Urea-extractable Antigens in Normal, Benign, and Neoplastic Mouse Epidermis

Carruthers, Ch.

doi:10.1159/000224533

Cited by 7 publications

(4 citation statements)

References 5 publications

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“…The carcinomas appeared deficient in normal epidermal antigens [3], Similar observations were made employing antisera prepared against defatted homogenates of epidermis, papillomas, and carcinomas [2]. Recently, the antigens were studied by means of immunodiffusion in which the various antisera were adsorbed with the urea-extracted antigens of epidermis, papillomas, and carcinomas [1]. The results also demonstrated quantitative differences in the distribution of the urea-extractable antigens in normal, benign, and neoplastic mouse epidermis.…”

Section: Introductionmentioning

confidence: 60%

“…Procedures have been given previously for the following: (a) preparation of normal epidermis, methylcholanlhrene-induced epidermal hyperplasia, papillomas, and squamous-cell carcinomas of mice; (b) isolation of the urea-and alkali-extractable proteins of these tissues; and (c) preparation of the antisera raised against the various proteins in rabbits [1][2][3]. The IgG fractions were obtained from normal rabbit serum and from the antisera through precipitation by 50% saturation with (NH,)2S04, followed by DEAE-cellulose chromatography [6], Radioiodination2 3 * .…”

Section: Methodsmentioning

confidence: 99%

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Antigenic Differences between Normal Mouse Epidermis and Methylcholanthrene-Induced Squamous-Cell Carcinomas

Bhattacharaya¹,

Carruthers²

1972

Oncology

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IgG preparations were made from antisera raised against the urea- and alkali-extracted antigens of normal mouse epidermis and methyl- cholanthrene-induced squamous-cell carcinomas. Immunodiffusion in agar with thoroughly adsorbed IgG immuno- globulins showed that the urea- and alkali-extracted proteins of the carcinomas had antigens in common. Antigens in common were also found in the epidermal urea-and alkali-extracted proteins, but the antigens common to the carcinoma proteins were not identical with the antigens common to the epidermal proteins. Preparations of antibodies against epidermal and carcinoma urea-extracted proteins showed specific adsorption to epidermal and carcinoma sediments, respectively. There was no significant in vivo localization of ¹²⁵I-labeled antibodies against epidermal and carcinoma urea-extracted protein in spleen, kidney, liver, and epidermis in normal mice, or in spleen, kidney, liver, and carcinomas in carcinoma-bearing mice.

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Section: Introductionmentioning

confidence: 60%

Section: Methodsmentioning

confidence: 99%

Antigenic Differences between Normal Mouse Epidermis and Methylcholanthrene-Induced Squamous-Cell Carcinomas

Bhattacharaya¹,

Carruthers²

1972

Oncology

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“…Prekeratin or tonofilamentous protein are precursors to keratin, but their interrelationship remains to be demonstrated. The extraction procedures for either involve solubilization in urea or citric acid and fractionation by pH precipitation (Rudall, 1952(Rudall, , 1968Carruthers et al, 1955;Carruthers, 1970;Crounse, 1963; Matoltsy, 1965;Rothberg et al, 1965;Bernstein et al, 1970;Skerrow, 1972;Tezuka and Freedberg, 1972). chain contains 12 more tyrosine residues than does the heavy chain, suggesting that the light chain is not generated from the heavy chain.…”

mentioning

confidence: 99%

Two polypeptide chain constituents of the major protein of the cornified layer of newborn rat epidermis

Huang¹,

Stern²,

Clagett³

et al. 1975

Biochemistry

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The insoluble component of stratum corneum of rat epidermis yields two major bands after extraction with 8 M urea-mercaptoethanol-dithiothreitol. The ratio of these two bands is about 1:1 in terms of protein stain intensity and S-[14C]carboxymethyl label. Both polypeptides were purified to homogeneity by DE-52-cellulose, sodium dodecyl sulfate hydroxylapatite C column chromatography, and preparative DodSO4-polyacrylamide gel electrophoresis. The heavier polypeptide contains 30% alpha helix and the lighter contains 27% alpha helix as determined by circular dichroism studies. Both are sensitive to Pronase and resistant to trypsin, collagenase, and elastase. The lighter chain is stable to pepsin but the heavier can be partially degraded to a smaller polypeptide with a molecular weight similar to that of light chain. Amino acid analysis shows that the light chain contains 12 more tyrosine residues than does the heavy chain, suggesting that the light chain is not generated from the heavy chain. However, the two chains may have a common peptide region. Antiserum prepared against the heavier polypeptide can be completely absorbed by purified lighter polypeptide and vice versa indicating that both chains have some common antigenic determinants. Antibody against either chain can cross-react with the stratum corneum and keratohyalin granules in the epidermis of newborn rat as indicated by fluorescent microscopic observation. Similarly, this antibody also cross-reacts with the cell surface or the contents of spinous and granular cells, and very weakly with basal cells, indicating that the two proteins may be present in the lower strata as well as the stratum corneum.

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“…The nature of these antigenic differences was demonstrated by using thoroughly adsorbed antisera or IgG preparations raised in rabbits against the urea proteins of epidermis, papilloma, and carcinoma by (a) fluorescence microscopy [3,5,6]; (b) immunodiffusion in agar [I, 2,7]; and (c) the paired label technique using 13lI and 125I [I]. The 1 The author acknowledges the excellent technical assistance of Mrs. A. Heining and McKenna and Miss A. Baumler.…”

Section: Introductionmentioning

confidence: 99%

Differences in the Urea-Extracted or Fibrous Proteins of Mouse Epidermis at Various Stages of Malignant Transformation

Carruthers¹

1974

Oncology

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The urea-extractable proteins of normal and hyperplastic mouse epidermis, papilloma, and squamous-cell carcinoma were fractionated by gel filtration on Sepharose 4B to yield proteins which were excluded and retarded. The level of the proteins which were excluded decreased from normal epidermis through hyperplastic epidermis, papilloma, and carcinoma, whereas the retarded protein fractions increased proportionately. Ultra-centrifugation of these urea proteins resulted in gel and supernatant fractions, each of which accounted for approximately 50% of the total proteins for normal epidermis, papilloma, and carcinoma. The gel and supernatant fractions and the proteins which were excluded and retarded by Sepharose 4B were employed in immunodiffusion in agar against antisera or IgG fractions of antisera raised against the various urea proteins. These results showed that antigenic differences existed between the fibrous proteins of normal epidermis and papilloma or carcinoma, but the latter two tissues were antigenically similar with respect to these proteins.

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Urea-extractable Antigens in Normal, Benign, and Neoplastic Mouse Epidermis

Cited by 7 publications

References 5 publications

Antigenic Differences between Normal Mouse Epidermis and Methylcholanthrene-Induced Squamous-Cell Carcinomas

Antigenic Differences between Normal Mouse Epidermis and Methylcholanthrene-Induced Squamous-Cell Carcinomas

Two polypeptide chain constituents of the major protein of the cornified layer of newborn rat epidermis

Differences in the Urea-Extracted or Fibrous Proteins of Mouse Epidermis at Various Stages of Malignant Transformation

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