| Hematoxylin-stainability of keratohyalin granules is due to the novel component, fibrinogen γ-chain protein. | |
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MedLine Citation:
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PMID: 20821224 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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Hematoxylin-stainability of keratohyalin granules (KHG) using biochemical and immunohistochemical techniques is due to the presence of a fibrinogen γ-chain protein. A protein with a molecular weight of 100 kDa was stained with anti-Ted-H-1 monoclonal antibody and hematoxylin solution (hematoxylin-stainable protein). Since the amino acid sequence of the hematoxylin-stainable protein was to that of fibrinogen γ-chain protein, a peptide was synthesized and an antibody against the peptide was produced. This antibody reacted with the hematoxylin-stainable protein and fibrinogen γ-chain protein on immunoblot analysis and with KHG on immunohistochemical examination. Furthermore, a commercial anti-fibrinogen γ-chain protein antibody (Ab) also reacted with the hematoxylin-stainable protein as well as fibrinogen. In contrast, anti-fibrinogen β-chain protein Ab did not react with the hematoxylin-stainable protein. The fibrinogen γ-chain protein also stained with hematoxylin. These findings suggested that fibrinogen γ-chain protein may be a novel component protein of KHG and may induce the hematoxylin-stainability of KHG. |
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Authors:
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Masae Takahashi; Yoshitaka Horiuchi; Tadashi Tezuka |
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Publication Detail:
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Type: Journal Article Date: 2010-09-07 |
Journal Detail:
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Title: Archives of dermatological research Volume: 302 ISSN: 1432-069X ISO Abbreviation: Arch. Dermatol. Res. Publication Date: 2010 Nov |
Date Detail:
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Created Date: 2010-10-04 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8000462 Medline TA: Arch Dermatol Res Country: Germany |
Other Details:
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Languages: eng Pagination: 679-84 Citation Subset: IM |
Affiliation:
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Institute for Health Sciences, Tokushima Bunri University, Yamashiro, Tokushima, Tokushima, Japan. masaet@tokushima.bunri-u.ac.jp |
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