A novel epidermal cell differentiation inhibitor (EDIN): purification and characterization from Staphylococcus aureus.
A factor inhibiting the calcium-induced terminal differentiation of cultured mouse keratinocytes was purified to homogeneity from the extracellular products of S. aureus E-1 and designated 'epidermal cell differentiation inhibitor' (EDIN). EDIN activity was sensitive to trypsin and heat-labile, suggesting that EDIN is a protein. EDIN gave a single band with a molecular weight of 27,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was found to be a single chain polypeptide, having an isoelectric point higher than 9. The N-terminal amino acid sequence of EDIN was determined as A-D-V-K-N-F-T-D-L. EDIN inhibited the differentiation of not only mouse but also human keratinocytes in culture.
Sugai
M
M
Department of Microbiology, Hiroshima University School of Dentistry, Japan.
Enomoto
T
T
Hashimoto
K
K
Matsumoto
K
K
Matsuo
Y
Y
Ohgai
H
H
Hong
Y M
YM
Inoue
S
S
Yoshikawa
K
K
Suginaka
H
H
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000831:Animals, Newborn; D002454:Cell Differentiation / Q000187:drug effects; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015603:Keratinocytes / Q000166:cytology* / Q000187:drug effects; D051379:Mice; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000472:pathogenicity*
D000596:Amino Acids; D011506:Proteins