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HETEROGENEITY OF EPIDERMAL PREKERATIN AND KERATIN BETWEEN SOLE AND BODY SKIN IN HUMANS
Author(s) -
Kitajima Yasuo,
Furuta Hiroko,
Tsuneda Yoriko,
Yoneda Kazufumi,
Mori Shunji
Publication year - 1984
Publication title -
the journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.9
H-Index - 65
eISSN - 1346-8138
pISSN - 0385-2407
DOI - 10.1111/j.1346-8138.1984.tb01468.x
Subject(s) - stratum corneum , keratin , precipitin , polyacrylamide gel electrophoresis , biochemistry , chemistry , keratin 6a , epidermis (zoology) , molecular mass , microbiology and biotechnology , biology , cell , anatomy , intermediate filament , immunology , genetics , cytoskeleton , enzyme , antigen
Recently, heterogeneity of stratum corneum keratin (α‐fibrous protein) in various anatomic sites has been described in humans as well as cows and rats. In order to study this heterogeneity more clearly in humans, we compared acid soluble (citrate buffer at pH 2.65) prekeratin, acid insoluble (8 M urea‐2‐mercaptoethanol soluble) living cell keratin, and stratum corneum keratin from sole and body (nonsole‐nonpalm) skin using SDS‐polyacrylamide gel electrophoresis (PAGE), amino acid analysis, and immunological analyses. In prekeratin, no differences were seen between sole and body by SDS‐PAGE. Prekeratins from the two sources showed a 4‐band pattern with molecular weights of 55,000, 59,000, 62,000 and 69,000. In living cell keratin, the 69,000 band disappeared and a 49,000 band appeared in sole, but not in body epidermis. In stratum corneum keratin, a distinct difference was seen between sole and body skin. The sole stratum corneum keratin showed a 3‐band pattern (55,000, 59,000 and 62,000 mw) while that of body showed a two‐band pattern (59,000 and 66,000 mw). Despite the heterogeneity of the SDS‐PAGE profiles, no significant differences were seen in amino acid composition amongst these specimens. Immunologically, using double diffusion, antiserum against stratum corneum keratin from the sole principally produced two precipitin lines against the same keratin of sole origin and one precipitin line against prekeratin, living cell keratin, and stratum corneum keratin of body origin. This precipitin line fused with one of the two precipitin lines produced between antiserum and the sole stratum corneum keratin. These results indicate that anatomical‐site heterogeneity in α‐fibrous protein of human epidermis does not exist at the acid‐soluble prekeratin level, but does at the acid‐insoluble keratin level of living cell layer and stratum corneum when examined by SDS‐PAGE, and that some, but not all, keratin antigens are immunologically common between sole and body.