Title
Kinetic characteristics of acidic and alkaline ceramidase in human epidermis
Author
Houben, E.
Uchida, Y.
Nieuwenhuizen, W.F.
de Paepe, K.
Vanhaecke, T.
Holleran, W.M.
Rogiers, V.
TNO Kwaliteit van Leven
Publication year
2007
Abstract
It has recently become evident that at least five ceramidase (CDase) isoforms are present in human epidermis, and that specifically acidic CDase (aCDase) and alkaline CDase (alkCDase) activities increase during keratinocyte differentiation, and thus might play a pivotal role(s) in permeability barrier function. Prior to investigating their possible roles in the epidermal barrier function, it is necessary to characterize basic kinetic parameters for these enzymes, as well as to determine the effects of the established CDase inhibitors and their activities. In this study, assays for both aCDase and alkCDase activities in fully differentiated human epidermis were optimized using a radiolabeled substrate. These studies revealed that aCDase activity is substantially higher than alkCDase activity, and that both isoenzymes are inhibited by a CDase inhibitor N-oleylethanolamine. These findings were also confirmed using an in situ enzyme assay. Copyright © 2007 S. Karger AG.
Subject
Nutrition
Food technology
Ceramidase
Epidermis
Kinetic parameters
acylsphingosine deacylase
enzyme inhibitor
ethanolamine derivative
isoenzyme
adult
article
enzyme activity
enzyme analysis
enzyme assay
enzyme inhibition
enzyme kinetics
enzyme substrate
enzymology
epidermis
female
human
human tissue
isoenzyme analysis
isotope labeling
normal human
nucleotide sequence
priority journal
zymography
Adult
Amidohydrolases
Enzyme Repression
Epidermis
Female
Humans
Hydrogen-Ion Concentration
Isoenzymes
Kinetics
Middle Aged
Skin Absorption
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DOI
https://doi.org/10.1159/000101388
TNO identifier
240021
ISSN
1660-5527
Source
Skin Pharmacology and Physiology, 20 (4), 187-194
Document type
article