Intérêt de la mobilisation précoce chez les patients greffés pulmonaires : revue de littérature

Introduction: Sprinting is a discipline found in many sports. Hamstring injuries are very common in sprinting athletes. It is therefore important to determine the risk factors for Hamstring injuries.Objective : Identify in the literature the risk factors for musculotendinous injuries in sprinters.Methods: 6 of 231 items meet the criteria, the analysis of the articles made it possible to extract results answering the problematic Résults: Analysis of the articles identified factors such as injury history, muscle imbalance, tendon build-up, mechanical load, sprint stretching and nordic hamstring training. Dsicussion: The review has a low level of evidence and certain biases which do not allow a causal link between the muscle injury and factors studied. Homewer, this review gives us some perspective on the occurrence of musculotendinous injury ofHamstrings.Introduction : le sprint est une discipline à part antérieur mais se retrouve dans de nombreux sports. Les blessures aux ischio-jambiers sont des événements très fréquents dans la population sprinteuse. Il paraît donc important de déterminer les facteurs ayant un impact dans la survenue des lésions musculo-tendineuses des ischio-jambiersObjectif : identifier dans la littérature les facteurs de risques de lésions musculo-tendineuses spécifiques au sprinteur.Méthodologie : 6 articles sur 231 répondent aux critères définis préalablement, l’analyse de ces articles ont permis d’extraire des résultats répondant à la problématique.Résultats : l’analyse des articles ont permis d’identifier les facteurs anthropologiques tels que les antécédents de blessures, le déséquilibre musculaire et la constitution du tendon. Ainsi que la présence de facteurs biomécanique comme la charge mécanique appliquée, les étirements statiques avant le sprint et l’entraînement par « Nordic Hamstring »Discussion : la revue possède un faible niveau de preuves et certains biais qui ne permettent pas d’affirmer un lien de causalité entre la survenue des lésions musculaire et les facteurs étudiés.Cependant cette revue nous donne des perspectives de réflexion sur la survenue des lésions musculo-tendineuse des ischio-jambiers

La nécropole Chambon du Vigneau (Pussigny, Indre-et-Loire) : un lieu à vocation funéraire pour une communauté de pasteurs ?

International audienc

Involvement of the H2 domain of the GacS unorthodox HK in the LadS signaling pathway.

<p>The pBBR<i>ladS</i> plasmid containing the <i>ladS</i> HK gene and the pBBRMCS4 corresponding empty cloning vector were conjugated in the PAKΔ<i>gacS</i> strain in which the <i>gacSH2</i> or <i>gacSH2</i>_<i>H→Q</i> gene versions or the corresponding suicide vector were chromosomally integrated at the Tn7 site. (A) RsmY (blue bars) and RsmZ (brick-red-colored bars) transcript levels were monitored using RT-qPCR and fold induction was presented in the strains PAKΔ<i>gacS</i>::<i>miniTn7gacSH2</i> (<i>gacSH2</i>) and PAKΔ<i>gacS</i>::<i>miniTn7gacSH2</i>_<i>H→Q</i> (<i>gacSH2</i>_<i>H→Q</i>) as compared to the PAKΔ<i>gacS</i>::<i>miniTn7</i> strain (<i>miniTn7</i>). (B) Biofilm production in glass tubes was illustrated (upper panel) and quantified after crystal violet-staining (lower panel). Corresponding levels of biofilm production represent mean values and standard deviations obtained from three independent experiments. Wilcoxon-Mann-Whitney tests were performed; ** and ns referred to p<0.01 and nonsignificant difference. <b>C.</b> PelA (violet bars) and ExoS (royal blue bars) transcript levels were monitored using RT-qPCR and fold induction was presented in the strains PAKΔ<i>gacS</i>::<i>miniTn7gacSH2</i> (<i>gacSH2</i>) and PAKΔ<i>gacS</i>::<i>miniTn7gacSH2H→Q</i> (<i>gacSH2H→Q</i>) as compared to the PAKΔ<i>gacS</i>::<i>miniTn7</i> strain (<i>miniTn7</i>). (D) Production of the H1-T6SS Hcp1 proteins was detected in whole cell extracts using western blot with an anti-Hcp1 polyclonal antibody. Numbers on the left side are molecular weight standards (kDa). Moderated t-tests were performed and *, **, *** and ns referred to p<0.05, p<0.01 and p<0.001 and nonsignificant difference, respectively. (E) Transcript levels of RsmY (blue bars), RsmZ (brick-red-colored bars), VgrG1 (green bars), PelA (violet bars) and ExoS (royal blue bars) were monitored using RT-qPCR. Fold induction was presented in the strains PAK, PAKΔ<i>ladS</i>, PAK<i>gacSH1</i>_<i>H→Q</i>, PAK<i>gacSH1</i>_<i>H→Q</i>Δ<i>ladS</i>, PAK<i>gacSH1</i>_<i>H</i>→_<i>Q</i><i>H2</i>_<i>H</i>→_<i>Q</i> and PAK<i>gacSH1</i>_<i>H</i>→_<i>Q</i><i>H2</i>_<i>H</i>→_<i>Q</i>Δ<i>ladS</i> in order to disable autophosphorylation of the GacSH1 domain and the functionality of the GacsH2 domain, respectively. Moderated t-tests were performed and *, **, *** and ns referred to p<0.05, p<0.01 and p<0.001 and nonsignificant difference, respectively.</p

Plasmids used in this study.

<p>Plasmids used in this study.</p

The GacSA-RetS-PA1611-LadS signaling network.

<p>(A) Current model for the regulatory elements influencing the expression of two sRNAs, RsmY and RsmZ. See text for details. (B) The multicomponent signal transduction system made of the LadS hybrid HK and the GacS/GacA TCS. In the presented model sustained by results obtained in the present study, this multicomponent signal transduction system made of the LadS hybrid HK and the GacS/GacA TCS forms a multiple-input system probably reflecting the variability of environmental conditions <i>P</i>. <i>aeruginosa</i> is faced with and may result in a range of gradations of chronic infection. IM (Inner Membrane), P (Periplasm), C (Cytoplasm).</p

Biofilm production, Pel EPS expression, H1-T6SS production and T3SS expression in the LadS signaling pathway.

<p>The pBBR<i>ladS</i> plasmid containing the <i>ladS</i> HK gene (dark bars) and the pBBRMCS4 corresponding empty cloning vector (light bars) were conjugated in the PAK, PAKΔrsmY, PAKΔ<i>rsmZ</i> or PAKΔ<i>rsmY</i>Δ<i>rsmZ</i> strains. (A) Biofilm production in glass tubes was illustrated (upper panel) and quantified after Crystal Violet-staining (lower panel). Corresponding levels of biofilm production represent mean values and standard deviations obtained from three independent experiments. (B) Activity of the <i>pelA–lacZ</i> transcriptional chromosomal fusion was monitored in the same strains with the pBBR<i>ladS</i> plasmid containing the <i>ladS</i> HK gene (dark violet bars) and the pBBRMCS4 corresponding empty cloning vector (light violet bars) after 4 hours of growth (OD_600nm≈3.5). Corresponding β-galactosidase activities are expressed in Miller units and correspond to mean values (with error bars) obtained from three independent experiments. (C) Production of the H1-T6SS VgrG1s proteins was detected in whole cell extracts using western blot with an anti-VgrG1 polyclonal antibody. Numbers on the left side correspond to molecular weight standards (kDa). (D) Activity of the <i>exoS–lacZ</i> transcriptional chromosomal fusion was monitored in the same strains with the pBBR<i>ladS</i> plasmid containing the <i>ladS</i> HK gene (dark royal blue bars) and the pBBRMCS4 corresponding empty cloning vector (light royal blue bars) after 6 hours of growth (OD_600nm≈4). Corresponding β-galactosidase activities are expressed in Miller units and correspond to mean values (with error bars) obtained from three independent experiments. Wilcoxon-Mann-Whitney tests were performed and *, **, *** and ns referred to p<0.05, p<0.01 and p<0.001 and nonsignificant difference, respectively.</p

H1 and D1 domain involvement of the LadS hybrid HK in the LadS signaling pathway.

<p>(A) The pBBR<i>ladSH1D1</i> plasmid containing the <i>ladSH1D1</i> cytoplasmic DNA region of the LadS hybrid HK fused to a C-terminal His-tag, the pBBR<i>ladSH1</i>_<i>H→Q</i><i>D1</i> and pBBR<i>ladSH1D1</i>_<i>D→A</i> variant plasmids and the pBBRMCS4 corresponding empty cloning vector were conjugated in the PAK strain. Production of the corresponding cytoplasmic versions of LadS was checked in whole cell extracts using western blot and a monoclonal anti-His antibody. Numbers on the left side are molecular weight standards (kDa) (upper panel). Activity of the <i>rsmY–lacZ</i> (blue bars) and <i>rsmY–lacZ</i> (brick-red-colored bars) transcriptional chromosomal fusions were monitored after 6 hours of growth (OD_600nm≈4) and corresponding β-galactosidase activities are expressed in Miller units and correspond to mean values (with error bars) obtained from three independent experiments. Wilcoxon-Mann-Whitney tests were performed and *, **, *** and ns referred to p<0.05, p<0.01 and p<0.001 and nonsignificant difference, respectively (middle panel). Production of the H1-T6SS VgrG1 protein was detected in whole cell extracts using western blot with an anti-VgrG1 polyclonal antibody. Numbers on the left side are molecular weight standards (kDa) (lower panel). (B) Biofilm production in glass tubes of PAK, PAKΔ<i>ladS</i> and of point chromosomal mutants PAK<i>ladSH1</i>_<i>H→Q</i><i>D1</i> and PAK<i>ladSH1D1</i>_<i>D→A</i> was presented (upper panel) and quantified after crystal violet-staining and extraction (lower panel). Corresponding levels of biofilm production represented by mean values and standard deviations were obtained from three independent experiments. Wilcoxon-Mann-Whitney tests were performed and *, **, *** and ns referred to p<0.05, p<0.01 and p<0.001 and nonsignificant difference, respectively. (C) Transcript levels of RsmY (blue bars), RsmZ (brick-red-colored bars), VgrG1b (T6SS) (green bars) and ExoS (T3SS) (royal blue bars) were monitored in PAK, PAKΔ<i>ladS</i> and in point chromosomal mutants PAK<i>ladSH1</i>_<i>H→Q</i><i>D1</i> and PAK<i>ladSH1D1</i>_<i>D→A</i> strains using RT-qPCR. Fold induction was presented for the three mutant strains as compared to the PAK strain. Moderated t-tests were performed; *, ** and *** referred respectively to p<0.05, p<0.01 and p<0.001. (D) Activity of the <i>pelA–lacZ</i> (violet bars) transcriptional chromosomal fusion was monitored after 6 hours of growth (OD_600nm≈5) and corresponding β-galactosidase activities are expressed in Miller units and correspond to mean values (with error bars) obtained from three independent experiments. Statistical tests were performed and ** referred to p<0.01.</p

<i>In vitro</i> transphosphorylation assays.

<p>(A) For transphosphorylation assay between LadS or GacS variants and GacSH2 variants or HptA protein, 2 mM of LadSH1D1 or LadSH1D1_D→A recombinant proteins were incubated with [γ-³²P] ATP and GacSH2 (lanes 1 and 2), GacSH2_H→Q (lanes 3 and 4) or HptA (lanes 5 and 6) at room temperature for 20 min (see <a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1006032#sec010" target="_blank">Materials and Methods</a>) then separated in an SDS-polyacrylamide gel in duplicate. (B) Transphosphorylation assay between the LadSH1D1_D→A or GacSH1 and LadSD1 or GacsD1 domains with or without the GacSH2 domain. Two mM of LadSD1 or GacSD1 recombinant proteins were incubated with [γ-³²P] ATP and LadSH1D1_D→A or GacSH1 (left panel<b>)</b> together with the GacSH2 domain (right panel) at room temperature for 20 min. In both experiments mixtures of proteins were separated in an SDS-polyacrylamide gel in duplicate. Numbers on the left side are molecular weight standards (kDa). Locations of the recombinant proteins are indicated by arrowheads. For each experiment presented in panels A and B, one gel was detected by western blot using an anti-penta-His antibody (upper panel) while the other was autoradiographied (lower panel).</p

Interactions between H1 domains of the LadS hybrid HK, the GacS unorthodox HK and the RetS hybrid HK using pull-down and two-hybrid experiments.

<p>(A) Pull-down experiments. N-terminal FLAG or Strep versions of the H1 domain of GacS, LadS and RetS HKs were constructed in pBBRMCS3 and pCR2.1 vectors, respectively, and expressed in <i>E</i>. <i>coli</i>. Cell lysates were immunoprecipitated using anti-Strep antibody-coupled beads, and FLAG and Strep derivatives were further detected using StrepTactin Alkaline Phosphatase conjugate (upper panel) and anti-FLAG antibody detection (lower panel). (B) In two-hybrid experiments, the <i>ladSH1</i>, <i>retSH1</i> and <i>gacSH1</i> DNA regions were cloned into the two-hybrid pUT18C or pKT25 vectors and corresponding vectors were co-transformed in BTH101 cells that were further streaked on LB plates containing X-gal. A blue color of colonies reflects interaction between chimeric proteins, while white color attests to the absence of interaction. The interactions were further quantified by measuring the corresponding ß-galactosidase levels expressed in Miller units (values and standard deviations of 3 independent clones below corresponding colonies).</p