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D Donner

Publications and source records attributed to D Donner.

12 recordsLinked to original sources

[99mTc pertechnetate scintigraphy and premedication for the search for ectopic gastric mucosa in Meckel's diverticulum].

BACKGROUND: Meckel's diverticulum (MD) is the most common anomaly of the large intestinal tract (1-3%) and is more frequent in children (62% < 2 years) and in males (66%). It often involves ectopic gastric mucosa which manifests through gastrointestinal bleeding in 50% of cases. 99m-Technetium scintigraphy (99mTcO4) is one of the procedures available for the non-invasive diagnosis of ectopic gastric mucosa. METHODS: Twenty-eight patients (11 females, 17 males), including 16 children and 12 adults, aged 8 months-80 years old, were included in the study. The patients were admitted to hospital for hematochezia and melena (22) associated with abdominal pain (5): 3 patients repeatedly presented occult blood in their stools. Two patients only suffered from abdominal cramps and one only anemia. Patients were studied using plain abdominal radiographs and ultrasound; 10 underwent gastroscopy and colonoscopy; radiological contrast studies were performed in 5 patients. All tests were inconclusive. All the patients were premedicated with oral cimetidine (20 mg/kg in pediatric patients and 300 mg q.i.d. for adults, 48 hours before the test) or with ranitidine i.v. (1 mg/kg, max 50 mg, in 20 minutes, one hour before the test); barium meals and colonoscopy were deferred for 2-3 days after examination. An intravenous injection of 37-180 Mbq of 99mTcO4 was given followed by a dynamic study of the abdomen in anterior projection. Images were acquired for one hour or until the visualisation of abnormal foci of intake: in this case, lateral and oblique images were acquired for a better localisation of the suspicious area. Some patients were administered furosemide i.v. (0.75 mg/kg). All underwent a follow-up period of 12 months. RESULTS: Pertechnetate scintigraphy was positive in 10 cases and the presence of ectopic gastric mucosa was confirmed by surgery. The study was negative in 18 cases: 3 of them were discharged with a diagnosis of Salmonella infection, polyp of the small bowel or ulcer of the large bowel respectively; the other 15 patients did not show symptoms of onset during follow-up. CONCLUSIONS: These results confirm the high diagnostic accuracy of pertechnetate scintigraphy to detect ectopic gastric mucosa if associated with H2-receptor-blocking agent premedication.

Adolescent↗

Tumor necrosis factor alpha stimulates gluconeogenesis from alanine in vivo.

An increase in gluconeogenesis contributes to the cachexia seen in severe injury, sepsis, and malignancy by converting amino acids from skeletal muscle to glucose. Since tumor necrosis factor alpha (TNF alpha) may mediate this cachexia, we examined the effect of this cytokine on gluconeogenesis. Twenty-eight male Fischer rats were injected intraperitoneally with TNF alpha (250 micrograms/kg) or saline, and after 4 hours, isolated hepatocytes were obtained by in situ collagenase liver perfusion. Hepatocytes were incubated with alanine (10 mM), and rates of gluconeogenesis were determined. Plasma lactate, glucose, insulin, glucagon, cortisol, and amino acids were measured. TNF alpha administration resulted in a 50% increase in gluconeogenesis from alanine (P < 0.05) and a three-fold increase in plasma glucagon (P = 0.01). Total and glucogenic plasma amino acids decreased with TNF alpha injection (P < 0.05). In vivo TNF alpha causes an increase in hepatic gluconeogenesis associated with increased plasma glucagon.

Alanine↗

SH2-containing phosphotyrosine phosphatase Syp is a target of p210bcr-abl tyrosine kinase.

The phosphorylation of proteins at tyrosine residues is critical in cellular signal transduction and neoplastic transformation. These mechanisms are regulated by the activities of both protein-tyrosine kinases and protein-tyrosine phosphatases. Recent studies have identified a novel protein-tyrosine phosphatase, termed Syp, that is widely expressed in various tissues. Syp encodes a cytoplasmic phosphatase that contains two Src homology 2 (SH2) domains. Since SH2 domains have been shown to target the association of signal-transducing molecules to activated tyrosine kinases, experiments were performed to determine whether Syp might form specific complexes with p210bcr-abl, a fusion protein believed to be involved in the pathogenesis of chronic myelogenous leukemia and, thus, possibly alter or mediate p210bcr-abl tyrosine kinase activity. We found that Syp was highly and constitutively tyrosine phosphorylated in three different murine cell lines transfected with a p210bcr-abl expression vector. Furthermore, p210bcr-abl, Syp, and Grb2 formed stable complexes in BCR-ABL-expressing cells. Complex formation between p210bcr-abl and Syp was mediated in vitro by the NH2-terminal SH2 domain of Syp. Last, p210bcr-abl tyrosine kinase was effectively dephosphorylated by Syp in vitro. These results suggest an interaction between Syp and BCR-ABL protein, which might play a role in cellular transformation of BCR-ABL.

Animals↗

Codon-specific missense errors in vivo.

We have developed a simple method for measuring the missense substitution of amino acids at specified positions in proteins synthesized in vivo. We find that the frequency of cysteine substitution for the single arginine in Escherichia coli ribosomal protein L7/L12 is close to 10(-3) for wild-type bacteria, decreases to 4 x 10(-4) in streptomycin-resistant bacteria containing mutant S12 (rpsL), and is virtually unchanged in Ram bacteria containing mutant S4 (rpsD). We have also found that the frequency of the cysteine substitution for the single tryptophan in E. coli ribosomal protein S6 is 3-4 x 10(-3) for wild-type bacteria, decreases to 6 x 10(-4) in streptomycin-resistant bacteria and is elevated to nearly 10(-2) in Ram bacteria.

Amino Acid Substitution↗

Guanosinetriphosphatase activity dependent on elongation factor Tu and ribosomal protein L7/L12.

Incubation of electrophoretically pure samples of the Escherichia coli 50S ribosomal protein L7/L12 together with elongation factor Tu leads to the hydrolysis of GTP. Addition of elongation factor Ts stimulates this reaction. Elongation factor G cannot replace elongation factor Tu for the ribosome-free GTPase reaction dependent on L7/L12. The data suggest that elongation factor Tu and the protein L7/L12 interact directly at the ribosomal A site.

Bacterial Proteins↗