Reducing AB plasma utilisation through the AB plasma appropriateness index.

OBJECTIVES: We hypothesised that there was inappropriate group AB plasma used in our hospital, identifiable by a novel key quality indicator (KQI) and mitigable through massive transfusion protocol (MTP) modification. BACKGROUND: Group AB plasma is a scarce resource strained by increasing usage worldwide when used as universal donor plasma in non-group AB patients. To reduce inappropriate use and to promote benchmarking to the best practice, we developed the AB plasma appropriateness index (ABAI). ABAI is the ratio of AB plasma transfused to group AB or unknown blood group patients to all AB plasma utilised, where values closer to 1 are better. METHODS: Data collected included AB plasma disposition by blood group, indications for transfusion, total blood utilisation, patient clinical characteristics and outcomes. ABAI during a 12-month period was retrospectively assessed, which led to implementation of pre-thawed group A plasma instead of group AB plasma for trauma patients starting in July 2017. RESULTS: The ABAI retrospectively showed inappropriate use in non-group AB patients in our hospital, the majority used to avoid expiry after thaw. When comparing 1-year pre- and post-implementation periods, ABAI improved from 0·464 to 0·900 (P < 0·0001). After exclusion of therapeutic plasma exchange, ABAI still improved (0·486-0·720, P < 0·0001). No differences in the length of stay or mortality associated in 32 patients receiving group A plasma for emergency release were observed. CONCLUSION: The ABAI is a novel KQI to indicate inappropriate AB plasma usage for quality improvement. This led to thawed A plasma use for MTPs, reducing inappropriate AB plasma usage.

Tumor promoter-stimulated Mr 92,000 gelatinase secreted by normal and malignant human cells: isolation and characterization of the enzyme from HT1080 tumor cells.

A Mr 92,000 metalloprotease, originally observed in neutrophils, has been found to be secreted by various normal and malignant cells of fibroblastic, hematopoietic, and epithelial origin. The responsiveness of the various cell types to the tumor promoter phorbol ester (phorbol myristate acetate) to secrete this enzyme and a corresponding Mr 72,000 gelatinase has been determined using gelatin zymograms. The latent zymogen form of the Mr 92,000 enzyme has been purified from phorbol myristate acetate-stimulated HT1080 human fibrosarcoma cells using sequential gelatin-Sepharose affinity chromatography and gel filtration. Selective elution from gelatin-Sepharose allows for a distinct separation of the Mr 92,000 gelatinase from the Mr 72,000 gelatinase. A fraction of the tumor cell derived latent Mr 92,000 enzyme is isolated as an apparent complex with human tissue inhibitor of metalloproteases, which is partially dissociated in sodium dodecyl sulfate and completely dissociated upon reduction of disulfide bonds and upon p-aminophenylmercuric acetate treatment. Organomercurial treatment rapidly allows for autoactivation of the proenzyme to active Mr 83,000 and Mr 75,000 species. At physiological pH, the enzyme rapidly degrades gelatin into small fragments and slowly cleaves native type V collagen at an apparent single site. Native type IV collagen is degraded to a much lesser extent. The NH2-terminal amino acid sequence of the Mr 92,000 proenzyme has been determined and is distinct from the Mr 72,000 gelatinase/type IV collagenase which is constitutively produced by fibroblasts. The Mr 92,000 enzyme is also immunologically distinct from the Mr 72,000 enzyme but immunologically cross-reactive with the neutrophil, high molecular weight gelatinase. The Mr 92,000 enzyme constitutes a distinct member of the matrix metalloprotease family. Its substrate specificity implies a broad physiological role, acting on basement membrane type V collagen as well as on denatured (gelatinized) collagens and thus may be involved in the invasive and migratory phenotype of human cells.

Indoor airborne fiber levels of MMVF in residential and commercial buildings.

Man-made vitreous fibers (MMVF) have been used widely in commercial and residential buildings for over 50 years. Concerns have been expressed since the late 1960s that MMVF products may erode and contribute to fiber levels in the indoor environment. This cooperative investigation was undertaken to quantify indoor respirable fiber levels by phase contrast optical microscopy (PCOM) and to differentiate between fiber types using scanning electron microscopy with energy-dispersive X-ray microanalysis (SEM-EDX). A total of 205 stationary samples were collected using standard industrial hygiene methods in 51 residential and commercial buildings. Twenty-one simultaneous outdoor samples were collected at 19 buildings. All samples were analyzed by PCOM following the NIOSH 7400 Fiber method, "B" counting rules, and 50 randomly selected samples were analyzed by SEM-EDX. The PCOM mean value for all respirable fiber levels was 0.008 f/cc with a median value of 0.007 f/cc and a maximum value of 0.029 f/cc. Ninety-seven percent of the respirable fibers identified by SEM-EDX were determined to be organic. MMVF were detected on only two samples. Airborne fiber levels were very low and the respirable fibers present were primarily organic. The inorganic fiber levels determined by SEM-EDX which included MMVF were less than 0.0001 f/cc.