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11. Step‐counting accuracy of activity monitors in persons with Down syndrome.

Author

Bertapelli, F., Curtis, J. S., Carlson, B., Johnson, M., Abadie, B., and Agiovlasitis, S.

Subjects
LEG physiology, HIP joint physiology, WRIST physiology, ACCELEROMETERS, ACTIGRAPHY, AGE distribution, ANTHROPOMETRY, BODY weight, RESEARCH evaluation, SEX distribution, STATURE, PEDOMETERS, MEASUREMENT errors, DOWN syndrome, BODY mass index, LIFESTYLES, MEDICAL equipment reliability, WAIST circumference, WALKING speed
Abstract

Background: Accelerometers and pedometers have been used to monitor the number of steps. However, the evidence on the step‐counting accuracy of these devices – especially accelerometers – is limited in persons with Down syndrome (DS). This study therefore examined the accuracy of accelerometers placed on the hip or wrist and of a pedometer with a uni‐axial accelerometer mechanism in measuring steps in persons with DS and whether device error is associated with walking speed, height, weight, body mass index, waist circumference, leg length, age or sex. Method: Seventeen persons with DS (eight women and nine men; age 33 ± 15 years) walked over‐ground for 6 min at their preferred speed. The steps were measured with a hip‐worn and a wrist‐worn ActiGraph accelerometer using the manufacturer's default (DF) and low‐frequency extension (LFE) filters, and with the NL‐1000 New Lifestyles pedometer on the hip. Steps were also measured with hand tally which served as the criterion. Results: Absolute percent error was considerable and differed statistically between devices (P = 0.001); however, error improved for accelerometers when LFE was applied (Hip‐DF: 31.6 ± 18.8%; Hip‐LFE: 9.7 ± 12.8%; Wrist‐DF: 32.7 ± 14.2%; Wrist‐LFE: 13.6 ± 10.2%; Pedometer: 23.2 ± 22.8%). Bland–Altman plots indicated underestimation of steps for accelerometers and the pedometer. Application of LFE, however, improved the prediction of the accelerometers. The number of steps measured by the hip accelerometer with LFE and by the pedometer did not differ statistically from actual steps. Steps by the remaining methods were significantly lower than hand tally (P ≤ 0.001). Correlations between percent error for each device and walking speed, anthropometry, age or sex ranged between −0.28 and +0.48, and were non‐significant, except for age. Conclusions: The results demonstrated that the pedometer and ActiGraph accelerometers have considerable error in measuring steps of persons with DS. Application of LFE, however, significantly improved the step‐counting performance of the Actigraph accelerometers. [ABSTRACT FROM AUTHOR]

Published
2019
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32. Spontaneous and induced dome formation by two clonal cell populations derived from a human adenocarcinoma cell line, ht29

Author

Fantini, J., Abadie, B., Tirard, A., Remy, L., Ripert, J. P., Battari, A. El, and Marvaldi, J.

Abstract

The replacement of glucose by galactose in the culture medium resulted in partial structural and functional enterocytic differentiation of HT29 cells. In order to characterize populations of homogeneously differentiated HT29 cells we have selected two clonal cell lines HT29-D4 and HT29-D9 with the following functional and structural characteristics when grown in a galactose-containing medium: (1) the two clonal cell populations were permanently morphologically differentiated as shown by the presence of mature junctional complexes and a well-organized brush border (especially for HT29-D4 cells); (2) HT29-D4 and HT29-D9 cells were able to form domes early in confluency, which indicated a functional state of differentiation; (3) the process of differentiation was fully reversible when glucose was added to the culture medium. The induction of domes was investigated in these two cell populations and we demonstrated for the first time that proteolytic enzymes are potent inducers of dome formation. The architecture of domes either obtained spontaneously or induced by proteolytic enzymes was not maintained in the presence of ouabain (a specific inhibitor of the Na+/K+-ATPase). In conclusion, HT29-D4 and HT29-D9 cells can be maintained permanently in a differentiated state in a glucose-free medium and were able to form domes at confluency. The observation that proteolytic enzymes were able to induce dome formation can help in the comprehension of the mechanism involved in the establishment of the differentiated state.

Published
1986
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33. Evidence for an ectophosvitin kinase activity that phosphorylates a 123 kDa endogenous substrate on a human colonic adenocarcinoma cell (HT 29)

Author

Fantini J, Jean-Marc Muller, Abadie B, el Battari A, Marvaldi J, and Tirard A

Subjects
Molecular Weight, Colonic Neoplasms, Humans, Membrane Proteins, Adenocarcinoma, Phosphorylation, Protein Kinases, Cell Line, Substrate Specificity
Abstract

When HT 29 cells grown as a monolayer were incubated in a synthetic medium in presence of 0.1 microM [gamma 32P]-ATP, the radioactivity was incorporated predominantly into three major endogenous polypeptides of 123 kDa, 50 kDa and 46 kDa. The radioactive proteins could be detected as soon as 30 s after the addition of the labelled ATP. When exogenous substrates such as casein or phosvitin were added in the synthetic medium, these proteins became phosphorylated. The phosvitin-kinase activity was released in the culture medium following an incubation of the cells with phosvitin. Depletion of the enzymatic activity from the cell surface as well as competition between phosvitin and endogenous substrates led specifically to the inhibition of the 123 kDa polypeptide phosphorylation. At low density, endogenous phosphorylation increased with the cell number, whereas on the contrary it decreased at high cell density. We concluded that the surface of HT 29 cells expressed several protein kinase activities. We have characterized one of them as an ectophosvitin kinase which phosphorylated specifically a 123 kDa polypeptide and whose expression or accessibility varied according to cell density.

Published
1987

36. Étude des relations entre la structure et la fonction de l'alpha-amylase pancréatique de porc

Author

Marchis-Mouren, G., Pasero, L., Abadie, B., Prodanov, E., Marchis-Mouren, G., Pasero, L., Abadie, B., and Prodanov, E.

Abstract

Ces quelques lignes résumant des travaux récents et même non publiés permettent de faire le point.  L'étude de la structure de l’a-amylase de porc est en bonne voie. L'établissement de la structure tridimensionnelle de l'enzyme devrait, comme dans le cas du lysozyme, éclairer le mécanisme d'action au niveau moléculaire de l’a-amylase de porc.

Published
1980

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