Document Detail

Hematoxylin-stainability of keratohyalin granules is due to the novel component, fibrinogen γ-chain protein.
MedLine Citation:
PMID:  20821224     Owner:  NLM     Status:  In-Process    
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.
Masae Takahashi; Yoshitaka Horiuchi; Tadashi Tezuka
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Publication Detail:
Type:  Journal Article     Date:  2010-09-07
Journal Detail:
Title:  Archives of dermatological research     Volume:  302     ISSN:  1432-069X     ISO Abbreviation:  Arch. Dermatol. Res.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-10-04     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8000462     Medline TA:  Arch Dermatol Res     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  679-84     Citation Subset:  IM    
Institute for Health Sciences, Tokushima Bunri University, Yamashiro, Tokushima, Tokushima, Japan.
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