How do mobile health applications support behaviour changes? A scoping review of mobile health applications relating to physical activity and eating behaviours.

OBJECTIVE: The objective of this review was to analyse how researchers conducting studies about mobile health applications (MHApps) effectiveness assess the conditions of this effectiveness. STUDY DESIGN: A scoping review according to PRIMSA-ScR checklist. METHODS: We conducted a scoping review of efficacy/effectiveness conditions in high internal validity studies assessing the efficacy of MHApps in changing physical activity behaviours and eating habits. We used the PubMed, Web of Science, SPORTDiscus and PsycINFO databases and processed the review according to the O'Malley and PRISMA-ScR recommendations. We selected studies with high internal validity methodologies (randomised controlled trials, quasi-experimental studies, systematic reviews and meta-analyses), dealing with dietary and/or physical activity behaviours; covering primary, secondary or tertiary prevention and dealing with behaviour change (uptake, maintenance). We excluded articles on MHApps relating to high-level sport and telemedicine. The process for selecting studies followed a set protocol with two authors who independently appraised the studies. RESULTS: Twenty-two articles were finally selected and analysed. We noted that the mechanisms and techniques to support behaviour changes were poorly reported and studied. There was no explanation of how these MHApps work and how they could be transferred or not. Indeed, the main efficacy conditions reported by authors refer to practical aspects of the tools. Moreover, the issue of social inequalities was essentially reduced to access to the technology (the shrinking access divide), and literacy was poorly studied, even though it is an important consideration in digital prevention. All in all, even when they dealt with behaviours, the evaluations were tool-focused rather than intervention-focused and did not allow a comprehensive assessment of MHApps. CONCLUSION: To understand the added value of MHApps in supporting behaviour changes, it seems important to draw on the paradigms relating to health technology assessment considering the characteristics of the technologies and on the evaluation of complex interventions considering the characteristics of prevention. This combined approach may help to clarify how these patient-focused MHApps work and is a condition for improved assessment of MHApps in terms of effectiveness, transferability and scalability.

The influence of professional factors in determining primary school teachers' commitment to health promotion.

The objectives of the study were to identify the professional issues that teachers perceived as important in their commitment to a health promotion (HP) programme launched in their schools and to understand their perceptions of the impact of the programme on themselves as professionals, individuals, on students, on school staff and on the relationship with students' families. A mixed methods design was used. An anonymous questionnaire was distributed to 54 participating teachers exploring their practices and perceptions of the programme and 26 semi-structured interviews were conducted which examined their professional commitment to the programme. The main factors that teachers identified as shaping their commitment were (1) their perceptions of the programme, specifically, its congruence with their own role and practice and also their perceived impact of the programme upon whole staff relations and (2) the specific school environment including school organization, quality of the relationships with parents and student behaviour. If HP programmes are to be successfully developed in schools, it is necessary to anchor them within the schools' mission. HP programmes need to make sense to teachers' educational perspectives. They need to be responsive to school needs. They also need to be cognisant of the internal tensions that programme implementation can engender among the whole staff, some of whom may be committed to HP in their school, while others, may not value HP in the same way. Therefore, implementation processes that are respectful of the challenges schools encounter and of the differing ontological perspectives that teachers may hold with regard to HP is important.

[Targeted screening of COPD in primary care: Feasibility and effectiveness]. / Détection précoce de la BPCO en soins primaires : un essai contrôlé randomisé.

INTRODUCTION: Chronic obstructive pulmonary disease (COPD) is a common but under-diagnosed pathology in primary care. The objective was to study the feasibility of a randomized controlled trial in general practice to detect new cases of COPD at an earlier stage. METHODS: A cluster randomized, controlled, multicenter intervention study comparing, according to a 2×2 factorial plan, two case finding strategies: a systematic GOLD-HAS hetero-questionnaire and coordination of the patient's path to facilitate access to spirometry. The PIL-DISCO pilot study took place in 2017. Patients between 40 and 80 years old, with no previous history of COPD, consulting their GP on a given day regardless of the reason, were included. RESULTS: 176 patients were included in 1.5 days. Spirometry was performed in none of the control arm, in 13 (29.5%) of the questionnaire arm, in 22 (50%) in the coordination arm and in 32 (72.7%) with the combination of the two strategies. Two cases of stage 2 COPD and thirteen other respiratory diseases were diagnosed. CONCLUSIONS: This study confirms the feasibility of the protocol in primary care in terms of speed of inclusion and acceptability. An extension phase aiming to include 3200 patients will assess the diagnostic value of the two strategies tested in general practice.

Stabilization of a semiconductor disk laser using an intra-cavity high reflectivity grating.

We demonstrate the use of a High Reflectivity Grating (HRG) as an intra-cavity element in a Semiconductor Disk Laser (or Vertical External Cavity Surface Emitting Laser) to stabilise its emission wavelength and polarization characteristics. Operation at 1058nm with up to 645mW of pump-limited output power and an M(2)~1.4 is achieved. We also show that this scheme permits tunable single-frequency operation.

Microchip-laser polarization control by destructive-interference resonant-grating mirror.

An output coupler comprising a resonant grating submirror monolithically associated with a standard multilayer submirror polarizes the emission of a Nd:YAG microchip laser linearly over its full emission bandwidth by intra-mirror destructive interference for the undesired polarization. A polarization extinction ratio of more than 25 dB is obtained up to 6.1microJ pulse energy. This passively Q-switched laser performance is almost identical to that of a gratingless non-polarized microchip laser. The design and fabrication of the resonant grating mirror are described.

Telomere dynamics, end-to-end fusions and telomerase activation during the human fibroblast immortalization process.

Loss of telomeric repeats during cell proliferation could play a role in senescence. It has been generally assumed that activation of telomerase prevents further telomere shortening and is essential for cell immortalization. In this study, we performed a detailed cytogenetic and molecular characterization of four SV40 transformed human fibroblastic cell lines by regularly monitoring the size distribution of terminal restriction fragments, telomerase activity and the associated chromosomal instability throughout immortalization. The mean TRF lengths progressively decreased in pre-crisis cells during the lifespan of the cultures. At crisis, telomeres reached a critical size, different among the cell lines, contributing to the peak of dicentric chromosomes, which resulted mostly from telomeric associations. We observed a direct correlation between short telomere length at crisis and chromosomal instability. In two immortal cell lines, although telomerase was detected, mean telomere length still continued to decrease whereas the number of dicentric chromosomes associated was stabilized. Thus telomerase could protect specifically telomeres which have reached a critical size against end-to-end dicentrics, while long telomeres continue to decrease, although at a slower rate as before crisis. This suggests a balance between elongation by telomerase and telomere shortening, towards a stabilized 'optimal' length.

The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies.

The inducible trimethylamine-N-oxide reductase which migrates on non-denaturing polyacrylamide gels with an RF of 0.22, has been purified from the soluble fraction of wild-type E. coli K12. The molecular weight of the purified enzyme estimated by molecular-sieve chromatography is about 230,000. It is composed of two subunits of molecular weight 110,000. Antiserum specific for the enzyme has been produced. Gel filtration on Sephadex G-200 of the soluble fraction gave two peaks of trimethylamine-N-oxide reductase, one with an Mr of 230,000 and an RF of 0.22, and another with an Mr of 120,000 and an RF of 0.36. Since the anti-trimethylamine-N-oxide reductase serum recognises the two forms and shows a single subunit with an Mr of 110,000, we conclude that in E. coli there is a single inducible trimethylamine-N-oxide reductase which can exist as a dimer or a monomer. Other immunological studies with anti-trimethylamine-N-oxide reductase serum on crude extracts prepared from cells grown in the absence of inducer showed that the constitutive trimethylamine-N-oxide reductase was not recognised by the antiserum. The same analyses carried out on a tor mutant (defective in the structural gene of the inducible enzyme) confirmed without ambiguity that the constitutive enzyme is immunologically distinct from the inducible enzyme. In the same way, using the anti-trimethylamine-N-oxide reductase serum, rocket immunoelectrophoresis analyses were able to show that the inducible apoenzyme is not regulated by the fnr gene product and that molybdate does not seem necessary for the synthesis or stabilisation of this enzyme.

Molybdenum cofactor: a compound in the in vitro activation of both nitrate reductase and trimethylamine-N-oxide reductase activities in Escherichia coli K12.

Nitrate reductase (nitrite: (acceptor) oxidoreductase, EC 1.7.99.4) and trimethylamine N-oxide reductase (NADH : trimethylamine-N-oxide oxidoreductase, EC 1.6.6.9) activities were reconstituted by incubation of the association factor FA (the putative product of the chlB gene) with the soluble extract of the chlB mutant grown anaerobically in the presence of trimethylamine N-oxide. When soluble extracts of the chlB mutant grown on 10 mM sodium tungstate, a molybdenum competitor, were used in complementation systems, no enzymatic reactivation was observed. Heated extracts of the parental strain 541 were shown to contain a thermoresistant molybdenum cofactor by their ability to reactivate NADPH-nitrate reductase activity in the nit1 mutant of Neurospora crassa. By complementation of parental strain heated extract with association factor FA and soluble extract of the chlB mutant grown in the presence of sodium tungstate, we were able to show for the first time that the molybdenum cofactor is an activator common to the in vitro reconstitution of both nitrate reductase and trimethylamine-N-oxide reductase activities.

Membrane reconstitution in chl-r mutants of Escherichia coli K 12. IX. Part played by phospholipids in the complementation process.

The supernatant extracts of the chl A and chl B mutants of Escherichia coli K 12, the phospholipids of which are labeled by growth in 32 P or [2- 3H]glycerol media, contain 20 times more radioactivity than the supernatant extract of the wild-type strain grown under the same conditions. We have observed that, after complementation, 80% of the radioactivity previously contained by Extracts A and B is incorporated into reconstituted particles. The chromatography of 3H-labeled Extract B on DEAE-cellulose and followed by gel filtration of radioactive fractions on Sephadex G-200 has shown that the phospholipids of Extract B are only bound to soluble proteins and not to fragments of membranes; it can be assumed that they have been solubilized in the form of a lipid-protein complex by cell breakage. When Extracts A and B are treated by phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) before being mixed together, an inhibition of the reconstitution of nitrate reductase activity which is proportional to the phospholipase C concentration and the length of treatment is observed. The analysis of lipids and phospholipids of particles (Peak I, Peak II and Peak III) formed during complementation and reconstituted nitrate reductase shows that their phospholipid contents (phosphatidylethanolamine, phosphatidylglycerol, diphosphatidylglycerol and phosphatidylserine) and especially that of Peak II (d equals 1.18) are closely related to that of native particles from the wild-type strain. These results allow one to propose a hypothesis explaining the mechanism involved in complementation.

Membrane reconstitution in chl-r mutants of Escherichia coli K 12. VIII. Purification and properties of the FA factor, the product of the chl B gene.

The isolation and purification of the product of the chl B gene of Escherichia coli K 12 from the chl A mutant have been attempted. The purified protein gives a single band in 10% sodium dodecylsulfate/polyacrylamide gel electrophoresis. The molecular weight is estimated to be 35 000. This protein, that we have named "FA factor", does not contain any lipid, has a strong tendency to lose its activity by polymerizing but can be kept in an active state when stored in buffer containing NaCl. The addition of purified FA protein to a soluble extract from the chl B mutant strain grown under anaerobiosis in the presence of nitrate initiates the "complementation reaction", i.e. the reconstitution of the nitrate reductase activity and the formation of particulate material similar to the native membrane with respect to the structure and enzymatic function. FA protein acts both on the rate of reconstitution and on the total amount of reconstituted enzyme. The complementation leads to the reconstitution of nonsedimentable nitrate reductase and to the formation of three types of particles of different buoyant densities (1.10, 1.18 and 1.23) the two lightest of which contain nitrate reductase. It is shown that FA factor is incorporated only into the particles of intermediate density. In vivo, this factor is located in the native membranes of chl A, chl C, chl D and wild-type strains, whatever the growth conditions, aerobiosis or anaerobiosis, and in the presence or absence of nitrate. Protein FA can be released from either of these membranes (native or reconstituted) by removing Mg-2+ or by subjecting Kaback's vesicles to mechanical treatments; in the case of 1.18-reconstituted particles and wild-type membranes, the release of FA protein does not exert any effect on the level of the nitrate reductase activity.

The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers.

We used an anti-trimethylamine-N-oxide reductase (EC 1.6.6.9) serum and different immunological techniques (Ouchterlony, rocket immunoelectrophoresis, immunoblotting) to show that dimethylsulphoxide (DMSO), tetrahydrothiophene 1-oxide (THTO) and pyridine N-oxide (PNO) were effective inducers of the inducible form of trimethylamine N-oxide reductase. We confirmed this genetically and biochemically using a strain in which phage MudII 1734 carrying lacZ was inserted into torA, the structural gene for inducible trimethylamine-N-oxide reductase. By subcellular fractionation and quantitation with rocket immunoelectrophoresis, we showed that the enzyme was principally localized in the periplasmic fraction. Constitutive trimethylamine-N-oxide reductase was localized in the membrane fraction and, like the inducible enzyme showed a broad specificity with respect to various compounds such as DMSO, THTO and PNO. Apart from their immunological properties, the two enzymes could be clearly differentiated by their temperature stability.

A common pathway for the activation of several molybdoenzymes in Escherichia coli K12.

Three molybdoenzymes, nitrate reductase, formate benzyl-viologen oxidoreductase and trimethylamine-N-oxide reductase which form part of different systems, have been studied in a parental strain of Escherichia coli K12. When the organism is grown in the presence of 10 mM tungstate, these three enzymes are present in an inactive form which may be activated in vivo by the addition of 1 mM sodium molybdate. The mixing of soluble fractions from chlA and chlB mutants grown under the appropriate conditions leads to the activation of nitrate reductase, formate benzyl-viologen oxidoreductase and trimethylamine-N-oxide reductase. The activation of each enzyme is maximal when the mutants are grown under conditions that lead to the induction of that enzyme in the wild-type strain. The employment of purified proteins, the association factor FA and the Protein PA, which are presumed to be the products of the chlA and chlB genes, has shown that these proteins are responsible for the activation of the three enzymes during the complementation process.

High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli.

Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxides, trimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat/Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.

A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli.

A biochemical and immunological study has revealed a new formate dehydrogenase isoenzyme in Escherichia coli. The enzyme is an isoenzyme of the respiratory formate dehydrogenase (FDH-N) which forms part of the formate to nitrate respiratory pathway found in the organisms when it is grown anaerobically in the presence of nitrate. The new enzyme, termed FDH-Z, cross reacts with antibodies raised to FDH-N and possesses a similar polypeptide composition to FDH-N. FDH-Z catalyses the phenazine methosulphate-linked formate dehydrogenase activity present in the aerobically-grown bacterium. FDH-Z and FDH-N exhibit distinct regulation. Like formate dehydrogenase N, formate dehydrogenase Z is a membrane-bound molybdoenzyme. With nitrate reductase it can catalyse electron transfer between formate and nitrate. Quinones are required for the physiological electron transfer to nitrate. It seems likely that like FDH-N, FDH-Z functions physiologically as a formate: quinone oxidoreductase.

Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution.

The periplasmic trimethylamine N-oxide (TMAO) reductase from the marine bacteria Shewanella massilia is involved in a respiratory chain, having trimethylamine N-oxide as terminal electron acceptor. This molybdoenzyme belongs to the dimethyl sulfoxide (DMSO) reductase family, but has a different substrate specificity than its homologous enzyme. While the DMSO reductases reduce a broad spectra of organic S-oxide and N-oxide compounds, TMAO reductase from Shewanella massilia reduces only TMAO as the natural compound. The crystal structure was solved by molecular replacement with the coordinates of the DMSO reductase from Rhodobacter sphaeroides. The overall fold of the protein structure is essentially the same as the DMSO reductase structures, organized into four domains. The molybdenum coordination sphere is closest to that described in the DMSO reductase of Rhodobacter capsulatus. The structural differences found in the protein environment of the active site could be related to the differences in substrate specificity of these enzymes. In close vicinity of the molybdenum ion a tyrosine residue is missing in the TMAO reductase, leaving a greater space accessible to the solvent. This tyrosine residue has contacts to the oxo groups in the DMSO reductase structures. The arrangement and number of charged residues lining the inner surface of the funnel-like entrance to the active site, is different in the TMAO reductase than in the DMSO reductases from Rhodobacter species. Furthermore a surface loop at the top of the active-site funnel, for which no density was present in the DMSO reductase structures, is well defined in the oxidized form of the TMAO reductase structure, and is located on the border of the funnel-like entrance of the active center.

99% efficiency measured in the -1st order of a resonant grating.

A resonant diffraction grating comprising a mirror, a dielectric layer and a high index corrugation at the layer-air interface is shown to exhibit off-Littrow the record diffraction efficiency of 99% in the -1st reflected order at 1064 nm wavelength thanks to the excitation of a leaky mode of the layer. Such high figure is obtained by a grating 5 to 10 times shallower than in current attempts to realize high efficiency all-dielectric gratings.

Complications following intravesical bacillus Calmette-Guerin treatment for bladder cancer: a case series of 22 patients.

BACKGROUND: Intravesical bacillus Calmette-Guerin (BCG) therapy is an effective and widely used treatment for superficial bladder carcinoma. Local complications are frequent whereas systemic complications are rare but can be serious, and their management is not well known. METHODS: We describe retrospectively the records of 22 patients treated in 3 infectious disease departments, for complications related to intravesical BCG therapy as treatment of bladder cancer. RESULTS: All the patients were male, with a median age of 68 years (range 56-88). Complications occurred after a median of 5 instillations (range 1-11) and were observed within 24 h following BCG instillation for 14 patients. Common symptoms were fever (n = 20), impaired general condition (n = 14), and shortness of breath (n = 7). Six patients had a systemic septic reaction leading to transfer into the intensive care unit for five of them. Lung infiltration was the most frequent presentation (n = 11). Mycobacterium bovis was isolated from only two patients, but histology showed the presence of a granuloma in nine patients. Antimycobacterial treatment was initialized in 17 patients; the outcome was favorable in 16 patients, with a median length of symptoms resolution of 22.5 days (range 5-425 days). Eleven patients received corticosteroids in addition to specific treatment and had a more rapid improvement. One patient died with disseminated BCGitis proved by biopsy. CONCLUSIONS: Complications following intravesical BCG therapy are rare but can be severe and fatal. Histology seems to be the method that contributes most in confirmation of the diagnosis. Antimycobacterial therapy is effective, and probably more efficient when combined with corticosteroids, but the regimen and duration of the treatment are not standardized.

The Ca2+- and reduced nicotinamide adenine dinucleotide phosphate-dependent hydrogen peroxide generating system is induced by thyrotropin in porcine thyroid cells.

Hydrogen peroxide (H2O2) is an essential electron acceptor for thyroid peroxidase-catalyzed iodination and coupling reactions. In the presence of iodide, its production is a limiting step in thyroid hormone biosynthesis. Several studies have demonstrated that the thyroid particulate fraction contains a Ca2+- and NADPH- dependent H@O@ generator (NADPH-O2:oxidoreductase), the so- called thyroid NADPH-oxidase. It has recently been demonstrated that cellular H2O2 release is under the tonic control of TSH in primary cultures of dog thyrocytes. The present study evaluates the effect of TSH on the thyroid NADPH-oxidase and cytochrome c reductase activities, two enzymes believed to be involved on H2O2 generation in the thyroid gland. There was almost no detectable NADPH-dependent H2O2 generator in the membranes of cells grown for 18 h without TSH. But cells grown in the presence of TSH (0.1 mU/ml) had a CA2+- and NADPH-dependent H2O2-generating activity that increased up to the third day in culture, as did the cell iodide organification capacity. This increase was also partially blocked by 12-O-tetradecanoylphorbol 13-acetate and cycloheximide. Forskolin and 8-bromo-cAMP both reproduced the action of TSH on the Ca2+- and NADPH-dependent H2O2 generator. In contrast, the thyroid NADPH-cytochrome c reductase activity in particles from control cells was similar to that of TSH-treated cells and was unaffected by forskolin or 12-O-tetradecanoylphorbol 13-acetate. These results suggest that NADPH-cytochrome c reductase activity is not regulated by TSH and, thus, reinforce the idea that this enzyme is not involved in thyroid H2O2 generation. On the other hand, the Ca2+- and NADPH-dependent H2O2 generator, so-called thyroid NADPH- oxidase, is induced by TSH through the cAMP cascade. Thus, it seems to be another marker of thyroid differentiation, in addition to thyroperoxidase and thyroglobulin, and could play a key role in thyroid hormone production.

Thyroid iodine organification defects: a case with lack of thyroglobulin iodination and a case without any peroxidase activity.

Two patients (G2, G3) with iodine organification defect were studied. The first patient (G2), a 25-year-old women with no clinical hypothyroidism, had had her goiter for 10 years; 62% of the thyroidal iodine was released by perchlorate indicating iodine organification defect. The thyroid tissue obtained at thyroidectomy contained a normal concentration of thyroid peroxidase (I2 formation from I-) when tested after solubilization of the enzyme by trypsin and digitonin treatment of the particulate material. 1. The enzymatic activity (G2-TPO) behaved on DEAE cellulose chromatography very differently from those of hog (P-TPO) or another human goiter peroxidase (G1-TPO) (Pommier, et al., J Clin Endocrinol Metab 39: 69, 1974): the molarity of elution was 2M NaCl instead of 0.15 mM. 2. Both P-TPO and G2-TPO catalyzed iodide peroxidation (I- leads to I2) but the Km (iodide) value for G2-TPO was much lower (2.3 x 10(-2) M) when compared with that of P-TPO (3.7 x 10(-3) M) or G1-TPO (3.5 x 10(-3) M). In addition, the optimum pH for this reaction differed markedly (pH 6.1 instead of 7.9). 3. G2-TPO was poorly efficient in catalyzing the oxidation of gaiacol to tetragaiacol. 4. G2-TPO was unable to perform the iodination of non-iodinated goiter thyroglobulin whatever the pH and the iodide concentration. 5. Thyroglobulin from this goiter (G2) was almost not iodinated (0.0014%), i.e., 0.07 atoms iodine/mole thyroglobulin), and its total content in the gland was very low (0.3-4 g/1000 g wet tissue instead of 25 g). A clear discrepancy was thus shown between the euthyroid state of this patient and the total lack of iodinating activity of the isolated peroxidase. The second patient (G3), a 17-year-old man with clinical hypothyroidism, had had his goiter for 5 years. 100% of the thyroidal iodine was released by perchlorate indicating a complete iodine organification defect. The thyroid tissue obtained at thyroidectomy contained no peroxidase activity when tested before and after treatment of the particulate material by trypsin and digitonin and even in the presence of hematin. Thyroglobulin from this goiter, which was almost non-iodinated (0.0014%), was present in normal amounts in the gland (congruent to 25 g/1000 g).

Ca2+ regulation of thyroid NADPH-dependent H2O2 generation.

A thyroid particulate fraction contains an NADPH-dependent H2O2-generating enzyme which requires Ca2+ for activity. A Chaps solubilized extract of the thyroid particulate fraction partially purified by DEAE chromatography did not show a dependence on Ca2+ for activity. Preincubation of the particulate fraction with Ca2+ yielded a preparation insensitive to Ca2+. The non-particulate fraction obtained after incubation of the particles in the presence of Ca2+ was able to inhibit, in the presence of EGTA, the Ca2+-desensitized particulate fraction and the enzyme isolated on DEAE. It is concluded that the reversible Ca2+ activation of the NADPH-dependent H2O2 generation was modulated in porcine thyroid tissue by (a) calcium-releasable inhibitor protein(s).