Localization of Fluorescein-Labeled Antibodies of Epidermal Proteins in Normal and Malignant Squamous Epithelium2

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Abstract
Antisera were prepared in rabbits against mouse and human epidermal proteins and mouse squamous cell carcinoma proteins. The distribution of these proteins in mouse epidermis undergoing malignant transformation and in human cancers was determined with the fluorescein-labeled antibody technique. The urea- and alkali-extractable proteins of epidermis 4 days after the hair was plucked and squamous cell carcinomas of mice, human epidermis, and its extractable proteins all shared common antigenic determinants, but specificity of staining revealed differences. The epidermises of mice had antigens not detected in the carcinomas; these carcinomas were antigen-deficient in epidermal proteins. Squamous cell carcinomas of the tongue, larynx, floor of the mouth, and bronchus (lung) of man were stained intensely with the antisera prepared against (a) normal human epidermis, (b) the alkali-extractable proteins and tonofibrin of human epidermis, and (c) urea-extractable proteins of mouse squamous cell carcinomas. Malignant melanomas did not stain with any of these antisera. The antisera prepared against the various proteins stained the human and mouse squamous cell carcinomas but not distinctively. However, some of the antisera and, particularly, tonofibrin antisera stained some samples of human epidermis uniquely in that structures resembling the intercellular bridges became evident.

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