The Investment Case for Malaria Elimination in Thailand: A Cost-Benefit Analysis.

After a dramatic decline in the annual malaria incidence in Thailand since 2000, the Thai government developed a National Malaria Elimination Strategy (NMES) to end local malaria transmission by 2024. This study examines the expected costs and benefits of funding the NMES (elimination scenario) versus not funding malaria elimination programming (resurgence scenario) from 2017 to 2036. Two case projection approaches were used to measure the number of malaria cases over the study period, combined with a set of Thailand-specific economic assumptions, to evaluate the cost of a malaria case and to quantify the cost-benefit ratio of elimination.

The Morphology of Self-Assembled Lipid-Based Nanoparticles Affects Their Uptake by Cancer Cells.

The morphology of nanoparticles (NPs) has been presumed to play an important role in cellular uptake and in vivo stability. This report experimentally demonstrates such dependence by using two types of uniform-sized self-assembled lipid-based NPs, namely nanodiscs and nanovesicles, composed of identical lipid composition. The morphology is characterized by small angle neutron scattering, dynamic light scattering and transmission electron microscopy.

Photo activation of HPPH encapsulated in "Pocket" liposomes triggers multiple drug release and tumor cell killing in mouse breast cancer xenografts.

We recently reported laser-triggered release of photosensitive compounds from liposomes containing dipalmitoylphosphatidylcholine (DPPC) and 1,2 bis(tricosa-10,12-diynoyl)-sn-glycero-3-phosphocholine (DC(8,9)PC). We hypothesized that the permeation of photoactivated compounds occurs through domains of enhanced fluidity in the liposome membrane and have thus called them "Pocket" liposomes. In this study we have encapsulated the red light activatable anticancer photodynamic therapy drug 2-(1-Hexyloxyethyl)-2-devinyl pyropheophorbide-a (HPPH) (Ex/Em410/670 nm) together with calcein (Ex/Em490/517 nm) as a marker for drug release in Pocket liposomes.

Low-visibility light-intensity laser-triggered release of entrapped calcein from 1,2-bis (tricosa-10,12-diynoyl)-sn-glycero-3-phosphocholine liposomes is mediated through a type I photoactivation pathway.

We recently reported on the physical characteristics of photo-triggerable liposomes containing dipalmitoylphosphatidylcholine (DPPC), and 1,2-bis (tricosa-10,12-diynoyl)-sn-glycero-3-phosphocholine (DC(8,9)PC) carrying a photo agent as their payload. When exposed to a low-intensity 514 nm wavelength (continuous-wave) laser light, these liposomes were observed to release entrapped calcein green (Cal-G; Ex/Em 490/517 nm) but not calcein blue (Cal-B; Ex/Em 360/460 nm). In this study, we have investigated the mechanism for the 514 nm laser-triggered release of the Cal-G payload using several scavengers that are known specifically to inhibit either type I or type II photoreaction pathways.

Digital screening methodology for the directed evolution of transglycosidases.

Engineering of glycosidases with efficient transglycosidases activity is an alternative to glycosyltransferases or glycosynthases for the synthesis of oligosaccharides and glycoconjugates. However, the engineering of transglycosidases by directed evolution methodologies is hampered by the lack of efficient screening systems for sugar-transfer activity. We report here the development of digital imaging-based high-throughput screening methodology for the directed evolution of glycosidases into transgalactosidases.

Identification and characterization of a gamma-glutamyl transpeptidase from a thermo-alcalophile strain of Bacillus pumilus.

A gamma-glutamyltranspeptidase (GGT, E.C. 2.

Cloning, expression and characterization of a 46.5-kDa metallopeptidase from Bacillus halodurans H4 sharing properties with the pitrilysin family.

A 1242 base pair DNA fragment from Bacillus halodurans H4 isolated from alkaline sediments of Lake Bogoria (Kenya) coding for a potential protease was cloned and sequenced. The hexa-histidine-tagged enzyme was overexpressed in Escherichia coli and was purified in one step by immobilized-metal affinity chromatography (IMAC) on Ni-NTA resin. The protease (ppBH4) presents an inverted zincin motif, HXXEH, which defines the inverzincin family.

Physico-chemical and immunological properties and partial amino acid sequencing of a new metalloprotease: endoprotease Thr-N.

Previous studies have described the isolation of a new metalloprotease with a strict specificity for the amide bonds of peptide substrates having a threonine residue at the P1' position [Biochem. Biophys. Res.

Identification and primary characterization of specific proteases in the digestive juice of Archachatina ventricosa.

The profile of sedimentation on a 4-20% (w/v) linear sucrose gradient of the digestive juice of the mollusk Archachatina ventricosa revealed the presence of at least four specific proteases. A first peak, corresponding to a sedimentation coefficient of 3.9 S, contained two endoproteases that could be assayed, one with Leu-pNA and the other with Met-pNA.

A novel endopeptidase with a strict specificity for threonine residues at the P1' position.

An endopeptidase was purified from Archachatina ventricosa by chromatography on columns of gel filtration, DEAE-Sepharose and phenyl-Sepharose. The preparation was shown to be homogeneous by polyacrylamide gel electrophoresis and capillary electrophoresis. The purified enzyme displayed two protein bands on SDS-polyacrylamide gel electrophoresis with estimated molecular weights of 90,000 and 121,000.

Electrostatic interactions of the butyrylcholinesterase dimer of mucosal cells of rat intestine with glycosaminoglycans.

The G2 form of butyrylcholinesterase (BChE) of mucosal cells of rat intestine is a rare amphiphilic species, which is related to class II of acetylcholinesterase. Preliminary work indicated that the enzyme can bind heparin and suggested particular properties as compared to other BChEs. Ionic properties of the G2 form BChE were studied with different ionic exchangers.

Ultrastructural localization of butyrylcholinesterase in epithelial cells of rat intestine.

The present study reports the histochemical detection, at the ultrastructural level, of butyrylcholinesterase (BChE) in the epithelial cells of rat intestine. The enzyme activity was observed in the crypt cells as well as in the mature cells of the villi. Inside the enterocytes, BChE was seen in the reticulum cisternae, Golgi apparatus and lipid droplets.

Butyrylcholinesterase amphiphilic forms of the mucosal cells of rat intestine bind heparin.

Mucosal cells of rat intestine express amphiphilic monomer (G1) and dimer (G2) as well as hydrophilic tetramer (G4) of butyrylcholinesterase (BChE). After incubation with heparin (3 and 15 microM), amphiphilic G2 form showed decreased migrations in nondenaturing electrophoresis whereas in these conditions, the mobility of hydrophilic forms from rat and human serum BChEs was unchanged. Sucrose gradient sedimentation and chromatography performed on HPLC gel filtration and on heparin-Sepharose confirmed that amphiphilic G1 and G2 forms were able to bind heparin.

Reversal of the decline in breastfeeding in Peninsular Malaysia? Ethnic and educational differentials and data quality issues.

Data from the First and Second Malaysian Family Life Surveys in 1976 and 1988, respectively, are analyzed to examine long-term trends in breastfeeding in Peninsular Malaysia, educational and ethnic differences therein, and the quality of retrospective data on infant feeding. The steady decrease between the mid-1950's and mid-1970's in breastfeeding was reversed to become a nearly monotonic increase since 1975. Part of the change is attributable to the changing composition of the Malaysian population.

Butyrylcholinesterase from intestinal epithelial cells of quail, chick and duck: a comparative study during development.

1. Epithelial cells of avian intestine express non-specific cholinesterase (butyrylcholinesterase, BuChE) activity both in the embryo and adult animal. 2.

Amphiphilic forms of butyrylcholinesterase in mucosal cells of rat intestine.

The properties of a cholinesterase from mucosal cells of rat intestine have been characterized. The enzyme was identified as butyrylcholinesterase because it was more sensitive to iso-OMPA (IC50 = 1.0 x 10(-6) M) than to BW284C51 (IC50 = 5.

Behaviour of butyrylcholinesterase in the intestinal epithelial cells of starved and refed rats.

1. The activity and the molecular characteristics of butyrylcholinesterase were studied in the epithelial cells of the following intestinal segments: duodenum, jejunum, ileum, caecum and colon of starved and refed rats. 2.

Human intestine epithelial cell acetyl- and butyrylcholinesterase.

The epithelial cells of the human intestine exhibit a cholinesterase activity which is restricted to the apex of the villi. This activity displays a maximum in the colon and a minimum in the jejunum. Contrary to most of the studied vertebrates, the human cells present both acetylcholinesterase and butyrylcholinesterase activities, acetylcholinesterase being predominant in all the intestinal segments: duodenum, jejunum, ileum and colon.

Sex-related differences in the expression of chick enterocyte butyrylcholinesterase during embryonic and post-hatching development.

The butyrylcholinesterase activity of chick enterocytes was studied from day 15 in ovo up to day 90 after hatching. The activities detected in both sexes at the level of jejuno-ileum change in a parallel manner, but the activity is always higher in the female than in the male during embryonic development. After hatching, the differences are less apparent although the study of the enzyme distribution along the intestine showed sex-related variations, mainly at the level of the anterior and middle parts of jejuno-ileum in the young adult.

Embryonic and post-natal changes in activity and molecular forms of mucosal cell butyrylcholinesterase in chicken intestine.

The mucosal cells of the chicken intestine contain a cholinesterase activity essentially due to butyrylcholinesterase. The enzyme is present during embryonic and post-hatching development. The activity reaches a maximum value at day 19 in ovo and decreases prior to and after hatching up to day 4 ex ovo.

Effects of electrical stimulation on molecular forms of butyrylcholinesterase in denervated fast and slow latissimus dorsi muscles of newly hatched chicken.

The effects of denervation and direct electrical stimulation upon the activity and the molecular form distribution of butyrylcholinesterase (BuChE) were studied in fast-twitch posterior latissimus dorsi (PLD) and in slow-tonic anterior latissimus dorsi (ALD) muscles of newly hatched chicken. In PLD muscle, denervation performed at day 2 substantially reduced the rate of rapid decrease of BuChE specific activity which takes place during normal development, whereas in the case of ALD muscle little change was observed. Moreover, the asymmetric forms which were dramatically reduced in denervated PLD muscle were virtually absent in denervated ALD muscle at day 14.

Characterization of cholinesterase molecular forms in the mucosal cells along the intestine of the chicken.

The presence of a butyrylcholinesterase (BuChE, EC 3.1.1.

Acetylcholinesterase and butyrylcholinesterase in the gut mucosal cells of various mammal species: distribution along the intestine and molecular forms.

1. A cholinesterase activity was shown to be present in the homogenates of the gut mucosal cells from seven mammal species examined. 2.

Soluble form of acetylcholinesterase from rabbit enterocytes: comparison of its molecular properties with those of the plasma membrane species.

A soluble form of acetylcholinesterase was shown to be present in rabbit enterocytes. The enzyme was obtained from a high-speed supernatant (105,000 X g centrifugation) after homogenization of intestinal mucosa without detergent. It was shown to possess no obvious hydrophobic character and could be classified as a low-salt-soluble (LSS) acetylcholinesterase.

Presence and characterization of acetylcholinesterase in brush-border and basolateral membranes of rabbit enterocytes.

Acetylcholinesterase is found in the brush-border and basolateral membranes purified from rabbit enterocytes. The sedimentation coefficients of the enzymes solubilized from two types of membrane are identical (5.5 +/- 0.