Diabetes self-management education exposure and glycated haemoglobin levels among Marshallese participants in a randomized controlled study.

AIMS: A randomized control trial (RCT) of diabetes self-management education (DSME), undertaken by a community-based participatory research (CBPR) partnership between the University of Arkansas for Medical Sciences (UAMS) and the Marshallese community in Arkansas. The RCT examined the effect of hours of intervention exposure, with the hypothesis that increased exposure is one reason the Adapted-Family DSME was found to be more effective than the Standard DSME. METHODS: Some 221 Marshallese with type 2 diabetes were randomized to an Adapted-Family DSME group (in-home setting) (n = 110) or a Standard DMSE group (community setting) (n = 111). The Adapted-Family DSME included 10 h of education that covered the core self-care elements recommended by the American Diabetes Association (ADA) and American Association of Diabetes Educators' (AADE) recommendations. The Standard DSME included 10 h of intervention with all ADA and AADE core elements. RESULTS: The number of hours of intervention exposure in the Adapted-Family DSME arm (mean = 8.0; median = 10.0) was significantly higher than the number of hours of intervention received in the Standard DSME arm (mean = 1.5; median = 0.0). As hypothesized, higher exposure was associated with a significant reduction in HbA1c in a model including only study arm and exposure (P = 0.01), and in a model including study arm, exposure, and all demographic variables (P = 0.046). CONCLUSIONS: This finding is consistent with previous reviews that showed increased exposure to DSME produced improved glycaemic control and ≥ 10 h of DSME produces clinically meaningful reductions in HbA1c .

Lipoproteins act as a reusable shuttle for lipid transport in the flying death's-head hawkmoth, Acherontia atropos.

High-density lipophorin (HDLp), the major insect plasma lipoprotein in resting insects, has been postulated to function as a 'reusable shuttle' for lipid transport between tissues, capable of accepting or depositing lipids with maintenance of the structural properties of the particle. Injection of differentially radiolabeled HDLp into resting death's-head hawkmoths revealed that disappearance of the [14C]palmitate labeled lipid component of HDLp (principally diacyglycerol) was relatively quickly (half-life approx. 3 h), whereas turnover time of the apolipoproteins (marked with [14C]protein hydrolysate) was considerably longer (half-life approx. 26 h). These results strongly support the above proposal. To fuel long-distance flight, insects transport lipid in the hemolymph in the form of diacylglycerol-rich low-density lipophorin (LDLp) resulting from a conversion of HDLp to LDLp. By injection of differentially radiolabeled LDLp into flying hawkmoths we demonstrate for the first time in vivo that this mechanism of lipoprotein conversion also functions as a 'reusable shuttle'. While half-life of the lipid moiety of LDLp labeled with [14C]palmitate or [14C]glycerol (mainly diacylglycerol) during flight was only 43 and 94 min, respectively, turnover rate of its apolipoprotein moiety was considerably lower (half-life approx. 30 h). The results demonstrate the unique role of HDLp, i.e., the reversible conversion to LDLp, in lipid delivery to insect flight muscles.

Binding of locust high-density lipophorin to fat body proteins monitored by an enzyme-linked immunosorbant assay.

Binding of locust high-density lipophorin (HDLp) to fat body proteins coated on immunoassay plates was studied using the ELISA method and ligand blotting techniques. HDLp binding proved to be correlated with the amount of fat body protein coated. From the concentration-dependent total HDLp binding an equilibrium dissociation constant could be calculated (Kd = 1.6 x 10(-8) M). Heparin inhibits the HDLp binding, indicating that positively charged groups are involved in the HDLp-fat body interaction. These groups were shown to be arginyl residues, as the arginine-specific treatment of HDLp by 1,2-cyclohexanedione resulted in a approximately 50% decrease in the binding ability of HDLp. HDLp binding is also affected by the pH. A decrease from pH 7.5 to pH 6.5 increases the binding affinity by approximately 250%. A monoclonal antibody specific for apolipophorin-II (apoLp-II) hampered the HDLp binding significantly, whereas a monoclonal anti-apoLp-I had no effect. Locust fat body HDLp binding proteins are highly specific for locust HDLp.

An insect lipoprotein hybrid helps to define the role of apolipophorin III.

Insects transport lipid for flight in the form of diacylglycerol-rich low density lipoproteins (low density lipophorin (LDLp)). A hybrid LDLp has been produced in vitro by using Locusta migratoria fat body, locust high density lipophorin, locust adipokinetic hormone, and Manduca sexta apolipophorin III (apoLp-III). The hybrid is similar in size and density to locust LDLp, contains several molecules of M. sexta apoLp-III, and lacks locust apoLp-III, as shown by immunochemical methods. Under the same conditions an apoLp-III from Thasus acutangulus is poorly incorporated into the locust lipoprotein. The role of apoLp-III as a recognition signal/activator of flight muscle lipoprotein lipase was assayed with labeled hybrid LDLp produced in vitro using M. sexta apoLp-III radiolabeled with 35S. In addition, hydrolysis of diacylglycerol was determined with lipid-labeled hybrid LDLp produced in vitro using [U-14C]glycerol incorporated into the diacylglycerol moiety. In vitro incubations of the labeled hybrid LDLp with L. migratoria flight muscles show that the lipase efficiently utilizes hybrid LDLp as a substrate and demonstrate that the carbohydrate moiety of locust apoLp-III (which is lacking in the M. sexta protein) is not required for interaction with the lipase. It also suggests that specific antigenic determinants of L. migratoria apoLp-III are not required for lipase activation since M. sexta apoLp-III lacks immunological cross-reactivity with L. migratoria apoLp-III.