title: Activation of bacterial ceramidase by anionic glycerophospholipids: possible involvement in ceramide hydrolysis on atopic skin by Pseudomonas ceramidase.
abstract: We have reported previously that the ceramidase from Pseudomonas aeruginosa AN17 isolated from a patient with atopic dermatitis requires detergents for hydrolysis of ceramide (Cer) [Okino, Tani, Imayama and Ito (1998) J. Biol. Chem. 273, 14368--14373]. In the present study, we report that some glycerophospholipids strongly activated the hydrolysis of Cer by Pseudomonas ceramidase in the absence of detergents. Among the glycerophospholipids tested, cardiolipin was most effective in stimulating hydrolysis of Cer followed by phosphatidic acid, phosphatidylethanolamine and phosphatidylglycerol, whereas phosphatidylcholine, lysophosphatidic acid and diacylglycerol were less effective. Interestingly, Staphylococcus aureus-derived lipids, which contain cardiolipin and phosphatidylglycerol as major lipid components, also strongly enhanced the hydrolysis of normal Cer, as well as the human skin-specific omega-hydroxyacyl Cer, by the enzyme in the absence of detergents. It was confirmed that several strains of P. aeruginosa, including AN17, secrete a significant amount of staphylolytic proteases to lyse S. aureus cells, resulting in the release of cardiolipin and phosphatidylglycerol. Since both P. aeruginosa and S. aureus are suspected of being present in microflora of atopic skin, we speculate that S. aureus-derived glycerophospholipids stimulate the hydrolysis of Cer in atopic skin by bacterial ceramidase.
authors.affiliation: Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581, Japan.
authors.forename: Katsuhiro
authors.initials: K
authors.lastname: Kita
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Sueyoshi
authors.forename: Nozomu
authors.initials: N
authors.lastname: Okino
authors.forename: Masanori
authors.initials: M
authors.lastname: Inagaki
authors.forename: Hideharu
authors.initials: H
authors.lastname: Ishida
authors.forename: Makoto
authors.initials: M
authors.lastname: Kiso
authors.forename: Shuhei
authors.initials: S
authors.lastname: Imayama
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakamura
authors.forename: Makoto
authors.initials: M
authors.lastname: Ito
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D002308:Cardiolipins / Q000494:pharmacology*; D055572:Ceramidases; D002518:Ceramides / Q000378:metabolism*; D003001:Cloning, Molecular; D003876:Dermatitis, Atopic / Q000378:metabolism* / Q000382:microbiology; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics; D020404:Glycerophospholipids / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D010714:Phosphatidylethanolamines / Q000494:pharmacology; D010715:Phosphatidylglycerols / Q000494:pharmacology; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism; D012867:Skin / Q000378:metabolism*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013329:Structure-Activity Relationship
chemical_list: D002308:Cardiolipins; D002518:Ceramides; D004791:Enzyme Inhibitors; D020404:Glycerophospholipids; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D011994:Recombinant Proteins; D000581:Amidohydrolases; D055572:Ceramidases