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Biomedical subjects

B J Metcalf

Publications and source records attributed to B J Metcalf.

11 recordsLinked to original sources
PubMed1997

Assessment of the ratio of carpal contents to carpal tunnel volume in patients with carpal tunnel syndrome: a preliminary report.

An anatomic basis for carpal tunnel syndrome (CTS) has been proposed but not confirmed; both volumetric and area studies have been used to address this issue. The authors have demonstrated that the ratio of the carpal tunnel contents (CTC) to carpal tunnel volume (CTV) provides information regarding the relative free space in the carpal tunnel as compared with canal volume alone. This study was undertaken to determine whether the CTC/CTV ratio was higher for patients with CTS than for normal subjects. Seven asymptomatic volunteers and 7 patients with symptoms of CTS underwent magnetic resonance imaging (MRI) so that the CTC/CTV ratios could be determined. Standard radiographs were analyzed to identify plain radiographic variables that differed between patients with CTS and control subjects, and no differences were found. On MRIs, however, CTC/CTV ratios were noted to be higher for patients with CTS than for matched control subjects.

Carpal Bones↗
PubMed1994

Chronic peripheral nerve pain treated with direct electrical nerve stimulation.

Chronic somatic peripheral nerve pain was treated prospectively in 24 nonrandomized patients by a program of direct electrical nerve stimulation. Patients qualified for the program if anesthetic (lidocaine) nerve block of the involved cutaneous zone of the peripheral nerve relieved symptoms and transcutaneous electrical nerve stimulation transiently improved and did not exacerbate somatic pain. Results were judged according to a pain score. Patients noted improved sleep and complete absence of the need for narcotic pain medication. On the basis of subjective and objective criteria, 18 patients had good or excellent results and 6 had implant failures. Of the six patients with failures, three failed the trial period and did not have implantation, and three had no significant pain relief and were judged as treatment failures. Three patients had late equipment failure after initial good results. Most patients had some relief of pain, which increased their quality of life and eliminated the need for narcotic analgesia. Direct electrical nerve stimulation should be considered for somatic peripheral nerve pain that has not been ameliorated with other methods. It will reduce, although not necessarily eliminate, pain and pain behavior in most patients.

Adolescent↗
PubMed1990

A recombinant non-fatty acylated form of the Hi-PAL (P6) protein of Haemophilus influenzae elicits biologically active antibody against both nontypeable and type b H. influenzae.

An approximately 15,000-dalton outer membrane lipoprotein of Haemophilus influenzae, the Hi-PAL (P6) protein, has been shown to elicit bactericidal and protective antibodies against both type b and nontypeable H. influenzae strains and is a vaccine candidate for these organisms. To determine whether the lipid modification of this protein is required for immunogenicity or the elicitation of biologically active antibodies, a genetic fusion was constructed that contains the sequence of mature Hi-PAL fused to the polylinker region of pUC19. The protein expressed by this clone does not contain detectable lipid and was purified to homogeneity. This recombinant fusion protein, rPAL, elicited a strong immune response when injected into rabbits, and the antiserum reacted well with native Hi-PAL. The antiserum was bactericidal against a number of clinical nontypeable strains, duplicating the activity of anti-Hi-PAL. The anti-rPAL antiserum was also protective against type b bacteremia in the infant rat model. These results demonstrate that purified rPAL elicits antibodies with biological activities that are similar to those of anti-Hi-PAL antibodies. Thus, the lipid component of Hi-PAL is not required for either immunogenicity or elicitation of biologically active antibodies.

Acylation↗
PubMed1990

Antigenic conservation of the 15,000-dalton outer membrane lipoprotein PCP of Haemophilus influenzae and biologic activity of anti-PCP antisera.

A gene from Haemophilus influenzae encoding an outer membrane lipoprotein of about 15,000 daltons and which comigrates with the peptidoglycan-associated lipoprotein (PAL) of H. influenzae on sodium dodecyl sulfate-polyacrylamide gel electrophoresis has been previously reported and designated pcp gene, and its product has been designated PCP. in order to obtain specific immunologic probes for the analysis of PCP expression, cellular location, and antigenic conservation in H. influenzae, pcp was fused to the lac polylinker region of plasmid pUC19 and the hybrid gene was expressed in Escherichia coli. PCP purified from these cells was used to generate rabbit and mouse polyclonal antisera and mouse monoclonal antibody against PCP. Western immunoblot analysis with anti-PCP monoclonal antibody demonstrated that PCP is present and antigenically conserved in 30 tested strains of H. influenzae, including 27 clinical nontypeable strains. Polyclonal antiserum against PCP killed 9 of 11 clinical H. influenzae strains in a complement-mediated bactericidal assay, and bactericidal activity was additive with bactericidal activity of antisera against PAL. These results indicate that PCP is a potentially valuable component for a subunit vaccine against nontypeable H. influenzae disease, especially in combination with PAL or other components.

Amino Acid Sequence↗
PubMed1989

Alkaline phosphatase fusions to the respiratory syncytial virus F protein as an approach to analyze its membrane topology.

Manoil and Beckwith (1985) have constructed a transposon, TnphoA, that permits the generation of hybrid proteins composed of alkaline phosphatase (AP) lacking its signal peptide fused to amino-terminal sequences of other proteins. This transposon has been used to localize export signals and analyze membrane topology of bacterial proteins. We have applied this approach to the membrane fusion protein (F) of respiratory syncytial virus (RSV). The transposon TnphoA and a plasmid directing bacterial expression of the F gene were used to construct F-AP hybrids. These hybrids yielded AP activity, indicating the presence of viral sequences that promoted protein transport through the cytoplasmic membrane. Sequence analysis showed that TnphoA was inserted at four different positions within the F1 subunit. Deletion of the hydrophobic F1 amino-terminus (fusion-related domain) resulted in AP transport to the periplasm, suggesting that the hydrophobic amino-terminus of the F2 subunit is sufficient to promote protein export. Some hybrids were apparently cleaved at or near the F2/F1 junction. The periplasmic localization of an uncleaved hybrid strongly suggested that the fusion-related domain of the F protein, when in the uncleaved F0 precursor, can be moved across the bacterial cytoplasmic membrane. Although these results apply to the recombinant F protein, they agree with the presumed signal sequence and membrane topology of the native F glycoprotein. Thus, this method may be useful in determining membrane topology and in localizing important domains of viral proteins.

Alkaline Phosphatase↗
PubMed1988

Cloning of genes encoding a 15,000-dalton peptidoglycan-associated outer membrane lipoprotein and an antigenically related 15,000-dalton protein from Haemophilus influenzae.

We have cloned and expressed in Escherichia coli a gene encoding a 15,000-apparent-molecular-weight peptidoglycan-associated outer membrane lipoprotein (PAL) of Haemophilus influenzae. The nucleotide sequence of this gene encodes an open reading frame of 153 codons with a predicted mature protein of 134 amino acids. The amino acid composition and sequence of the predicted mature protein agree with the chemically determined composition and partial amino acid sequence of PAL purified from H. influenzae outer membranes. We have also identified a second gene from H. influenzae that encodes a second 15,000-apparent-molecular-weight protein which is recognized by antiserum against PAL. This protein has been shown to be a lipoprotein. The nucleotide sequence of this gene encodes an open reading frame of 154 codons with a predicted mature protein of 136 amino acids and has limited sequence homology with that of the gene encoding PAL. Southern hybridization analysis indicates that both genes exist as single copies in H. influenzae chromosomal DNA. Both genes encode polypeptides which have amino-terminal sequences similar to those of reported membrane signal peptides and are associated primarily with the outer membrane when expressed in E. coli.

Amino Acid Sequence↗