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Fatty acids resources:

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Am J Respir Cell Mol Biol. 2002 Jun;26(6):731-8.
Subinhibitory bismuth-thiols reduce virulence of Pseudomonas aeruginosa.

Wu CL, Domenico P, Hassett DJ, Beveridge TJ, Hauser AR, Kazzaz JA.

CardioPulmonary Research Institute, Division of Pulmonary and Critical Care Medicine, Winthrop-University Hospital, SUNY School of Medicine at Stony Brook, Mineola, New York 11501, USA.

Pseudomonas aeruginosa is a common pathogen in mechanically ventilated patients and produces a wide array of virulence factors. Bismuth-thiols (BTs) are active in vitro against all bacterial lung pathogens, including P. aeruginosa. The objective of these studies was to examine the biochemical and morphologic effects of sublethal BT concentrations on P. aeruginosa and to evaluate virulence in cell culture. Bismuth-dimercaprol, at a fraction of the minimal inhibitory concentration, reduced alginate expression by 67% in P. aeruginosa, whereas subinhibitory bismuth-ethanedithiol (BisEDT) reduced alginate by 92% in P. syringae. BisEDT effects on lipopolysaccharide content and type III secreted cytoxins were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Subinhibitory BisEDT reduced cell-associated lipopolysaccharide, and inhibited processing of the secreted cytotoxic protein ExoU. BisEDT-induced outer membrane blebbing and aggregation of cytoplasmic material was noted in electron microscopy. Virulence of P. aeruginosa was assessed by adherence to epithelial cells and sensitivity to serum killing. BisEDT inhibited adherence of P. aeruginosa to 16HBE14o- cells by 28% and to a collagen matrix by 53%. BisEDT-treated bacteria were also 100-fold more sensitive to serum bactericidal activity. In summary, low BT concentrations affect P. aeruginosa in a variety of ways, the combination of which may help prevent or resolve respiratory tract infection.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12034573&dopt=Abstract

Am J Respir Cell Mol Biol. 2002 Jun;26(6):739-47.
Porcine surfactant protein D is N-glycosylated in its carbohydrate recognition domain and is assembled into differently charged oligomers.

van Eijk M, van de Lest CH, Batenburg JJ, Vaandrager AB, Meschi J, Hartshorn KL, van Golde LM, Haagsman HP.

Department of Biochemistry and Cell Biology, Graduate School of Animal Health, Faculty of Veterinary Medicine, Utrecht University, The Netherlands. m.vaneijet.uu.nl

Surfactant protein D (SP-D) belongs to a subgroup of mammalian collagenous Ca(2+)-dependent lectins known as the collectins. It is thought to play a significant role in the innate immune response against microorganisms within the lungs and at other mucosal surfaces. This report documents the isolation and characterization of SP-D purified from porcine lung lavage using mannan affinity chromatography and gel filtration. Ultrastructural analysis shows both dodecameric and higher order oligomeric complexes of SP-D. The molecular mass of monomeric porcine SP-D (50 kD) is larger than that of SP-D from humans (43 kD). The difference in mass is due to the presence of an Asparagine-linked glycosylation in the carbohydrate recognition domain of porcine SP-D, which is absent in SP-D of other species investigated so far. Analysis of this carbohydrate moiety indicates that it is a highly heterogeneous, complex type oligosaccharide which is sialylated. The heterogeneity of oligosaccharide sialylation results in the existence of many differently charged porcine SP-D isoforms. The removal of the carbohydrate moiety reduces the inhibitory effect of porcine SP-D on influenza A virus haemagglutination. Therefore, the carbohydrate moiety may influence interactions with pathogens.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12034574&dopt=Abstract

Neurology. 2002 May 28;58(10):1471-5.
Homocysteine, vitamin B6, and vascular disease in AD patients.

Miller JW, Green R, Mungas DM, Reed BR, Jagust WJ.

Department of Medical Pathology, University of California, Davis, School of Medicine, Sacramento 95817, USA. jwmillecdavis.edu

BACKGROUND: Cerebrovascular disease is a cause of dementia and is associated with elevated plasma levels of homocysteine. Patients with AD tend to have unexplained elevations of homocysteine concentrations vs healthy control subjects. Vitamin B(6) status, a potential determinant of plasma homocysteine, has not been characterized in patients with AD. OBJECTIVE: To investigate plasma homocysteine, vitamin B(6) status, and the occurrence of vascular disease in patients with AD. METHODS: Forty-three patients with AD and 37 control subjects without AD were studied for homocysteine, B vitamin status (folate, vitamin B(12), pyridoxal-5'-phosphate [PLP]), kidney function (creatinine), and thyroid function (thyroid-stimulating hormone, thyroxin). In addition, the presence of vascular disease was assessed by reviewing both medical histories and brain imaging data provided by CT and MRI. RESULTS: The OR for elevated plasma homocysteine (>12 micromol/L) was only 2.2 (not significant) for subjects with AD. In contrast, the OR was 10.0 (p = 0.03) for subjects with vascular disease (n = 26). The OR for low plasma PLP (<25 nmol/L) was 12.3 (p = 0.01) for patients with AD. No significant relationship was observed between vascular disease and PLP level or between plasma homocysteine and PLP concentrations. CONCLUSIONS: Elevated plasma homocysteine in patients with AD appears related to vascular disease and not AD pathology. In addition, low vitamin B(6) status is prevalent in patients with AD. It remains to be determined if elevated plasma homocysteine or low vitamin B(6) status directly influences AD pathogenesis or progression.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12034781&dopt=Abstract

Neurology. 2002 May 28;58(10):1541-3.
Juvenile Alexander disease with a novel mutation in glial fibrillary acidic protein gene.

Sawaishi Y, Yano T, Takaku I, Takada G.

Department of Pediatrics, Akita University School of Medicine, Japan. sawaished.med.akita-u.ac.jp

Early-onset (infantile) Alexander disease is associated with mutations in the glial fibrillary acidic protein (GFAP) gene and two hot spots correlate to the severe phenotype. No molecular mechanisms have been elucidated in late-onset (juvenile) Alexander disease. The authors report a novel GFAP mutation in a patient with juvenile Alexander disease. The authors discuss similar molecular mechanisms in another intermediate filament disease and propose a possible molecular pathogenesis in juvenile Alexander disease.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12034796&dopt=Abstract

Nucleic Acids Res. 2002 Jun 1;30(11):2453-9.
A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family.

Nikolskaya AN, Galperin MY.

National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.

Sequence analysis of bacterial genomes revealed a novel DNA-binding domain. This domain is found in several response regulators of the two-component signal transduction system, such as Pseudomonas aeruginosa AlgR, involved in the regulation of alginate biosynthesis and in the pathogenesis of cystic fibrosis; Clostridium perfringens VirR, a regulator of virulence factors, and in several regulators of bacteriocin biosynthesis, previously unified in the AgrA/ComE family. Most of the transcriptional regulators that contain this DNA-binding domain are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. We refer to it as the LytTR ('litter') domain, after Bacillus subtilis LytT and Staphylococcus aureus LytR response regulators, involved in regulation of cell autolysis. In addition to response regulators, the LytTR domain is found in combination with MHYT, PAS and other sensor domains.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12034833&dopt=Abstract

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