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Hematoxylin Stainable Epidermal Protein of the Newborn Rat
Author(s) -
Takahashi Masae,
Tezuka Tadashi
Publication year - 1989
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.1346-8138.1989.tb01245.x
Subject(s) - stratum corneum , polyclonal antibodies , antigenicity , microbiology and biotechnology , chemistry , epidermis (zoology) , tissue transglutaminase , guinea pig , biochemistry , biology , antibody , enzyme , anatomy , immunology , endocrinology , genetics
Based on the activity of transglutaminase, the change of antigenicity in situ of hematoxylin stainable protein (HSP) purified from 3‐day‐old rat epidermis and located on the cell membrane region of the stratum corneum was investigated by indirect immunofluorescent technique using a polyclonal antibody against hematoxylin stainable protein. Three different techniques were employed: (i) the skin section was incubated with a commercial guinea pig liver transglutaminase (GLT), (ii) the skin section was incubated with an epidermal extract of Tris‐HCl (EX), and (iii) the skin section was incubated with an epidermal extract of 1% Triton X‐100 (EXT). The sections incubated in Tris‐HCl or Triton X‐100 were used as controls. Each incubation was done both in the presence and absence of Ca 2+ ions. After these incubations, an indirect immunofluorescent technique using a polyclonal antibody was performed. In the presence of Ca 2+ ions, the specific fluorescence of the cell membrane region of the entire stratum corneum cells disappeared after the preincubation with GLT. That of the lower one third of the stratum corneum disappeared after the incubation with EXT. In contrast, in the absence of Ca 2+ ions, no preincubation with GLT, EX, or EXT showed any disappearance of the fluorescence anywhere in the stratum corneum. There was also no disappearance of the fluorescence in the control sections. These findings suggest that the antigenicity of HSP in situ could be lost by the activity of transglutaminase.