Dyspepsia: A stepwise approach to evaluation and management.

Let a patient's age and specific symptoms steer your initial investigation. Consider treatment options beyond antibiotics for H pylori gastritis and PPIs.

Clinical evaluation of e-Quit worRx: a mobile app to enhance smoking cessation shared decision making in primary care.

Background: Smoking is the leading preventable cause of morbidity and mortality in the United States. Primary care providers (PCPs) have a unique opportunity to engage patients to quit smoking, but to be effective, clinicians must be able to personalize evidence-based interventions that are useful and appealing to patients in a time efficient manner. We pilot tested a novel iPad application (app), called e-Quit worRx™, designed to enhance patient-centered shared-decision making (SDM) about smoking cessation, with the primary goal of determining feasibility in primary care offices.

Challenges in the Development of e-Quit worRx: An iPad App for Smoking Cessation Counseling and Shared Decision Making in Primary Care.

Background: Smoking is the leading preventable cause of morbidity and mortality in the United States, killing more than 450,000 Americans. Primary care physicians (PCPs) have a unique opportunity to discuss smoking cessation evidence in a way that enhances patient-initiated change and quit attempts. Patients today are better equipped with technology such as mobile devices than ever before.

Diabetes in homeless persons: barriers and enablers to health as perceived by patients, medical, and social service providers.

The ways homelessness and diabetes affect each other is not well known. The authors sought to understand barriers and enablers to health for homeless people with diabetes as perceived by homeless persons and providers. The authors performed semistructured interviews with a sample of participants (seven homeless persons, six social service providers, and five medical providers) in an urban Midwest community.

The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.

Apolipoproteins are key structural elements of lipoproteins and critical mediators of lipid metabolism. Their detergent-like properties allow them to emulsify lipid or exist in a soluble lipid-free form in various states of self-association. Unfortunately, these traits have hampered high-resolution structural studies needed to understand the biogenesis of cardioprotective high-density lipoproteins (HDLs).

Purification of recombinant apolipoproteins A-I and A-IV and efficient affinity tag cleavage by tobacco etch virus protease.

The expression of recombinant apolipoproteins provides experimental avenues that are not possible with plasma purified protein. The ability to specifically mutate residues or delete entire regions has proven to be a valuable tool for understanding the structure and function of apolipoproteins. A common feature of many recombinant systems is an affinity tag that allows for straightforward and high-yield purification of the target protein.

Mass spectrometric determination of apolipoprotein molecular stoichiometry in reconstituted high density lipoprotein particles.

Plasma HDL-cholesterol and apolipoprotein A-I (apoA-I) levels are strongly inversely associated with cardiovascular disease. However, the structure and protein composition of HDL particles is complex, as native and synthetic discoidal and spherical HDL particles can have from two to five apoA-I molecules per particle. To fully understand structure-function relationships of HDL, a method is required that is capable of directly determining the number of apolipoprotein molecules in heterogeneous HDL particles.

Effect of intraperitoneal and intravenous administration of cholecystokinin-8 and apolipoprotein AIV on intestinal lymphatic CCK-8 and apo AIV concentration.

CCK and apolipoprotein AIV (apo AIV) are gastrointestinal satiety signals whose synthesis and secretion by the gut are stimulated by fat absorption. Intraperitoneally administered CCK-8 is more potent in suppressing food intake than a similar dose administered intravenously, but the reason for this disparity is unclear. In contrast, both intravenous and intraperitoneally administered apo AIV are equally as potent in inhibiting food intake.

A three-dimensional homology model of lipid-free apolipoprotein A-IV using cross-linking and mass spectrometry.

Human apolipoprotein A-IV (apoA-IV) is a 46-kDa exchangeable plasma protein with many proposed functions. It is involved in chylomicron assembly and secretion, protection from atherosclerosis through a variety of mechanisms, and inhibition of food intake. There is little structural basis for these proposed functions due to the lack of a solved three-dimensional structure of the protein by x-ray crystallography or NMR.

Enhanced placental cholesterol efflux by fetal HDL in Smith-Lemli-Opitz syndrome.

Previous studies from this laboratory have shown that maternal-derived cholesterol can be effluxed from trophoblasts to fetal HDL and plasma. We had the opportunity to study for the first time the ability of HDL and plasma from a fetus with the Smith-Lemli-Opitz syndrome (SLOS) to efflux cholesterol from trophoblasts. It was unclear whether cholesterol could be effluxed to fetuses with SLOS since lipoprotein levels are often very low.

Modulation of apolipoprotein A-IV lipid binding by an interaction between the N and C termini.

Apolipoprotein A-IV (apoA-IV) is a 376-amino acid exchangeable apolipoprotein made in the small intestine of humans. Although it has many proposed roles in vascular disease, satiety, and chylomicron metabolism, there is no known structural basis for these functions. The ability to associate with lipids may be a key step in apoA-IV functionality.

The biotin-capture lipid affinity assay: a rapid method for determining lipid binding parameters for apolipoproteins.

The lipid affinity of plasma apolipoproteins is an important modulator of lipoprotein metabolism. Mutagenesis techniques have been widely used to modulate apolipoprotein lipid affinity for studying biological function, but the approach requires rapid and reliable lipid affinity assays to compare the mutants. Here, we describe a novel method that measures apolipoprotein binding to a standardized preparation of small unilamellar vesicles (SUVs) containing trace biotinylated and fluorescent phospholipids.

Specific sequences in the N and C termini of apolipoprotein A-IV modulate its conformation and lipid association.

Apolipoprotein (apoA-IV) is a 376-residue exchangeable apolipoprotein that may play a number of important roles in lipid metabolism, including chylomicron assembly, reverse cholesterol transport, and appetite regulation. In vivo, apoA-IV exists in both lipid-poor and lipid-associated forms, and the balance between these states may determine its function. We examined the structural elements that modulate apoA-IV lipid binding by producing a series of deletion mutants and determining their ability to interact with phospholipid liposomes.