Myofascial pain may mimic trigeminal neuralgia.
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Diagnosis, Differential↗
Biomedical subjects
G Maloney
Publications and source records attributed to G Maloney.
Use of activated recombinant coagulation factor VII in patients undergoing reconstruction surgery for traumatic fracture of pelvis or pelvis and acetabulum: a double-blind, randomized, placebo-controlled trial.
BACKGROUND: Activated recombinant coagulation factor VII (rFVIIa) effectively prevents and controls bleeding in patients with coagulopathy. Data show that rFVIIa may reduce blood loss and eliminate the need for transfusion in patients with normal haemostasis undergoing major surgery. We assessed the efficacy of rFVIIa in patients with normal haemostasis undergoing repair surgery of major traumatic fracture of the pelvis or the pelvis and acetabulum, who were expected to have a large volume of blood loss. METHODS: We performed a double-blind, randomized, placebo-controlled trial involving 48 patients undergoing major pelvic-acetabular surgery. Patients were randomized to receive an i.v. bolus injection of rFVIIa 90 microg kg(-1) or placebo as add-on therapy at the time of the first skin incision. All patients also received intraoperative salvaged red blood cells (RBC). RESULTS: There was no significant difference in the total volume of perioperative blood loss, the primary outcome variable, between the rFVIIa and placebo groups. In addition, there were no differences between the two groups in the total volume of blood components, including salvaged RBC transfused, number of patients requiring allogeneic blood components, total volume of fluids infused, total operating time, time taken after entry to the intensive care unit to reach normal body temperature and acid-base status, and time spent in hospital. No adverse events, in particular thromboembolic events, were reported in either group. CONCLUSIONS: In patients with normal haemostasis undergoing repair surgery of traumatic pelvic-acetabular fracture, the prophylactic use of rFVIIa does not decrease the volume of perioperative blood loss.
Acetabulum↗
Kidney complications. Examining the disease process & prehospital management of patients with ESRD.
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Adult↗
Different effects of nocturnal parafunction on the masticatory system: the Weak Link Theory.
It is proposed that damage to the masticatory system from intense parafunction can be assessed more accurately by the Weak Link Theory. The theory predicts that the more intense and the more prolonged the forces, the more the tendency of damage to either. 1. the periodontal tissue; 2. the teeth; or 3. the orofacial structures. To test the theory, 22 subjects were selected based on reports of nocturnal bruxism. Each was assessed for masticatory system breakdown on the Russell Periodontal Index, the Helkimo Dysfunction Index, and a Tooth Wear Index. A Bruxcore (Forgione, A. 1974 J Dent Res 53:127) was used to obtain an objective score of bruxism. Five of eleven subjects with mild bruxism scored high on only one index. Significantly more subjects (ten of eleven) with moderate to severe bruxism scored high on one index only.
Female↗
Human monoclonal antibody homodimers. Effect of valency on in vitro and in vivo antibacterial activity.
Human IgG1 mAb dimers specific for either group B streptococci or Escherichia coli K1 bacteria were formed using chemical cross-linkers. The effect of antibody valency on biologic efficacy was investigated by comparing the IgG dimers against the corresponding IgG monomers. Binding activity and relative avidity were assessed using Ag binding and competition ELISA, and functional activity was analyzed using opsonophagocytic assays. These in vitro assays revealed that the dimers were greater than or equal to 50-fold more active than the monomers. A neonatal rat infection model showed the in vivo protective efficacy of the dimers was greater than or equal to 20-fold greater than that of the monomers. Enhancing the activity of mAb by chemical cross-linking may be a useful strategy for salvaging low affinity IgG mAb that possess poor functional properties.
Animals↗
Peptides related to the carboxyl terminus of human platelet factor IV with antibacterial activity.
A peptide (C13) corresponding to the last 13 amino acids of the carboxyl terminus of human platelet factor IV was found to be antibacterial. Amino acid substitutions predicted to disrupt either the amphipathic or alpha-helical nature of C13 rendered the peptide inactive. Antibacterial activity was demonstrated in normal human serum on bacteria which had been previously exposed to low levels of cefepime, a beta-lactam antibiotic. Peptide analogues were examined for more potent antibacterial activity in an antibacterial assay that employed normal human serum and low levels of cefepime. A peptide analogue (C18G) with 80-fold more antibacterial activity than C13 was identified. Studies in C8-deficient sera confirmed an essential role of human serum complement for optimal antibacterial activity. Additional studies showed low levels of cefepime, although not essential, enhanced the antibacterial activity of C18G. Animal protection experiments demonstrated that either peptide C18G or an analogue with all D amino acids (C18X) significantly increased the survival of neutropenic mice when coadministered with a low level of cefepime. This work has resulted in the identification of a new group of antibacterial peptides.
Amino Acid Sequence↗
Comparison of functional activities between IgG1 and IgM class-switched human monoclonal antibodies reactive with group B streptococci or Escherichia coli K1.
The influence of valence and heavy chain on antibody activity was investigated using transfectoma-derived, class-switched IgG1 and IgM human monoclonal antibodies (MAbs) reactive with the bacterial pathogens Escherichia coli K1 and group B Streptococcus species. IgG-IgM pairs were compared in vitro for antigen binding and opsonic activities and in vivo for protective efficacy in neonatal rats. For the anti-E. coli pair, the IgM MAb was 1000-fold more potent in all assay formats. Importantly, the 50% protection dose (PD50) of the IgM MAb was 10-20 ng/rat, while 100 micrograms of the IgG MAb was only minimally protective. For the group B streptococcal MAbs, the IgM was 100- and 4500-fold more potent in binding and opsonization assays, respectively. However, while 20 micrograms of IgM protected neonatal rats, 100 micrograms of IgG MAb was partly protective. These experiments demonstrate the utility of recombinant DNA technology for creating a panel of antibodies that may aid in selecting potential immunotherapeutic candidates.
Animals↗
[Plants in the books of the Epidemics].
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Greece, Ancient↗
Human monoclonal antibodies to group B streptococcus. Reactivity and in vivo protection against multiple serotypes.
Group B streptococcal (GBS) infections cause significant mortality and morbidity among infants. Passive antibody immunotherapy has been proposed as treatment for infected infants. To this end, two human mAb-secreting cell lines were produced by EBV immortalization of human B cells. The mAbs were specific for the group B polysaccharide and bound to strains of all five serotypes as demonstrated by ELISA and crossed immunoelectrophoresis. The mAbs reacted and opsonized 100% (132/132) of the clinical isolates tested which represented all four capsule types. Both prophylactic and therapeutic protection with these mAbs were demonstrated in neonatal rats given lethal infections of types Ia and III human clinical isolates. These data indicate that a single human mAb directed against the group B carbohydrate can protect against GBS infections caused by the different serotypes. This antibody may be useful in the passive immunotherapy of infants infected with GBS.
Animals↗
Human monoclonal antibody with protective activity for Escherichia coli K1 and Neisseria meningitidis group B infections.
We produced human monoclonal antibody that demonstrated specific reactivity to the K1 capsule of Escherichia coli and the group B polysaccharide of Neisseria meningitidis. The antibody was nonreactive with several strains of K1- E. coli and other gram-negative bacteria. All E. coli K1 clinical isolates tested were reactive with the antibody. When assayed for in vitro opsonophagocytic ability, the antibody caused bacterial removal only in the presence of human complement and neutrophils, an observation suggesting a non-bacteriolytic, neutrophil-dependent killing mechanism. Finally, and perhaps most importantly, the antibody was highly protective for infectious disease when used prophylactically in three animal models. The data suggest a potential use for human monoclonal antibodies in preventing and/or treating infections of the blood.
Animals↗