title: A novel epidermal cell differentiation inhibitor (EDIN): purification and characterization from Staphylococcus aureus.
abstract: 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.
authors: Department of Microbiology, Hiroshima University School of Dentistry, Japan.
authors: M
authors: M
authors: Sugai
authors: T
authors: T
authors: Enomoto
authors: K
authors: K
authors: Hashimoto
authors: K
authors: K
authors: Matsumoto
authors: Y
authors: Y
authors: Matsuo
authors: H
authors: H
authors: Ohgai
authors: Y M
authors: YM
authors: Hong
authors: S
authors: S
authors: Inoue
authors: K
authors: K
authors: Yoshikawa
authors: H
authors: H
authors: Suginaka
mesh_terms: 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*
chemical_list: D000596:Amino Acids; D011506:Proteins