Biochemical, Biomarker, and Behavioral Characterization of the Grn Mouse Model of Frontotemporal Dementia.

Heterozygous loss-of-function mutations in the progranulin gene (GRN) are a major cause of frontotemporal dementia due to progranulin haploinsufficiency; complete deficiency of progranulin causes neuronal ceroid lipofuscinosis. Several progranulin-deficient mouse models have been generated, including both knockout mice and knockin mice harboring a common patient mutation (R493X). However, the Grn mouse model has not been characterized completely.

Antisense oligonucleotides targeting the miR-29b binding site in the GRN mRNA increase progranulin translation.

Heterozygous GRN (progranulin) mutations cause frontotemporal dementia (FTD) due to haploinsufficiency, and increasing progranulin levels is a major therapeutic goal. Several microRNAs, including miR-29b, negatively regulate progranulin protein levels. Antisense oligonucleotides (ASOs) are emerging as a promising therapeutic modality for neurological diseases, but strategies for increasing target protein levels are limited.

Biochemical, biomarker, and behavioral characterization of the mouse model of frontotemporal dementia.

Heterozygous loss-of-function mutations in the progranulin gene () are a major cause of frontotemporal dementia due to progranulin haploinsufficiency; complete deficiency of progranulin causes neuronal ceroid lipofuscinosis. Several progranulin-deficient mouse models have been generated, including both knockout mice and knockin mice harboring a common patient mutation (R493X). However, the mouse model has not been characterized completely.

Targeting nonsense-mediated RNA decay does not increase progranulin levels in the Grn R493X mouse model of frontotemporal dementia.

A common cause of frontotemporal dementia (FTD) are nonsense mutations in the progranulin (GRN) gene. Because nonsense mutations activate the nonsense-mediated RNA decay (NMD) pathway, we sought to inhibit this RNA turnover pathway as a means to increase progranulin levels. Using a knock-in mouse model harboring a common patient mutation, we tested whether either pharmacological or genetic inhibition of NMD upregulates progranulin in these GrnR493X mice.

Influence of storage time and elevated ripening temperature on the chemical and sensory properties of white Cheddar cheese.

Aged cheese is an increasingly popular dairy product. One approach to reduce Cheddar cheese maturation time is by utilizing elevated temperature, despite potential problems including development of imbalanced or off-flavors and negative changes in texture. Therefore, the objective of this study was to evaluate the influence of elevated ripening temperature on chemical and sensory properties of aged white Cheddar cheese.

Discriminating aging and protein-to-fat ratio in Cheddar cheese using sensory analysis and a potentiometric electronic tongue.

The objectives of this study were to evaluate the flavor and taste attributes of full-fat Cheddar cheeses with different protein-to-fat ratios (PFR) over aging time using a descriptive sensory analysis panel and a consumer panel, and to correlate these attributes with instrumental parameters obtained by the potentiometric electronic tongue. Three Cheddar cheese formulations (PFR of 0.74, 0.

Enhanced functionality of pea-rice protein isolate blends through direct steam injection processing.

Direct steam injection (DSI) processing with pH adjustment was investigated to enhance the functionality of pea-rice protein isolate blends (PR). Protein slurries at concentration of 5%(w/w) of commercial pea and rice protein isolates in the ratio of 2:1(w/w) across a range of steam temperatures (66-107°C) and pH values (2-11) were studied. After DSI treatment, the PR were freeze-dried to obtain the final dry protein powder.

Influence of High-Pressure Processing at Low Temperature and Nisin on Listeria innocua Survival and Sensory Preference of Dry-Cured Cold-Smoked Salmon.

Unlabelled: Cold-smoked salmon (CSS) production lacks a validated kill step for Listeria monocytogenes. Although Listeria spp. are reduced by nisin or high-pressure processing (HPP), CSS muscle discoloration is often observed after HPP.

Use of Volatiles as Indicators of Lipid Oxidation in Muscle Foods.

Lipid oxidation has long been recognized as a leading cause of quality deterioration in muscle foods and is often the decisive factor in determining food product storage life. Lipid oxidation generates a number of products, including volatile compounds, which are the major contributors to the development of rancid off-flavors and odors. Over the years, methodologies have been developed to quantify lipid oxidation products in muscle foods.

ELISA for monitoring lipid oxidation in chicken myofibrils through quantification of hexanal-protein adducts.

The objectives of this study were to optimize a monoclonal competitive indirect enzyme-linked immunosorbent assay (CI-ELISA) for hexanal detection, optimize solubilization and alkylation procedures for the formation of hexanal-protein adducts, and compare the ability the CI-ELISA, thiobarbituric acid reactive substances assay (TBARS), and a solid-phase microextraction-gas chromatography-mass spectrometry (GC/MS-SPME) method for monitoring lipid oxidation in freeze-dried chicken protein. Freeze-dried myofibrils with added methyl linoleate (0.6 mmol/g of protein) were stored at 50 degrees C at two water activities (a(w) = 0.

Solid phase microextraction-gas chromatography for quantifying headspace hexanal above freeze-dried chicken myofibrils.

A method using solid phase microextraction (SPME) combined with gas chromatography/mass spectrometry (GC/MS) was developed and used to determine the oxidation of freeze-dried chicken myofibrils spiked with methyl linoleate. Freeze-dried chicken myofibrils were found to act as a significant reservoir for hexanal. Recovery of hexanal emissions from the headspace above spiked myofibrils was 95% using a 5 min sampling time, with a total analysis time of approximately 12 min/sample.

Gelation of chicken pectoralis major myosin and heat-denatured beta-lactoglobulin.

Thermal, rheological, and microstructural properties of myosin (1 and 2% protein) were compared to mixtures of 1% myosin and 1% heat-denatured beta-lactoglobulin aggregates (myosin/HDLG) and 1% myosin and 1% native beta-lactoglobulin (myosin/beta-LG) in 0.6 M NaCl and 0.05 M sodium phosphate buffer, pH 6.

Gelling properties of heat-denatured beta-lactoglobulin aggregates in a high-salt buffer.

Thermal denaturation, rheological, and microstructural properties of gels prepared from native beta-lactoglobulin (beta-LG) and preheated or heat-denatured beta-LG (HDLG) aggregates were compared. The HDLG was prepared by heating solutions of 4% beta-LG in deionized water, pH 7.0, at 80 degrees C for 30 min and then diluted to the desired concentration in 0.

Thermal Inactivation of Escherichia coli O157: H7, Salmonella senftenberg , and Enzymes with Potential as Time-Temperature Indicators in Ground Beef.

The USDA has established processing schedules for beef products based on the destruction of pathogens. Several enzymes have been suggested as potential indicators of heat processing. However, no relationship between the inactivation rates of these enzymes and those of pathogenic microorganisms has been determined.

Lactate Dehydrogenase Polyclonal Antibody Sandwich ELISA for Determination of Endpoint Heating Temperatures of Ground Beef.

An enzyme-linked immunosorbent assay (ELISA) for the protein marker lactate dehydrogenase (LDH) was developed to determine endpoint heating temperature (EPT) of ground beef. Ground beef was placed in 10 by 75 mm tubes and heated to temperatures between 62 and 74°C at 2°C intervals. Electrophoresis and immunoblotting of meat extracts indicated a decrease in the intensity of the LDH band as temperature was increased.

Lactate Dehydrogenase as Safe Endpoint Cooking Indicator in Poultry Breast Rolls: Development of Monoclonal Antibodies and Application to Sandwich Enzyme-Linked Immunosorbent Assay (ELISA).

A sandwich enzyme-linked immunosorbent assay (ELISA) was developed to detect lactate dehydrogenase (LDH) as a marker protein for verifying endpoint cooking of uncured poultry products. Monoclonal antibodies were prepared against chicken muscle LDH and used with rabbit polyclonal antibodies developed against turkey or chicken muscle LDH for capture and detection in the assay, respectively. Minimum assay detection limits for turkey and chicken muscle LDH were 1 ng/ml.