The Experts below are selected from a list of 234 Experts worldwide ranked by ideXlab platform
Guowang Xu - One of the best experts on this subject based on the ideXlab platform.
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metabolomic identification of potential Phospholipid biomarkers for chronic glomerulonephritis by using high performance liquid chromatography mass spectrometry
Journal of Chromatography B, 2007Co-Authors: Chang Wang, Sumin Zhao, Xin Lu, Guowang XuAbstract:Plasma Phospholipids metabolic profile of chronic glomerulonephritis was investigated using high performance liquid chromatography/mass spectrometry (LC/MS) and principal component analysis. The plasma samples of 18 patients with chronic glomerulonephritis, 17 patients with chronic renal failure (CRF) without renal replacement therapy and 18 healthy persons were collected and analyzed. It was found that combination of the LC/MS technique with PCA can be successfully applied to Phospholipid profile analysis. The results showed that primary chronic glomerulonephritis and CRF had Phospholipids metabolic abnormality. Nineteen Phospholipid species were identified as possible biomarkers in plasma samples of chronic glomerulonephritis and chronic renal failure. Moreover, the identification of the molecular structure of the potential Phospholipid markers was obtained by ESI-MS/MS experiment. It suggests that Phospholipids can be used as potential biomarkers on the progress of primary chronic glomerulonephritis.
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Metabolomic identification of potential Phospholipid biomarkers for chronic glomerulonephritis by using high performance liquid chromatography–mass spectrometry
Journal of Chromatography B, 2007Co-Authors: Chang Wang, Sumin Zhao, Xin Lu, Guowang XuAbstract:Plasma Phospholipids metabolic profile of chronic glomerulonephritis was investigated using high performance liquid chromatography/mass spectrometry (LC/MS) and principal component analysis. The plasma samples of 18 patients with chronic glomerulonephritis, 17 patients with chronic renal failure (CRF) without renal replacement therapy and 18 healthy persons were collected and analyzed. It was found that combination of the LC/MS technique with PCA can be successfully applied to Phospholipid profile analysis. The results showed that primary chronic glomerulonephritis and CRF had Phospholipids metabolic abnormality. Nineteen Phospholipid species were identified as possible biomarkers in plasma samples of chronic glomerulonephritis and chronic renal failure. Moreover, the identification of the molecular structure of the potential Phospholipid markers was obtained by ESI-MS/MS experiment. It suggests that Phospholipids can be used as potential biomarkers on the progress of primary chronic glomerulonephritis.
Thomas C Sudhof - One of the best experts on this subject based on the ideXlab platform.
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a single c2 domain from synaptotagmin i is sufficient for high affinity ca2 Phospholipid binding
Journal of Biological Chemistry, 1993Co-Authors: Bazbek Davletov, Thomas C SudhofAbstract:Abstract Synaptotagmin I is a Ca(2+)- and Phospholipid-binding protein of synaptic vesicles with an essential function in neurotransmission. Ca2+/Phospholipid binding by synaptotagmin I may be mediated by its C2 domains, sequence motifs that have been implicated in the Ca2+ regulation of a variety of proteins. However, it is currently unknown if C2 domains are sufficient for Ca2+/Phospholipid binding or if they even directly participate in Ca2+/Phospholipid binding. In order to address this question, we have studied the Ca2+/Phospholipid-binding properties of the first C2 domain of synaptotagmin I. Our results show that this C2 domain by itself binds Ca2+ and Phospholipids with high affinity (half-maximal binding at 4-6 microM free Ca2+) and exhibits strong positive cooperativity. The C2 domain is specific for negatively charged Phospholipids and for those divalent cations that are known to stimulate synaptic vesicle exocytosis (Ca2+ > Sr2+, Ba2+ > Mg2+). These studies establish that C2 domains can serve as independently folding Ca2+/Phospholipid-binding domains. Furthermore, the cation specificity and the cooperativity of Ca2+ binding by the C2 domain from synaptotagmin I support a role for this protein in mediating the Ca2+ signal in neurotransmitter release.
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A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/Phospholipid binding.
Journal of Biological Chemistry, 1993Co-Authors: Bazbek Davletov, Thomas C SudhofAbstract:Abstract Synaptotagmin I is a Ca(2+)- and Phospholipid-binding protein of synaptic vesicles with an essential function in neurotransmission. Ca2+/Phospholipid binding by synaptotagmin I may be mediated by its C2 domains, sequence motifs that have been implicated in the Ca2+ regulation of a variety of proteins. However, it is currently unknown if C2 domains are sufficient for Ca2+/Phospholipid binding or if they even directly participate in Ca2+/Phospholipid binding. In order to address this question, we have studied the Ca2+/Phospholipid-binding properties of the first C2 domain of synaptotagmin I. Our results show that this C2 domain by itself binds Ca2+ and Phospholipids with high affinity (half-maximal binding at 4-6 microM free Ca2+) and exhibits strong positive cooperativity. The C2 domain is specific for negatively charged Phospholipids and for those divalent cations that are known to stimulate synaptic vesicle exocytosis (Ca2+ > Sr2+, Ba2+ > Mg2+). These studies establish that C2 domains can serve as independently folding Ca2+/Phospholipid-binding domains. Furthermore, the cation specificity and the cooperativity of Ca2+ binding by the C2 domain from synaptotagmin I support a role for this protein in mediating the Ca2+ signal in neurotransmitter release.
Hyunhee Jang - One of the best experts on this subject based on the ideXlab platform.
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functional and conformational modulation of human cytochrome p450 1b1 by anionic Phospholipids
Archives of Biochemistry and Biophysics, 2010Co-Authors: Hyunhee JangAbstract:We investigated the interaction of human P450 1B1 (CYP1B1) with various Phospholipid bilayers using the N-terminally deleted (Delta2-4)CYP1B1 and (Delta2-26)CYP1B1 enzymes. Among anionic Phospholipids, phosphatidic acid (PA) and cardiolipin specifically increased the catalytic activities, membrane binding affinities, and thermal stabilities of both CYP1B1 proteins when phosphatidylcholine matrix was gradually replaced with these anionic Phospholipids. PA- or cardiolipin-dependent changes of CYP1B1 conformation were revealed by altered Trp fluorescence and CD spectra. However, both PA and cardiolipin exerted more significant effects with the (Delta2-4)CYP1B1 than the (Delta2-26)CYP1B1 implying the functional importance of N-terminal region for the interaction with the Phospholipid membranes. In contrast, other anionic Phospholipids such as phosphatidylserine and the neutral Phospholipid phosphatidylethanolamine had no apparent effects on the catalytic activity or conformation of CYP1B1. These data suggest that the chemical and physical properties of membranes influenced by PA or cardiolipin composition are critical for the functional roles of CYP1B1.
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Functional and conformational modulation of human cytochrome P450 1B1 by anionic Phospholipids.
Archives of Biochemistry and Biophysics, 2009Co-Authors: Hyunhee JangAbstract:Abstract We investigated the interaction of human P450 1B1 (CYP1B1) with various Phospholipid bilayers using the N-terminally deleted (Δ2–4)CYP1B1 and (Δ2–26)CYP1B1 enzymes. Among anionic Phospholipids, phosphatidic acid (PA) and cardiolipin specifically increased the catalytic activities, membrane binding affinities, and thermal stabilities of both CYP1B1 proteins when phosphatidylcholine matrix was gradually replaced with these anionic Phospholipids. PA- or cardiolipin-dependent changes of CYP1B1 conformation were revealed by altered Trp fluorescence and CD spectra. However, both PA and cardiolipin exerted more significant effects with the (Δ2–4)CYP1B1 than the (Δ2–26)CYP1B1 implying the functional importance of N-terminal region for the interaction with the Phospholipid membranes. In contrast, other anionic Phospholipids such as phosphatidylserine and the neutral Phospholipid phosphatidylethanolamine had no apparent effects on the catalytic activity or conformation of CYP1B1. These data suggest that the chemical and physical properties of membranes influenced by PA or cardiolipin composition are critical for the functional roles of CYP1B1.
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lateral segregation of anionic Phospholipids in model membranes induced by cytochrome p450 2b1 bi directional coupling between cyp2b1 and anionic Phospholipid
Archives of Biochemistry and Biophysics, 2007Co-Authors: Hyunhee Jang, Ho Zoon ChaeAbstract:The lateral segregation of anionic Phospholipids phosphatidic acid (PA), phosphatidylinositol (PI), and phosphatidylserine (PS) was detected after addition of cytochrome P450 2B1 (CYP2B1). The tendency of lipid clustering was highly dependent on the type of anionic Phospholipids examined. PA was the most highly clustered while PI and PS clustered to a lesser degree. Moreover, liposomes containing anionic Phospholipids form anionic Phospholipid-rich microdomains in the presence of CYP2B1. Anionic Phospholipids (mostly notably PA) also increased the ability of CYP2B1 to bind to lipid monolayers. In addition to the ability of CYP2B1 to modulate the physical properties of the membrane, the membrane itself can have reciprocal effects on the activity and conformation of CYP2B1. The catalytic activity of CYP2B1 increased as a function of anionic Phospholipid concentration and in the presence of 10 mol% PA, the activity increased by 85%. These results suggest a bi-directional coupling between the CYP2B1 and anionic Phospholipids.
Chang Wang - One of the best experts on this subject based on the ideXlab platform.
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metabolomic identification of potential Phospholipid biomarkers for chronic glomerulonephritis by using high performance liquid chromatography mass spectrometry
Journal of Chromatography B, 2007Co-Authors: Chang Wang, Sumin Zhao, Xin Lu, Guowang XuAbstract:Plasma Phospholipids metabolic profile of chronic glomerulonephritis was investigated using high performance liquid chromatography/mass spectrometry (LC/MS) and principal component analysis. The plasma samples of 18 patients with chronic glomerulonephritis, 17 patients with chronic renal failure (CRF) without renal replacement therapy and 18 healthy persons were collected and analyzed. It was found that combination of the LC/MS technique with PCA can be successfully applied to Phospholipid profile analysis. The results showed that primary chronic glomerulonephritis and CRF had Phospholipids metabolic abnormality. Nineteen Phospholipid species were identified as possible biomarkers in plasma samples of chronic glomerulonephritis and chronic renal failure. Moreover, the identification of the molecular structure of the potential Phospholipid markers was obtained by ESI-MS/MS experiment. It suggests that Phospholipids can be used as potential biomarkers on the progress of primary chronic glomerulonephritis.
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Metabolomic identification of potential Phospholipid biomarkers for chronic glomerulonephritis by using high performance liquid chromatography–mass spectrometry
Journal of Chromatography B, 2007Co-Authors: Chang Wang, Sumin Zhao, Xin Lu, Guowang XuAbstract:Plasma Phospholipids metabolic profile of chronic glomerulonephritis was investigated using high performance liquid chromatography/mass spectrometry (LC/MS) and principal component analysis. The plasma samples of 18 patients with chronic glomerulonephritis, 17 patients with chronic renal failure (CRF) without renal replacement therapy and 18 healthy persons were collected and analyzed. It was found that combination of the LC/MS technique with PCA can be successfully applied to Phospholipid profile analysis. The results showed that primary chronic glomerulonephritis and CRF had Phospholipids metabolic abnormality. Nineteen Phospholipid species were identified as possible biomarkers in plasma samples of chronic glomerulonephritis and chronic renal failure. Moreover, the identification of the molecular structure of the potential Phospholipid markers was obtained by ESI-MS/MS experiment. It suggests that Phospholipids can be used as potential biomarkers on the progress of primary chronic glomerulonephritis.
Bazbek Davletov - One of the best experts on this subject based on the ideXlab platform.
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a single c2 domain from synaptotagmin i is sufficient for high affinity ca2 Phospholipid binding
Journal of Biological Chemistry, 1993Co-Authors: Bazbek Davletov, Thomas C SudhofAbstract:Abstract Synaptotagmin I is a Ca(2+)- and Phospholipid-binding protein of synaptic vesicles with an essential function in neurotransmission. Ca2+/Phospholipid binding by synaptotagmin I may be mediated by its C2 domains, sequence motifs that have been implicated in the Ca2+ regulation of a variety of proteins. However, it is currently unknown if C2 domains are sufficient for Ca2+/Phospholipid binding or if they even directly participate in Ca2+/Phospholipid binding. In order to address this question, we have studied the Ca2+/Phospholipid-binding properties of the first C2 domain of synaptotagmin I. Our results show that this C2 domain by itself binds Ca2+ and Phospholipids with high affinity (half-maximal binding at 4-6 microM free Ca2+) and exhibits strong positive cooperativity. The C2 domain is specific for negatively charged Phospholipids and for those divalent cations that are known to stimulate synaptic vesicle exocytosis (Ca2+ > Sr2+, Ba2+ > Mg2+). These studies establish that C2 domains can serve as independently folding Ca2+/Phospholipid-binding domains. Furthermore, the cation specificity and the cooperativity of Ca2+ binding by the C2 domain from synaptotagmin I support a role for this protein in mediating the Ca2+ signal in neurotransmitter release.
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A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/Phospholipid binding.
Journal of Biological Chemistry, 1993Co-Authors: Bazbek Davletov, Thomas C SudhofAbstract:Abstract Synaptotagmin I is a Ca(2+)- and Phospholipid-binding protein of synaptic vesicles with an essential function in neurotransmission. Ca2+/Phospholipid binding by synaptotagmin I may be mediated by its C2 domains, sequence motifs that have been implicated in the Ca2+ regulation of a variety of proteins. However, it is currently unknown if C2 domains are sufficient for Ca2+/Phospholipid binding or if they even directly participate in Ca2+/Phospholipid binding. In order to address this question, we have studied the Ca2+/Phospholipid-binding properties of the first C2 domain of synaptotagmin I. Our results show that this C2 domain by itself binds Ca2+ and Phospholipids with high affinity (half-maximal binding at 4-6 microM free Ca2+) and exhibits strong positive cooperativity. The C2 domain is specific for negatively charged Phospholipids and for those divalent cations that are known to stimulate synaptic vesicle exocytosis (Ca2+ > Sr2+, Ba2+ > Mg2+). These studies establish that C2 domains can serve as independently folding Ca2+/Phospholipid-binding domains. Furthermore, the cation specificity and the cooperativity of Ca2+ binding by the C2 domain from synaptotagmin I support a role for this protein in mediating the Ca2+ signal in neurotransmitter release.
