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Effect of Divalent Cations and Proteases on Skin Sulfhydryl Oxidase Activity
Author(s) -
Yamada Hiromichi,
Takamori Kenji,
Ogawa Hideoki
Publication year - 1987
Publication title -
the journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.9
H-Index - 65
eISSN - 1346-8138
pISSN - 0385-2407
DOI - 10.1111/j.1346-8138.1987.tb03563.x
Subject(s) - chemistry , divalent , trypsin , enzyme , proteases , elastase , biochemistry , plasmin , cathepsin , enzyme assay , chelation , chymotrypsin , egta , calcium , inorganic chemistry , organic chemistry
Abstract Crude skin sulfhydryl oxidase was independently isolated from the living cell layer, the granular cell layer, and the lower living cell layer (spinous and basal) of cow snout. The properties of this enzyme were subsequendy investigated. The addition of 1 mM CuCl 2 and FeCl 2 stimulated the enzyme activity to 216% and 166% of the initial activity, respectively. Neither CaCl 2 nor MgCl 2 had much effect on the activity, and ZnCl 2 inhibited it. Diethyldithiocarbamate (DEDTC), a copper ion chelating agent, inhibited the activity in a dose and pre‐incubation time‐dependent manner: however, other divalent cation chelators such as EDTA, EGTA, o‐phenanthrolin and α,α'‐dipyridyl did not have any effect on the enzyme's behavior. From these findings, it was determined that Cu 2+ was essential for the activity of skin sulfhydryl oxidase. This enzyme was stimulated to 130–150% of its initial activity by treatment with 1 mg/ml trypsin, chymotrypsin or urokinase but was not affected by plasmin, elastase or cathepsin D. Trypsin treatment enhanced the activity in a dose and treatment‐time dependent manner. Skin sulfhydryl oxidase from the lower living cell layer (spinous and basal) was more highly activated by trypsin treatment than was that from the granular cell layer. These findings suggest that this enzyme may be activated by some kind of serine proteases during the keratinocytes autolysis process in the granular cell layer.