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Biomedical subjects

E Palmer

Publications and source records attributed to E Palmer.

226 records · Page 13Linked to original sources
PubMedDate not supplied

The short extracellular domain of the T cell receptor zeta chain is involved in assembly and signal transduction.

The zeta chain is required in the TCR complex to guarantee its surface expression and function. However, an understanding of the interaction(s) between the zeta chain and the other proteins in the TCR/CD3 has not yet been achieved. In this report, we attempt to assign a functional role to the short extracellular (EC) domain of the zeta chain by studying its unique positive charge, a lysine at position 9, because of its interesting location to the interchain disulphide bond of the zeta chain homodimer. We show that amino acid exchanges of lysine 9 to glycine, serine, cysteine or asparagine generate TCR complexes which are clearly defective in antigenic signalling. Interestingly, the non-conservative point mutations were segregating TCR complex signalling pathways. However, lysine 9 is not critical for TCR complex surface expression unless the positively charged lysine is exchanged for the negatively charged amino acid aspartic acid. The zeta chain mutant bearing a lysine to cysteine exchange is the sole mutant to be inefficiently co-precipitated with the TCR/CD3 complex suggesting a loose interaction of the zeta chain within the TCR complex.

Amino Acid Sequence↗
PubMedDate not supplied

Primary structure of human T-cell receptor alpha-chain.

The T-cell receptor has been studied intensely over the past 10 years in an effort to understand the molecular basis for major histocompatibility complex (MHC) restricted antigen recognition. The use of anti-receptor monoclonal antibodies to isolate and characterize the receptor from human and murine T-cell clones has shown that the protein consists of two disulphide-linked glycopeptides, alpha and beta, distinct from known immunoglobulin light and heavy chains. Like immunoglobulin light and heavy chains, however, both the alpha- and beta-chains are composed of variable and constant regions. Molecular cloning has revealed that the beta-chain is evolutionarily related to immunoglobulins, and is encoded in separate V (variable), D (diversity), J (joining) and C (constant) segments that are rearranged in T cells to produce a functional gene. We report here cDNA clones encoding the alpha-chain of the receptor of the human T-cell leukaemia line HPB-MLT. Using these cDNA probes, we find that expression of alpha-chain mRNA and rearrangement of an alpha-chain V-gene segment occur only in T cells. The protein sequence predicted by these cDNAs is homologous to T-cell receptor beta-chains and to immunoglobulin heavy and light chains, particularly in the V and J segments.

Amino Acid Sequence↗
PubMedDate not supplied

Quantitative and qualitative assessment of milk production after pharmaceutical induction of lactation in the mare.

The induction of lactation is performed in ruminants by steroidogenic impregnation, followed by drugs intended to increase prolactin secretion. The aim of this study was to induce lactation in barren mares and to evaluate milk production. Five treated and 5 control mares were used in June and September in year 1, and 12 mares were used in year 2. Mares were administered a vaginal pessary (500 mg altrenogest and 50 mg estradiol benzoate) for 1 week. The 2nd week, another sponge with 100 mg estradiol benzoate was administered, together with 50 mg/100 kg body weight (BW) sulpiride in oil (IM q12h). All mares were milked by hand. Drug treatment was stopped after I L was obtained. Milk production and composition and plasma prolactin concentration were measured. In year 2, the same steroid treatment was applied, but mares received sulpiride (n = 6) or domperidone (1.1 mg/kg PO q12h) (n = 6). A milking machine and oxytocin injections 1 minute before the start of milking were used. In year 1, all treated mares started milking within 1-5 days after sulpiride treatment. Mean daily milk production was 0.88 +/- 0.52 L/500 kg BW. Milk immunoglobulin G (IgG) contents increased in all mares (IgG concentration range, 14-92 g/L). Plasma prolactin increased during sulpiride treatment (range. 27.7 +/- 2.9 to 43.7 +/- 6.7 ng/mL [before] to 289.0 +/- 7.8 ng/mL during treatment, P < .001). In year 2, results were similar to those in year 1, with peak IgG concentrations ranging from 4.2 to 106.7 g/L and a larger daily milk production (3.13 +/- 0.75 with sulpiride and 3.45 +/- 0.51 L/500 kg BW with domperidone). In conclusion, lactation can be induced in mares within 2 weeks, and some mares produce good-quality colostrum.

Administration, Intravaginal↗
PubMedDate not supplied

Pain as an indicator of bone metastasis.

Patients with breast or prostate cancer routinely referred for bone scintigraphy were evaluated for the presence of skeletal pain, as determined by a self administered questionnaire. Pain was a common finding, whether or not metastatic disease was present, and occurred in over half of patients. Although most patients with bone metastases did report bone pain, a significant fraction (21% of breast and 22% of prostate patients) were asymptomatic. A distinct minority of individual anatomic regions of metastasis were painful: pain was reported in 23% of sites of breast metastases and 15% of metastatic prostate cancer sites. Of all sites at which pain was present, metastases were demonstrated in only about one half. These results indicate that pain is not a reliable indicator of the presence of location of metastatic bone disease.

Adolescent↗
PubMedDate not supplied

Disposition of salmeterol xinafoate in laboratory animals and humans.

The disposition of [14C]salmeterol xinafoate, a new inhaled beta 2-adrenoceptor agonist with both bronchodilator and antiinflammatory activity, has been studied in laboratory animals and humans following intravenous and oral administration. [14C]Salmeterol was rapidly absorbed in animal species and humans with Cmax observed within 2 hr. Cmax was similar for normalized oral dose level in mice, rats, and rabbits. In dogs, Cmax was higher and reflected the greater oral bioavailability in this species. The plasma t1/2, after intravenous administration, was 5 hr in rats and 2 hr in dogs. The volume of distribution of salmeterol was significantly greater than total body water in both rats (40 liters/kg) and dogs (6 liters/kg) and indicated high tissue uptake of the compound. Plasma clearance was high in rats (95 ml/min/kg) and dogs (30 ml/min/kg). Radioactive drug-related material was widely distributed throughout body tissues in rats. The highest concentrations were present in kidney, liver, gastrointestinal tract, pituitary, lung, heart, and bone marrow. Transfer of radioactive drug-related material across the placental barrier or into milk, studied in rats, was low. In all species the majority of an oral or intravenous dose (55-75%) was excreted in feces. Biliary excretion in rats and dogs accounted for 53% (0-27 hr) and 40% (0-8 hr) of an oral dose, respectively, indicating good absorption across the gastrointestinal tract. Enterohepatic circulation was significant in rats. Salmeterol was cleared predominantly by metabolism in animals and humans.(ABSTRACT TRUNCATED AT 250 WORDS)

Absorption↗