A Novel Epidermal Cell Differentiation Inhibitor (EDIN): Purification and Characterization from Staphylococcus Aureus

Overview

Journal Biochem Biophys Res Commun

Publisher Elsevier

Specialty Biochemistry

Date 1990 Nov 30

PMID 2256941

Citations 23

Authors

M Sugai

T Enomoto

K Hashimoto

K Matsumoto

Y Matsuo

H Ohgai

Y M Hong

S Inoue

K Yoshikawa

H Suginaka

Affiliations

Soon will be listed here.

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.

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