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Biomedical subjects

A Roussel

Publications and source records attributed to A Roussel.

12 recordsLinked to original sources

Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics.

The solution structure of human neuropeptide Y has been solved by conventional two-dimensional NMR techniques followed by distance-geometry and molecular-dynamics methods. The conformation obtained is composed of two short contiguous alpha-helices comprising residues 15-26 and 28-35, linked by a hinge inducing a 100 degree angle. The first helix (15-26) is connected to a polyproline stretch (residues 1-10) by a tight hairpin (residues 11-14). The helices and the polyproline stretch are packed together by hydrophobic interactions. This structure is related to that of the homologous avian pancreatic polypeptide and bovine pancreatic polypeptide. The C- and N-terminii, known to be involved in the biological activity for respectively the receptor binding and activation, are close together in space. The side chains of residues Arg33, Arg35 and Tyr36 on the one hand, and Tyr1 and Pro2 on the other, form a continuous solvent-exposed surface of 4.9 mm2 which is supposed to interact with the receptor for neuropeptide Y.

Amino Acid Sequence

Reversible translocation of antibiotic resistance determinants in Salmonella ordonez.

Salmonella ordonez (BM 2000) codes for kanamycin (Km, aphA), ampicillin (Ap), streptomycin (SmSp:aadA and Sm:aphC), chloramphenicol (Cm), tetracycline (Tc) and sulfonamide (Su) resistances and for production of colicin Ib (Cib). Genetical analysis by incompatibility testing, conjugation, transformation and physical studies using electron microscopy, agarose gel electrophoresis, led us to associate the Km and Cib characters to a 98.7 kilobase (kb) IncI1 plasmid (pIP565), and the Sm (aphC) and Su determinants to a 8.3 kb plasmid (pIP605). The ApCmSmSp(aadA)SuTc determinants were not associated in BM2000 S. ordonez with a plasmid structure. Following conjugation of S. ordonez to E. coli, the ApCmSmSpSuTc determinants were found stably associated with a single plasmid structure (pIP173, 127.5 kb) belonging to IncI1 group. Agarose gel electrophoresis of plasmid DNA restriction endonuclease digests and electron microscopy heteroduplex analysis showed that the acquisition of the ApCmSmSpSuTc determinants resulted from the insertion into pIP565 of a 28.8 kb DNA sequence. This sequence coding for ApCmSmSpSuTu resistances in S. ordonez could be translocated either to pIP565 plasmid or to several IncI1 plasmids but never to plasmids belonging to IncW, IncP or IncFII, suggesting the existence of specific sequences on the IncI1 receptor plasmids. Moreover, R-determinants were translocated back "en bloc" from pIP173 to the chromosome of a susceptible S. ordanez. The results were consistent with the presence in BM2000 S. ordonez chromosomal DNA of an integrated translocatable sequence encoding ApCmSmSpSuTc resistances. Such a structural association could account for the stability of these resistances in the Salmonella ordonez serotype.

Ampicillin

Plasmid epidemics.

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Aminoglycosides

Molecular studies and possible relatedness between R plasmids from groups B and D streptococci.

Resistance plasmids isolated from Streptococcus agalactiae (group B) and S. faecalis (group D) have been compared in regard to resistance markers, molecular weight, and DNA-DNA homology. Three of them (pIP501, pIP612, and pIP613) have been found to confer identical (or very similar) resistance patterns (erythromycin, lincomycin, and streptogramin B, respectively) and to have similar molecular weights (19.8 x 10(6), 22.7 x 10(6), and 17.6 x 10(6), respectively) and a high level of DNA-DNA homology in hybridization experiments (90 to 100%). These results are compatible with the view that these plasmids may derive from one common ancestor, and/or that they can be transferred between unrelated Streptococcus strains belonging to the same or different groups.

Anti-Bacterial Agents

Nitrite studies in oesophageal cancer.

As nitrate consumption may have considerable importance for the in vivo formation of nitrites and potentially carcinogenic N-Nitroso compounds, we have studied salivary nitrite levels in patients with oesophageal cancer and adult volunteers before and after administering 100 ml beet juice containing 160 mg nitrate. Initial salivary nitrite levels were slightly lower in the cancer patients, perhaps because of previous malnutrition. In both groups there was a marked increase in salivary nitrite levels 90 minutes after ingesting beet juice and the attained levels in the two groups were similar. The results imply that formation of salivary nitrite is highly dependent on exogenous dietary nitrate and that there is no difference in the capacity to form nitrites between oesophageal cancer patients and healthy adult subjects.

Adult

[Esophageal cancer in Western France. Retrospective analysis of 1400 cases].

A retrospective review was made of 1 400 cases of cancer of the esophagus treated at the Centre "Francois Baclesse" between 1964 and 1975. The disease appeared at an earlier age and more frequently in men (95%) than in women. The lesions were located predominantly in the middle third of the esophagus. There was a high frequency of local, regional and general extension of the disease due to late diagnosis. Less than one-third of the patients were eligible for surgery--which was excluded in the other cases because of age or the presence of associated pathology or secondary neoplasm--and only 10 per 100 of this group were potentially curable.

Adult

Zinc and insulin sensitivity.

Many studies have shown that zinc deficiency could decrease the response to insulin. In genetically diabetic animals, a low zinc status has been observed contrary to induced diabetic animals. The zinc status of human patients depends on the type of diabetes and the age. Zinc supplementation seems to have beneficial effects on glucose homeostasis. However, the mechanism of insulin resistance secondary to zinc depletion is yet unclear. More studies are therefore necessary to document better zinc metabolism in diabetes mellitus, and the antioxidant activity of zinc on the insulin receptor and the glucose transporter.

Animals