Tonofilament differentiation in human epidermis, isolation and polypeptide chain composition of keratinocyte subpopulations

Skerrow, David; Skerrow, Christine J.

doi:10.1016/0014-4827(83)90105-2

Cited by 123 publications

(49 citation statements)

References 21 publications

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“…Serial sectioning of human and rabbit plantar epidermis parallel to the skin surface has suggested that the keratins found in the outer dead epidermal layers are produced by modification of existing gene products [17, 231. Similar conclusions have been drawn from a comparison of total protein extracts of human granular cells and dead corneocytes [27], and from peptide mapping experiments [19, 231. In the present study we have compared individual mouse and human keratins by one-dimensional and two-dimensional peptide mapping (V8 protease and trypsin respectively). We have found that, in both species studied, a precursor-product relationship exists between certain prekeratins from the living epidermal cell layers and the SC keratins.…”

supporting

confidence: 75%

“…While basal cells from mouse epidermis contain two major prekeratins (larger basic, smaller acidic), cells in a suprabasal position contain two additional prekeratins (basic -acidic pair) and not only one as described by Skerrow and Skerrow for human epidermis [27], probably a discrepancy caused by the method used. Spinous cells contain these four prekeratins in approximately equal quantities but by the time these cells reach the granular layer, the relative content of 'suprabasal' prekeratins is higher.…”

Section: Fig 4 Compavison Of Individual 125-i-labelledprekevutins (mentioning

confidence: 90%

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Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Bowden

Quinlan

Breitkreutz

et al. 1984

European Journal of Biochemistry

112

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Keratins from the living cell layers of human and neonatal mouse epidermis (prekeratins) have been compared to those from the stratum corneum (SC keratins). Human and mouse epidermis contained four prekeratins, two ofeach keratin subfamily; type I1 basic (PI 6.5 -8.5 ; human 68 kDa, 60.5 kDa and mouse 67 kDa, 60 kDa) and type I acidic (PI 4.7 -5.7; human 57 kDa, 51 kDa and mouse 58 kDa, 53 kDa). While all four were present in equal amounts in adult human epidermis, two (67 kDa basic, 58 kDa acidic) were more prominent in neonatal mouse epidermis. Preliminary results with cell fractions (basal, spinous and granular) indicated that quantitative differences were a function of morphology, basal cells containing the smaller member of each subfamily and granular cells the larger. Mouse stratum corneum extracts contained four keratins (three in human): type 11 neutral -acidic (PI 5.7 -6.7; human 65 kDa and mouse 64 kDa, 62 kDa) and type I acidic (PI 4.9 -5.4; human 57.5 kDa, 55 kDa and mouse 58.5 kDa, 57.5 kDa). In both species, one-dimensional and two-dimensional peptide mapping (with V8 protease and trypsin respectively) indicated that while all four prekeratins were distinct gene products, similarities existed in the type I1 basic and the type I acidic keratin subfamilies. A strong homology also existed between type I1 SC keratins and the larger basic (type 11) prekeratin (human 68 kDa and mouse 67 kDa) and between type I SC keratins and the larger acidic (type I) prekeratin (human 57 kDa and mouse 58 kDa). These results indicate a precursor-product relationship within each keratin subfamily, between SC keratins and the prekeratins abundant in the adjacent granular layer. This differentiation-related keratin processing was similar in mouse and human epidermis, and may represent a widespread phenomenon amongst keratinising epithelia.

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supporting

confidence: 75%

Section: Fig 4 Compavison Of Individual 125-i-labelledprekevutins (mentioning

confidence: 90%

Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Bowden

Quinlan

Breitkreutz

et al. 1984

European Journal of Biochemistry

112

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“…Both in vivo and in vitro, filaments composed of these keratins are loosely bundled (Eichner et al, 1986). Upon stratification, these epithelial cell types diverge, and each expresses a unique set of keratins that are tissue-specific for their particular program of differentiation (Fuchs and Green, 1980;Viac et al, 1980;Woodcock-Mitchell et al, 1982;Skerrow and Skerrow, 1983;Crewther et al, 1983;van Muijen et al, 1986;Schermer et al, 1986). The expression of these new sets of keratins is frequently associated with an increase in bundling of keratin filaments (Steinert, 1978;Eichner et al, 1986).…”

mentioning

confidence: 99%

Expression of keratin K14 in the epidermis and hair follicle: insights into complex programs of differentiation.

Coulombe

Kopan

Fuchs

1989

The Journal of Cell Biology

188

143

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“…(a) Cytoplasmic proteins such as keratins. Immunolocalization and cell fractionation experiments have established that basal cells of normal epidermis synthesize two major keratin polypeptides, a 50/50'-kD acidic keratin and a 58-kD basic keratin, whereas cells of the suprabasal layers possess an additional 56.5-kD acidic and a 65-67-kD basic keratin (3,5,20,23,26,27,30,31,33). (b) Cell peripheral proteins, including involucrin (1,18), kerotolinin (34), and several other high molecular weight proteins (21,22).…”

mentioning

confidence: 99%

Differentiation-dependent changes in the solubility of a 195-kD protein in human epidermal keratinocytes.

S.-P.¹,

Sun²

1986

The Journal of Cell Biology

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Abstract. We have prepared a monoclonal antibody, AEll, that recognizes specifically a 195-kD protein (pI 5.4) of human keratinocytes. This antigen constitutes ,o0.01-0.1% of total protein in keratinocytes of skin, esophagus, and cornea, and is readily detectable in these cells by immunofluorescent staining and immunoblotting. However, it is barely detectable in MCF mammary carcinoma cells and HeLa cells, and is undetectable in nonepithelial cell types. Results from serial extraction experiments have shown that this protein exists in two distinct pools: a Tris-soluble, and a Tris-insoluble but urea-or SDS-soluble one. The distribution of the 195-kD protein between these two pools appears to be differentiation-related, since relatively undifferentiated cells selected by a low-calcium medium contain primarily the soluble form, while highly differentiated cells contain mainly the insoluble form. Data from immunofluorescent staining and trypsin-sensitivity experiments suggest that the soluble form is cytoplasmic, whereas the insoluble form is submembranously located at the cell periphery of upper, differentiated cells. The insoluble, cell peripheral form of the 195-kD antigen increases progressively during epidermal differentiation; its insolubility appears to be related to the formation of disulfidebond(s). These results indicate that the 195-kD protein, which has recently been suggested to be involved in cornified envelope formation (Simon, M., and H. Green, 1985, Cell, 36:827-834), undergoes significant changes in its solubility characteristics and intracellular location during keratinocyte maturation.UdPaNG terminal differentiation, epidermal cells unergo major biochemical changes. The molecules that undergo such alterations can be divided into two broad categories according to their intracellular location. (a) Cytoplasmic proteins such as keratins. Immunolocalization and cell fractionation experiments have established that basal cells of normal epidermis synthesize two major keratin polypeptides, a 50/50'-kD acidic keratin and a 58-kD basic keratin, whereas cells of the suprabasal layers possess an additional 56.5-kD acidic and a 65-67-kD basic keratin (3,5,20,23,26,27,30,31,33). (b) Cell peripheral proteins, including involucrin (1, 18), kerotolinin (34), and several other high molecular weight proteins (21, 22). Serving as the substrates for the Ca++-dependent transglutaminase (8, 28), these proteins are covalently cross-linked, forming a cornified envelope which is a submembranous structure characteristic of the cornified cells (17,24).In a series of experiments designed to generate monoclonal antibodies to the keratinocyte cell surface and its related components, we fused the spleen cells from Balb/c mice previously immunized with intact, human epidermal keratinocytes with X63.Ag8.653 mouse myeloma cells. Supernatants from wells containing hybridoma cells were screened for their ability to stain the periphery of keratinocytes in frozen sections of human epidermis by indirect immunofluorescent staining. We r...

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Tonofilament differentiation in human epidermis, isolation and polypeptide chain composition of keratinocyte subpopulations

Cited by 123 publications

References 21 publications

Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Expression of keratin K14 in the epidermis and hair follicle: insights into complex programs of differentiation.

Differentiation-dependent changes in the solubility of a 195-kD protein in human epidermal keratinocytes.

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