Highly-expressed S100A3, a calcium-binding protein, in human hair cuticle

Analyses on sodium dodecyl sulfate-polyacrylamide gel electrophoreses showed that the human hair cuticle extracts mainly consist of a 7-kDa component and keratin proteins. The S-carboxymethylation of the cuticle extracts made the 7-kDa band shift to the 15-kDa position. After electroblotting of the...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1312; no. 2; pp. 94 - 98
Main Authors Kizawa, Kenji, Uchiwa, Hideyo, Murakami, Umeji
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 13.06.1996
Subjects
Amino Acid Sequence
Calcium binding protein
Calcium-Binding Proteins - analysis
Calcium-Binding Proteins - chemistry
Cell Extracts - chemistry
Chromatography, High Pressure Liquid
Cuticle
Electrophoresis, Polyacrylamide Gel
Hair
Hair - chemistry
Humans
Immunoblotting
Microscopy, Fluorescence
Molecular Sequence Data
Molecular Weight
Peptides - chemistry
S100 Proteins
S100A3
Trypsin - metabolism
Hair
Fmoc, N-(9-fluorenyl)methoxycarbonyl
PVDF, polyvinylidene difluoride
SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoreses
FITC, fluorescein isothiocyanate
Cuticle
SCM, S-carboxymethyl
S100A3
MAP, multiple antigen peptide
Calcium binding protein
Online AccessGet full text

Cover

More Information
Summary:Analyses on sodium dodecyl sulfate-polyacrylamide gel electrophoreses showed that the human hair cuticle extracts mainly consist of a 7-kDa component and keratin proteins. The S-carboxymethylation of the cuticle extracts made the 7-kDa band shift to the 15-kDa position. After electroblotting of the S-carboxymethyl derivative, the membrane pieces carrying the 15-kDa band were treated with trypsin and the released peptides were separated by reverse-phased HPLC. Amino acid sequence analyses revealed that the peptides corresponded to the partial sequences deduced from human genome coding for S100A3, a cysteine-rich calcium binding protein. The anti S100A3 serum, prepared by immunizing a synthetic peptide antigen, reacted with the 7-kDa and 15-kDa bands in immunoblotting analyses. Immunofluorescence microscopy showed intense labeling to the cuticular layer with the anti S100A3 serum. These results indicated that S100A3 was highly expressed in the human hair cuticle.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0167-4889
0006-3002
1879-2596
DOI:10.1016/0167-4889(96)00023-7