ABSTRACT
OBJECTIVE: To investigate the question of whether supplementation with an oral oil formulation rich in natural stable fish oil can alter skin elasticity, transepidermal water loss (TEWL), and skin roughness in healthy women. METHODS: Twenty-four healthy women aged 40-60 years participated in a single-blind randomized trial for testing the effect of a proprietary oral supplement for skin nutrition (Eskimo Skin Care) on skin elasticity, TEWL, and skin roughness. Skin elasticity was measured by an optical cutometer, TEWL by a water-loss module based upon the vapour gradient principle, and skin roughness with a three-dimensional microtopography imaging system. RESULTS: Skin elasticity increased by 10% after 3 months of treatment with the supplement, a statistically significant increase in comparison with the control group (p=0.0298). There was a trend, though not statistically significant, towards a positive influence on the skin's barrier function. No effect on the skin roughness was observed. CONCLUSION: Eskimo Skin Care, an oral preparation rich in natural stable fish oil, can improve skin elasticity.
Subject(s)
Dietary Supplements , Fatty Acids, Omega-3/pharmacology , Skin/drug effects , Administration, Oral , Adult , Elasticity/drug effects , Fatty Acids, Omega-3/administration & dosage , Female , Humans , Middle Aged , Pilot Projects , Water Loss, Insensible/drug effectsABSTRACT
The human MOCS3 protein contains an N-terminal domain similar to the Escherichia coli MoeB protein and a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 is proposed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin (MPT) synthase during Moco biosynthesis in humans. Recent studies have shown that the MOCS3 rhodanese-like domain (MOCS3-RLD) catalyzes the transfer of sulfur from thiosulfate to cyanide and is also able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z. MOCS3-RLD contains four cysteine residues of which only C412 in the six amino acid active loop is conserved in homologous proteins from other organisms. ESI-MS/MS studies gave direct evidence for the formation of a persulfide group that is exclusively formed on C412. Simultaneous mutagenesis of the remaining three cysteine residues showed that none of them is involved in the sulfur transfer reaction in vitro. A disulfide bridge was identified to be formed between C316 and C324, and possible roles of the three noncatalytic cysteine residues are discussed. By ESI-MS/MS a partially gluconoylated N-terminus of the His6-tagged MOCS3-RLD was identified (mass increment of 178 Da) which resulted in a heterogeneity of the protein but did not influence sulfurtransferase activity.
Subject(s)
Coenzymes/biosynthesis , Metalloproteins/biosynthesis , Nucleotidyltransferases/biosynthesis , Nucleotidyltransferases/chemistry , Sulfides/chemistry , Sulfurtransferases/biosynthesis , Sulfurtransferases/chemistry , Thiosulfate Sulfurtransferase/chemistry , Amino Acid Sequence , Animals , Cysteine/chemistry , Cysteine/genetics , Disulfides/chemistry , Histidine/genetics , Humans , Mice , Molecular Sequence Data , Molybdenum Cofactors , Mutagenesis, Site-Directed , Nucleotidyltransferases/genetics , Peptide Mapping , Protein Structure, Tertiary , Pteridines , Sequence Homology, Amino Acid , Spectrometry, Mass, Electrospray Ionization/methods , Sulfhydryl Compounds/chemistry , Sulfurtransferases/genetics , Thiosulfate Sulfurtransferase/geneticsABSTRACT
Recent studies have identified the human genes involved in the biosynthesis of the molybdenum cofactor. The human MOCS3 protein contains an N-terminal domain similar to the Escherichia coli MoeB protein and a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. The MOCS3 protein is believed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C terminus of the smaller subunit of molybdopterin (MPT) synthase. The MOCS3 rhodanese-like domain (MOCS3-RLD) was purified after heterologous expression in E. coli and was shown to catalyze the transfer of sulfur from thiosulfate to cyanide. In a defined in vitro system for the generation of MPT from precursor Z, the sulfurated form of MOCS3-RLD was able to provide the sulfur for the thiocarboxylation of MOCS2A, the small MPT synthase subunit in humans. Mutation of the putative persulfide-forming active-site cysteine residue C412 abolished the sulfurtransferase activity of MOCS3-RLD completely, showing the importance of this cysteine residue for catalysis. In contrast to other mammalian rhodaneses, which are mostly localized within mitochondria, MOCS3 in addition to the subunits of MPT synthase are localized in the cytosol.
