Evaluating Accuracy of Rectal Fecal Stool Assessment Using Transgluteal Cleft Approach Ultrasonography.

BACKGROUND: Transabdominal ultrasound is used to detect fecal impaction, but the rectum is difficult to visualize without bladder urine or with gastrointestinal gas. OBJECTIVE: We developed a transgluteal cleft approach that is unaffected by these factors and sought to determine if our ultrasound method could detect and classify fecal matter in the lower rectum using this approach. METHODS: We classified ultrasound images from hospitalized patients into four groups: Group 1 (bowed and rock-like echogenic areas), Group 2 (irregular and cotton candy-like hyperechoic areas), Group 3 (flat and mousse-like hyperechoic areas), and Group 4 (linear echogenic areas in the lumen). Stool characteristics were classified as hard, normal, and muddy/watery. Sensitivity and specificity were determined based on fecal impaction and stool classification accuracy. RESULTS: We obtained 129 ultrasound images of 23 patients. The sensitivity and specificity for fecal retention in the rectum were both 100.0%. The recall rates were 71.8% for Group 1, 93.1% for Group 2, 100.0% for Group 3, and 100.0% for Group 4. The precision rates were 96.6% for Group 1, 71.1% for Group 2, 88.9% for Group 3, and 100.0% for Group 4. Our method was 89.9% accurate overall. CONCLUSION: Transgluteal cleft approach ultrasound scanning can detect and classify fecal properties with high accuracy.

Lasso-grafting of macrocyclic peptide pharmacophores yields multi-functional proteins.

Protein engineering has great potential for devising multifunctional recombinant proteins to serve as next-generation protein therapeutics, but it often requires drastic modifications of the parental protein scaffolds e.g., additional domains at the N/C-terminus or replacement of a domain by another. A discovery platform system, called RaPID (Random non-standard Peptides Integrated Discovery) system, has enabled rapid discovery of small de novo macrocyclic peptides that bind a target protein with high binding specificity and affinity. Capitalizing on the optimized binding properties of the RaPID-derived peptides, here we show that RaPID-derived pharmacophore sequences can be readily implanted into surface-exposed loops on recombinant proteins and maintain both the parental peptide binding function(s) and the host protein function. We refer to this protein engineering method as lasso-grafting and demonstrate that it can endow specific binding capacity toward various receptors into a diverse set of scaffolds that includes IgG, serum albumin, and even capsid proteins of adeno-associated virus, enabling us to rapidly formulate and produce bi-, tri-, and even tetra-specific binder molecules.

[Analysis of occupational health activities through classifying reports from medical facilities in Japan].

OBJECTIVES: The objectives of this study were to analyze current trends in occupational health activities by classifying reports from medical facilities in Japan. METHODS: Reports of current workplace-level occupational health activities from medical activities that were collected by the Japan Medical Association Occupational Health Committee were used for the study. Of 5,000 questionnaire forms sent to medical facilities, 1,920 responses were returned. The freely described reports on ongoing occupational health activities contained in these responses were classified according to each of the following aspects of reported activities: 1) details of occupational health activities including main actors in workplace-level actions; and 2) approaches taken for occupational safety and health. The classification of the reports was implemented by a working group comprising selected occupational health practitioners and researchers. RESULTS: Among 1,920 survey responses, 581 valid texts were analyzed. Altogether, 1,044 occupational health activities currently undertaken by the facilities were extracted. The reported activities that were classified according to details of occupational health activities mainly comprised "Measures for preventing overwork, labor management, and work-style reform" (35.7%), "Measures for improving mental health" (21.0%), and "Review of occupational safety and health management systems" (19.3%). Medical facilities implementing "Measures for mental health" alongside "Measures for preventing overwork, labor management, and work-style reform" were reported in 13.2% of the responding medical facilities. "Occupational health professionals or safety and health management staff" (71.7%) were the most frequent main actors of these activities, followed by "Members of the workplace" (18.4%) and "Outsourced experts" (2.4%). "Comprehensive safety and health management" (42.0%) was the most common approach taken for occupational safety and health, followed by "Management focusing on topics" (23.8%) and "Case management" (16.5%). Most of these activities focused on primary prevention aimed at labor management including prevention of overwork, work-style reform, and mental health promotion. Another key trend could be "Teamwork among occupational safety and health staff, workers, and employers at respective workplaces as well as outsourced experts." DISCUSSION: Several key trends were extracted from current occupational health activities at medical facilities. In most cases, these measures were implemented simultaneously. This suggests the importance of combining primary prevention measures for mental health with measures for labor management including prevention of overwork. These activities reflect emerging trends that incorporate teamwork between experts, workers, and employers, and provide new perspectives on workplace-level occupational safety and health activities.

Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer.

Cyclophilins facilitate the peptidyl-prolyl isomerization of a trans-isomer to a cis-isomer in the refolding process of unfolded proteins to recover the natural folding state with cis-proline conformation. To date, only short peptides with a cis-form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans-form proline, i.e. succinyl-Ala-trans-Pro-Ala-p-nitroanilide and acetyl-Ala-Ala-trans-Pro-Ala-amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis-form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Neta2 of Arg is formed to fix the peptide. On the other hand, in the cis-isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans-isomer formation of a hydrogen bond between CO preceding Ala-Pro and His47 Nepsilon2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala-Pro. Although loss of double bond character of the amide bond of Ala-Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.