (24), but they are not prominent in epidermal cells, esophageal cells, or epithelial cells of the oral cavity (10,15,23).…”

mentioning

confidence: 99%

Tissue specificity of epithelial keratins: differential expression of mRNAs from two multigene families.

Kim¹,

Rheinwald²,

Fuchs³

1983

Mol. Cell. Biol.

120

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Human epithelial cells cultured from stratified and simple squamous tissues all produce keratins of 40,000 to 58,000 daltons, but within this range the number and sizes vary with different epithelial cells. We have shown that this tissue-specific variation in the keratins is not due to posttranslational modification or processing, but rather to the differential expression of a family of heterogeneous but closely related mRNAs. All of these epithelial keratin mRNAs can be further grouped into two distinct subfamilies by their ability to hybridize with either of two cloned epidermal keratin cDNAs. All of the keratin mRNAs hybridize to one or the other, but not both, of the two cloned cDNAs. However, the mRNAs within each group hybridize with varying degrees of stringency, indicating that they are of similar but not identical sequence. Both types of keratin mRNAs are always expressed in every epithelial cell line studied, suggesting that filament assembly is dependent on the presence of both types of keratins. Within each of these two groups, the slight sequence differences in each class may reflect subtle tissue-specific variations in the structural and functional requirements of the epithelial cytoskeleton.

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Protein modifications during the keratinization of normal and psoriatic human epidermis

Cited by 91 publications

References 15 publications

Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin.

Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin.

Keratin gene expression in mouse epidermis and cultured epidermal cells.

Tissue specificity of epithelial keratins: differential expression of mRNAs from two multigene families.

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