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1.
BMC Pediatr ; 24(1): 343, 2024 May 17.
Article in English | MEDLINE | ID: mdl-38760698

ABSTRACT

BACKGROUND: The Modified Shuttle Test-Paeds (Paeds), a recently developed 10-meter Shuttle run test for aerobic capacity in children. This study aims to investigate the construct validity (known-group and convergent validity) and test-retest reliability of the recently developed test for cardiorespiratory fitness, the Modified Shuttle Test-Paeds (Paeds). METHODS: A total of 144 participants (6-12 y) were tested on the Paeds test, and 84 children were tested on the 20-meter Shuttle Run test (20 m-SRT) to assess construct validity. To evaluate test-retest reliability, 46 children were tested twice on the Paeds. RESULTS: No sex differences were found, but there was an age effect. A strong correlation was found between Paeds and the 20 m-SRT (rs=0.78, p < 0.001). The test-retest reliability was good (ICC 0.84; 95% CI 0.74-0.91). CONCLUSION: Paeds appears to be a reliable and valid tool for estimating cardiorespiratory fitness in typically developing children aged 6-12 years and has the advantages of being shorter, needing less space, not requiring pacing and being self-motivational. More studies are needed to assess whether children reach an aerobic steady state in three minutes and how much of the results of the Paeds test can be explained by the agility component of the task (turning and grasping or aiming a bean bag). For clinical use, psychometric properties should be studied in various patient groups (e.g., ADHD, DCD, and children with intellectual disabilities).


Subject(s)
Cardiorespiratory Fitness , Exercise Test , Humans , Child , Male , Female , Cardiorespiratory Fitness/physiology , Reproducibility of Results , Exercise Test/methods
2.
Biochim Biophys Acta ; 887(2): 133-41, 1986 Jul 11.
Article in English | MEDLINE | ID: mdl-3521747

ABSTRACT

For the study of the biosynthesis, processing and secretion of mucus glycoproteins in rat gastric mucous cells, antibodies were raised against purified gastric mucus glycoproteins and against deglycosylated gastric mucus glycoproteins. Indirect immunofluorescence analysis of gastric mucosa sections revealed that both antibodies specifically labelled the mucus glycoprotein-synthesizing cells in the gastric mucosa. Stomach segments were pulse-labelled with [35S]cysteine and chased for various times. The radioactively labelled (glyco)proteins were quantitatively immunoprecipitated and analyzed by SDS-polyacrylamide gel electrophoresis. Less than 3% of the total radioactivity incorporated in protein was found to be present in mucus glycoproteins. Antibodies raised against native mucus glycoproteins recognized only high-molecular-weight mucus glycoproteins, while the antibodies against deglycosylated glycoproteins also bound to probable precursor forms. The synthesis of mature mucus glycoproteins (Mr greater than 300 000) required about 90 min. After 3 h of chase, only a small portion of the pulse-labelled mucus glycoproteins had been secreted; the majority of the radioactive glycoproteins at that time was still associated with the tissue. Immature (glyco)proteins were not secreted into the medium.


Subject(s)
Gastric Mucosa/metabolism , Glycoproteins/biosynthesis , Mucus/metabolism , Animals , Chemical Precipitation , Fluorescent Antibody Technique , Immunosorbent Techniques , Male , Molecular Weight , Protein Processing, Post-Translational , Rats , Time Factors
3.
J Recept Res ; 4(1-6): 521-36, 1984.
Article in English | MEDLINE | ID: mdl-6098671

ABSTRACT

alpha-MSH-induced pigment dispersion in melanophores shows an absolute requirement for extracellular Ca2+. To localize Ca2+ sites involved in the mechanism of action of alpha-MSH we studied the effects of Ca2+ deprivation on alpha-MSH and forskolin-induced melanophore responses. In an in vitro melanophore system employing ventral tailfins of Xenopus tadpoles, melanophore responses were assayed in terms of pigment dispersion and the phosphorylation state of a 53 kDa melanophore-specific protein. In the same melanophore system alpha-MSH has been shown to specifically increase the phosphorylation of this 53 kDa protein. Forskolin induces a dose-dependent pigment dispersion (EC50 7 X 10(-7) M). In contrast to the dispersion induced by alpha-MSH forskolin-induced dispersion does not require extracellular Ca2+. Moreover, in a Ca2+-free medium melanophores with permanently activated MSH-receptors aggregate, but can be redispersed by the addition of forskolin. Forskolin increases 53 kDa phosphorylation in a dose-dependent manner. Maximal stimulation with forskolin (10(-5) M) is four-fold and equals maximal 53 kDa phosphorylation obtainable with alpha-MSH. The MSH-induced increase in 53 kDa phosphorylation is inhibited by Ca2+ deprivation, whereas the forakolin-induced increase is unaffected. Our results suggest that alpha-MSH and forskolin stimulate melanophores through a common pathway and confirm that cAMP is a second messenger in alpha-MSH action in this system. We conclude that the Ca2+ sites in the mechanism of alpha-MSH action on melanophores precede adenylate cyclase activation.


Subject(s)
Calcium/metabolism , Diterpenes/pharmacology , Melanocyte-Stimulating Hormones/pharmacology , Melanophores/drug effects , Skin Pigmentation/drug effects , Animals , Bucladesine/pharmacology , Colforsin , Cyclic AMP/pharmacology , Larva , Melanophores/metabolism , Phosphorylation , Xenopus laevis
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