Hematoxylin-stainability of keratohyalin granules is due to the novel component, fibrinogen γ-chain protein.
Arch Dermatol Res
; 302(9): 679-84, 2010 Nov.
Article
em En
| MEDLINE
| ID: mdl-20821224
ABSTRACT
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 ß-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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Pele
/
Fibrinogênio
/
Grânulos Citoplasmáticos
/
Dermatite Atópica
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article