A variety of studies has a need to estimate the amount and pattern of daily energy expenditure. To this end, a 3-day activity record was developed and is described. Every 15-min period over 3 days, including a weekend day, was qualified in terms of energy cost on a 1 to 9 scale corresponding to a range of 1.0 MET to 7.8 METs and higher. A reliability study of 61 subjects indicated a highly reproducible procedure as shown by an intraclass correlation of 0.96 for mean kcal of energy expenditure over 3 days. Repeatability was unchanged whether or not the hours of sleep were included in the record. Samples of 150 children and 150 adults were also drawn to investigate the relationship between energy expenditure, physical working capacity, and body fatness. Results support the hypothesis that mean energy expenditure per kg of body weight is significantly correlated with physical working capacity expressed per kg of body weight (r = 0.31; p less than 0.01). Mean energy expenditure per kg of body weight is negatively related to body fat (-0.08 less than or equal to r less than or equal to -0.13). It is concluded that the 3-day activity record is a procedure suitable to estimate energy expenditure in population studies.

Aims:  To evaluate the immunosuppressive properties of the exopolysaccharide (EPS) from high‐EPS producer Lactobacillus rhamnosus RW‐9595M on inflammatory cytokines produced by macrophages. Methods and Results:  The conditioned media (CM) were produced by macrophages treated with parental Lact. rhamnosus ATCC 9595 and its isogenic variant, the high‐EPS producer Lact. rhamnosus RW‐9595M, and the levels of TNF‐α, IL‐6, IL‐10 and IL‐12 were evaluated. Results revealed that CM from parental Lact. rhamnosus induced higher levels of TNF‐α, IL‐6 and IL‐12 but inhibited IL‐10 production, whereas its mucous variant induced low or no TNF‐α and IL‐6. Addition of purified EPS to macrophages treated with parental Lact. rhamnosus decreased the inflammatory cytokines and inhibited the metabolic activity of lymphocytes. The intermediate polysaccharide chains (16–30 units) produced by time‐controlled hydrolysis of EPS increased the IL‐10 produced by macrophages. Conclusions:  Polysaccharide chains of EPS induced immunosuppression by the production of macrophagic anti‐inflammatory IL‐10. Significance and impact of the Study:  These results indicate that the EPS from Lact. rhamnosus RW‐9595M may be useful as a new immunosuppressive product in dairy food.

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The three-dimensional structure of neuropeptide tyrosine (NPY) 13 -36, a specific Y2 receptor agonist, has been investigated by two-dimensional 'H-NMR spectroscopy in solution. Analysis of the doublequantum-filtered correlation spectroscopy (DQFCOSY), total correlation spectroscopy (TOCSY) and nuclear Overhauser enhancement spectroscopy (NOESY) spectra provided a complete assignment of the proton signals. The interproton connectivities observed in the NOESY spectra comprised 166 intraresidue and 95 interresidue distance ranges which were used as constraints for molecular modeling by distance geometry, simulated annealing and energy minimization. The optimal structures are characterized by a helical C-terminal fragment Leu30-Tyr36 and a wide loop from Leu17 to Ser22. The structure of NPY 13-36 is analogous to the structure of NPY under the same solvent conditions. Comparison with other reported Y2 agonists suggests that the helical Leu30-Tyr36 fragment is the most critical for activity.Keywords : neuropeptide tyrosine agonist ; three-dimensional structure; NMR; molecular modeling.Neuropeptide tyrosine or NPY is a 36-amino acid peptide belonging to a family of biologically active peptides which includes peptide YY (PYY) and pancreatic polypeptide (PP). NPY is widely distributed in both the central and peripheral nervous systems and produces a variety of effects especially on the feeding behavior, cardiovascular function and anxiety [ l , 21. Its structure is characterized by the presence of five tyrosine and of four proline residues concentrated in a N-terminal polyproline segment.NPY performs its varied biological functions through the interaction with distinct G-protein-coupled receptor subtypes. Responses to Pro34] The three-dimensional structure of NPY has been investigated by two-dimensional 'H-NMR spectroscopy [12-16) and molecular modeling based on the crystal structure of PP [17-191. All investigations agree on the general structure of NPY which is folded in its center forming a hairpin structure with the N-and C-terminal segments in close proximity. The N-terminal polyproline segment (residues 1 -13) is generally disordered and the C-terminal segment (residues 15 -36) is generally helical, [20-221 and 1,1,1,3,3,3-hexa-fluoro-2-('H2)propano1/20 mM aqueous ('HJacetic acid (3 : 7 at pH 2.7) [23]. Recently, NMR data were reported for NPY 13-36 in ('H,)TFE/water (9 : 1) but the three-dimensional structure could not be determined due to resonance overlap [24]. However, the chemical shift values for the NH and a protons are consistent with helical structure.In this study, the structure of the most common Y2 receptor agonist, NPY 13 -36, has been determined by two-dimensional NMR spectroscopy and molecular modeling. Experiments were performed in deuterated dimethylsulfoxide [(2H,)Me,SO], a solvent of medium polarity which should represent the various media in which the peptide can exist and which is not a helix inducer. These conditions allow us to compare the structure of this fragment with our previously repor...

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