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diacylglycerol/кариес
Врската е зачувана во таблата со исечоци
Страница 1 од 23 резултати
Streptococcus mutans diacylglycerol kinase homologue: a potential target for anti-caries chemotherapy.
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Aciduricity is a major cariogenic characteristic of Streptococcus mutans, and various genes have been implicated in this ability of S. mutans. Sixteen S. mutans mutant strains, each defective in a different gene, were constructed and their aciduricity was assessed. Of the mutants, the diacylglycerol
Lack of promotion activity of diacylglycerol oil on 4-nitroquinoline 1-oxide induced carcinogenesis in the oral cavity of SD rats.
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A recent study using c-Ha-ras proto-oncogene transgenic (rasTg) rats demonstrated possible enhancing effects of diacylglycerol (DAG) on 4-nitroquinoline 1-oxide (4NQO) induced carcinogenesis of the tongue. To assess effects in their Sprague-Dawley back strain, a two-stage carcinogenesis study using
alpha-cyclodextrin extracts diacylglycerol from insect high density lipoproteins.
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alpha-Cyclodextrins are water-soluble cyclic hexamers of glucose units with hydrophobic cavities capable of solubilizing lipophiles. Incubating alpha-cyclodextrin with high density lipophorin from Manduca sexta or Bombyx mori resulted in a cloudy, turbid solution. Centrifugation separated a pale
Diacylglycerol kinase zeta attenuates pressure overload-induced cardiac hypertrophy.
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BACKGROUND
The Gaq protein-coupled receptor (GPCR) signaling pathway, which includes diacylglycerol (DAG) and protein kinase C (PKC), plays a critical role in the development of cardiac hypertrophy and heart failure. DAG kinase (DGK) phosphorylates DAG and controls cellular DAG levels, thus acting
Possible enhancing activity of diacylglycerol on 4-nitroquinoline 1-oxide induced carcinogenesis of the tongue in human c-Ha-ras proto-oncogene transgenic rats.
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1,2-diacylglycerol (1,2-DAG) is involved in cell proliferation as an activator of protein kinase C (PKC) and has been shown to stimulate growth of cancer cells, raising the possibility of a role in tumor promotion. Ingested DAG oil, containing 70% 1,3-DAG and 30% 1,2-DAG, is digested and considered
Suppressed histamine release from rat peritoneal mast cells by ultraviolet B irradiation: decreased diacylglycerol formation as a possible mechanism.
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This study was designed to investigate the effect of ultraviolet B (UVB) irradiation on mast cell functions. Purified mast cells obtained from rat peritoneal cavity were irradiated with UVB and subsequently exposed to a degranulator, compound 48/80, or the calcium ionophore A-23187. The amount of
PROTEIN STRUCTURE. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels.
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Insulin-induced gene 1 (Insig-1) and Insig-2 are endoplasmic reticulum membrane-embedded sterol sensors that regulate the cellular accumulation of sterols. Despite their physiological importance, the structural information on Insigs remains limited. Here we report the high-resolution structures of
A major role for phospholipase A2 in antigen-induced arachidonic acid release in rat mast cells.
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Cross-linking of IgE receptors by antigen stimulation leads to histamine release and arachidonic acid release in rat peritoneal mast cells. Investigators have reported a diverse distribution of [3H]arachidonate that is dependent on labelling conditions. Mast cells from rat peritoneal cavity were
Effects of protein and fat concentration in coproduct-based growing calf diets on adipogenic and lipogenic gene expression, blood metabolites, and carcass composition.
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Crossbred calves ( = 30; age = 95 ± 1.7 d; BW = 179 ± 18 kg) were fed 1 of 5 growing diets: 1) corn-based control, 2) low-fat, low-protein coproduct blend, 3) high-fat, low-protein coproduct blend, 4) low-fat, high-protein coproduct blend, and 5) high-fat, high-protein coproduct blend for 112 d
The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end.
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TRPC3 plays important roles in neuronal differentiation and immune cell maturation by mediating the cationic current in response to phospholipase C activation, Ca2+ depletion, and diacylglycerol stimulation. Here, we purified the TRPC3 channel using a glycosylated tetramer and observed the structure
1-Palmitoyl-2-linoleoyl-3-acetyl-rac-glycerol (PLAG) attenuates gemcitabine-induced neutrophil extravasation.
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Cancer patients treated with chemotherapy often experience a rapid decline of blood neutrophils, a dose-limiting side effect called chemotherapy-induced neutropenia. This complication brings about dose reductions or cessation of chemotherapy during treatment of cancer patients because a rapid
The turnover of molecular species of phosphatidylinositol in Ehrlich ascites tumor cells.
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It has been shown previously the 32Pi is incorporated into phosphatidylinositol 30 times faster than into the other phospholipids classes in Ehrlich ascites tumor cells, whereas [1-14C] glycerol is incorporated at almost the same rate (Waku, K., Nakazawa, Y. and MOri, W. (1976) J. Biochem. 79,
A phosphatidic acid-binding protein is important for lipid homeostasis and adaptation to anaerobic biofilm conditions in Pseudomonas aeruginosa.
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A quantitative Pseudomonas aeruginosa proteomics approach revealed increased abundance of the so-far uncharacterized protein PA3911 in anaerobic biofilms grown under conditions of the cystic fibrosis lung. Physiological relevance of ORF PA3911 was demonstrated, inter alia, using phenotype microarray
FAD-I, a Fusobacterium nucleatum Cell Wall-Associated Diacylated Lipoprotein That Mediates Human Beta Defensin 2 Induction through Toll-Like Receptor-1/2 (TLR-1/2) and TLR-2/6.
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We previously identified a cell wall-associated protein from Fusobacterium nucleatum, a Gram-negative bacterium of the oral cavity, that induces human beta defensin 2 (hBD-2) in primary human oral epithelial cells (HOECs) and designated it FAD-I (Fusobacterium-associated defensin inducer). Here, we
The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain.
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Protein kinase C is specifically activated by binding two membrane lipids: the second messenger, diacylglycerol, and the amino phospholipid, phosphatidylserine. This binding provides the energy to release an autoinhibitory pseudosubstrate from the active site. Interaction with these lipids recruits
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