This study aims to understand the fate and transport of per- and polyfluoroalkyl substances (PFAS) and inorganic fluoride (IF) at an undisclosed municipal wastewater treatment plant (WWTP) operating a sewage sludge incinerator (SSI). A robust statistical analysis characterized concentrations and mass flows at all WWTP and SSI primary influents/effluents, including thermal-treatment derived airborne emissions. WWTP-level net mass flows (NMFs) of total PFAS were not statistically different from zero.
View Article and Find Full Text PDFIn the U.S. menthol remains the sole permitted characterizing cigarette flavor additive in part because efforts to link menthol cigarette use to increased tobacco-related disease risk have been inconclusive.
View Article and Find Full Text PDFThe use of measured volatile organic chemical (VOC) concentrations in indoor air to evaluate vapor intrusion is complicated by (i) indoor sources of the same VOCs and (ii) temporal variability in vapor intrusion. This study evaluated the efficacy of utilizing induced negative and positive building pressure conditions during a vapor intrusion investigation program to provide an improved understanding of the potential for vapor intrusion. Pressure control was achieved in five of six buildings where the investigation program was tested.
View Article and Find Full Text PDFHybridoma (Larchmt)
April 2011
We describe here a novel IgG monoclonal antibody to erythroid-related factor (ERAF), also known as alpha hemoglobin stabilizing protein (AHSP) and eryththroid differentiation related factor (EDRF). Our antibody named PCE 5 is an IgG(1) kappa chain and is to the peptide sequence MVTVVE ranked highly in our active site analysis and binds with high affinity to ERAF.
View Article and Find Full Text PDFBackground: Treatment with riboflavin and ultraviolet (UV) light reduces the pathogens present in blood components. This study assessed changes to the coagulation proteins that had occurred during this treatment of fresh plasma units before freezing.
Study Design And Methods: Twenty fresh plasma units (230 +/- 30 mL) were treated by the Mirasol process (CaridianBCT Biotechnologies) and frozen within 8 hours of donation.
The human prion diseases, such as variant Creutzfeldt-Jakob disease (vCJD), are characterized by the conversion of the normal cellular prion protein (PrP(C)) into an abnormal disease associated form (PrP(Sc)). Monoclonal antibodies (MAbs) that recognize these different PrP isoforms are valuable reagents both in the diagnosis of these diseases and in prion disease research in general but we know of no attempts to raise MAbs against native human PrP(C). We immunized prion protein gene ablated (PrP(-/-)) mice with native human PrP(C) purified from platelets (pHuPrP) generating a predominantly IgG isotype anti-pHuPrP polyclonal antibody response in all mice.
View Article and Find Full Text PDFBackground: Four recent cases of transfusion-related transmission of variant Creutzfeldt-Jakob disease (vCJD) highlight the need to develop a highly sensitive and specific screening test to detect infectivity in the blood of asymptomatic infected individuals. Protein misfolding cyclic amplification (PMCA), a method for the amplification of minute amounts of disease-associated abnormal prion protein (PrP(Sc)) to readily detectable levels, could be incorporated into such a test provided that a suitable substrate source for routine use in human PMCA reactions can be found.
Study Design And Methods: With the use of seed sources from individuals with variant and sporadic CJD, the use of human platelets (PLTs) as a PMCA substrate source was evaluated.
Prion protein type and codon 129 genotype are thought to be major determinants of susceptibility and phenotype in human prion diseases. Using an in-vitro system (protein misfolding cyclic amplification) we have attempted to model human prion protein conversion using the abnormal prion protein associated with each of the major sporadic Creutzfeldt-Jakob disease subtypes, in substrates containing the normal cellular form of the prion protein of each of the three possible human PRNP codon 129 polymorphic genotypes. The prion protein type is converted with fidelity in these amplification reactions, but the efficiency of conversion depends both on the methionine/valine polymorphic status of the sporadic Creutzfeldt-Jakob disease seed and substrate homogenate, and on the abnormal prion protein type.
View Article and Find Full Text PDFBackground: There has recently been renewed interest in freezing platelets (PLTs) in dimethyl sulfoxide (DMSO) for the treatment of major traumatic injuries, especially in military situations. This study examined PLTs that were frozen in small volumes of 6 percent DMSO at -80 degrees C.
Study Design And Methods: Buffy coat-derived pooled leukoreduced PLT concentrates were frozen in 6 percent DMSO and stored at -80 degrees C.
Human prion diseases are characterized by the conversion of the normal host cellular prion protein (PrP(C)) into an abnormal misfolded form [disease-associated prion protein (PrP(Sc))]. Antibodies that are capable of distinguishing between PrP(C) and PrP(Sc) may prove to be useful, not only for the diagnosis of these diseases, but also for a better understanding of the molecular mechanisms involved in disease pathogenesis. In an attempt to produce such antibodies, we immunized mice with an aggregated peptide spanning amino acid residues 106 to 126 of human PrP (PrP106-126).
View Article and Find Full Text PDFBackground: A test is needed to identify blood donors who are in the preclinical phase of variant Creutzfeldt-Jakob disease (CJD). alpha-Hemoglobin stabilizing protein (AHSP; syn. ERAF, EDRF) transcript levels are reduced in the blood of mice incubating transmissible spongiform encephalopathy.
View Article and Find Full Text PDFExpert Opin Med Diagn
February 2008
Variant Creutzfeldt-Jakob disease (vCJD) is a transmissible neurodegenerative prion disease that continues to present a unique problem for medical diagnostics. Uncertainties remain over the prevalence of vCJD in the UK population and its incubation period in individuals of different genotypes. Although the infectious agent that causes vCJD is widely distributed in the peripheral tissues of patients and those carrying the disease, it does not provoke any host immune response that would be amenable to detection.
View Article and Find Full Text PDFInformation is lacking regarding efficiency of removal of circulating dendritic cells (DCs) by leucoreduction (LR) of blood. This is important since DCs may play a role in transporting abnormal prion, the likely infectious agent of variant Creutzfeldt-Jakob disease. In this study, we report development of a real-time polymerase chain reaction (RT-PCR) assay to quantify residual DCs in LR whole blood via measurement of selected messenger RNA (mRNA) markers.
View Article and Find Full Text PDFSensitive and specific detection of abnormal prion protein in blood could provide a diagnostic test or screening assay for animal and human prion diseases. Here, the application of an immunocapillary electrophoresis (ICE) method developed for sheep scrapie to brain, spleen and blood from patients with Creutzfeldt-Jakob disease (CJD) is described. The assay involves organic-solvent extraction, a competitive immunoassay using fluorescently labelled synthetic prion protein peptides and polyclonal antibodies specific for those sequences, and analysis by capillary electrophoresis using laser-induced fluorescence detection.
View Article and Find Full Text PDFBackground: Universal leukodepletion (LD) has been implemented in the United Kingdom to reduce the risk of transfusion-transmitted variant Creutzfeldt-Jakob disease. If LD causes microvesiculation of blood cells, however, potentially infectious membrane-associated prion could reach the final products.
Study Design And Methods: We have measured microvesicles (MV) derived from red cells (RBC-MV), platelets (PLT-MV), and white blood cells (WBC-MV) and cellular prion protein (PrP(c)) in blood components produced by four whole-blood, five RBC, three PLT, and two plasma LD filters and three plateletpheresis techniques.
Biochem Biophys Res Commun
September 2005
A method for the extraction and purification of PrP(C), in its native monomeric form, from outdated human platelet concentrates is described. Both calcium ionophore platelet activation and lysis in Triton X-100 were evaluated as methods for the extraction of soluble platelet PrP(C) in its monomeric form. Following platelet activation, the majority of released PrP(C) was detected as a disulphide linked high molecular weight complex, which under reducing conditions could be separated into what appear to be stable non-disulphide linked PrP dimers or PrP covalently linked to another as yet unidentified protein.
View Article and Find Full Text PDFBackground: A highly sensitive dissociation-enhanced lanthanide fluoroimmunoassay (DELFIA) and flow cytometry techniques have previously been developed and employed to characterize soluble cellular prion protein (PrP(c)) expression in whole blood and separated components from healthy adult blood donors. No previous studies with these techniques have evaluated the concentration and expression of PrP in the blood of patients with variant Creutzfeldt-Jakob disease (vCJD).
Study Design And Methods: For blood from vCJD patients, sporadic CJD (sCJD) patients, non-CJD neurological controls, and healthy adults, PrP(c) was measured by DELFIA and cell-associated PrP was measured by flow cytometry.
Analytical ultracentrifugation (AUC) provides first-principle hydrodynamic and thermodynamic information concerning the size, shape and interactions of macromolecules. The fundamental measurement needed in AUC is the macromolecular concentration as a function of radial position and time. Currently, the Beckman Coulter XLI analytical ultracentrifuge may be equipped with absorbance and refractive detectors, which provide complementary concentration determinations.
View Article and Find Full Text PDFThe neuronal prion protein (PrPC) is also expressed within peripheral tissues including human blood. The majority of blood PrPC is found within the plasma fraction. We hypothesized that the vascular endothelium could be a source of this PrPC.
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