[Intra- and interobserver reproducibility of the French version of the Constant-Murley shoulder assessment during rehabilitation after rotator cuff surgery]. / Etude de reproductibilité intra et inter-observateur de la version française du score de Constant au cours de la rééducation des coiffes opérées.

PURPOSE OF THE STUDY: The Constant-Murley scapular score is currently considered to be the gold standard for shoulder assessment in Europe. Few studies have examined the metrological qualities of this score. Our aim was to study the reliability and validity of the French version in a population undergoing reeducation after rotator cuff surgery. We wanted to determine how pertinent the score is during the reeducation phase (1-12 months after surgery). MATERIAL AND METHODS: Fifty-three patients volunteered to participate in this study. Shoulder assessment was performed by three observers. Intraobserver reproducibility was determined for 102 tests and two series of 32 and 56 tests were used to determine interobserver reproducibility. The internal coherence was studied on a sample of 61 tests. Three observers analyzed the apparent validity of the Constant Murley score. RESULTS: The correlations were satisfactory (intraobserver 0.96; interobserver 0.91 and 0.89 with the Spearman test) and sensitive (intraobserver 0.01; interobserver 0.07 and 0.01 with the Wilcoxon test). Despite satisfactory internal coherence (Cronbach alpha=0.75), the reproducibility of the overall score did not correspond necessarily to the reproducibility of the constituent scores. The measurement error might be related to patient- and observer-related interpretation variability. The apparent validity of the French version might be criticized for assessing rotator cuffs after surgery. CONCLUSION: A precise consensual protocol is needed for conducting the shoulder assessment and establishing the Constant-Murley score during the reeducation phase after rotator cuff surgery.

Mass spectrometric determination of acromelic acid A from a new poisonous mushroom: Clitocybe amoenolens.

As Clitocybe acromelalga, the mushroom Clitocybe amoenolens is responsible for erythermalgia. Acromelic acids isolated from C. acromelalga have been suspected to be to some extend the active principles. The objective was to develop a specific and sensitive liquid chromatographic-mass spectrometric method that would allow acromelic acid A identification and quantification in mushrooms. The method involved a single-step methanol-water extraction followed by a selective cleanup of the extract with solid-phase extraction cartridges (strong-anion exchange). The chromatographic separation was achieved on a porous graphitic carbon column with acetonitrile-water-formic acid as mobile phase. Detection was done with a mass analyzer equipped with a TurboIonSpray source, operated in the negative ionization mode. Acromelic acid A concentration was determined in dried mushroom at around 325 ng/mg in C. amoenolens and 283 ng/mg in C. acromelalga.

Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase.

An aminopeptidase B (Ap-B) was previously purified to homogeneity from rat testis extracts and characterized. In the present work, by using oligonucleotides selected on the basis of partial amino acid microsequences of pure Ap-B and PCR techniques, the nucleotide sequence of a 2.2-kb cDNA was obtained. The deduced amino acid sequence corresponds to a 648-residue protein (72.3 kDa) containing the canonical "HEXXHX18E" signature, which allowed its classification as a member of the M1 family of metallopeptidases. It exhibits 33% identity and 48% similarity with leukotriene-A4 hydrolase, a relation further supported by the capacity of Ap-B to hydrolyze leukotriene A4. Both enzymes also were closely related to a partially sequenced protein from Dictyostelium discoideum, which might constitute the putative common ancestor of either aminopeptidase or epoxide hydrolase, or both. Ap-B and its mRNA were detected in the germ line and in the Sertoli and peritubular cells of the seminiferous tubules. Because the enzyme was found in the medium conditioned by spermatocytes and spermatids and in the acrosome during spermatozoa formation, together these observations suggested an involvement of this exometallopeptidase in the secretory pathway. It is concluded that this ubiquitous enzyme may be involved in multiple processing mechanisms.