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Biomedical subjects

K Kristiansen

Publications and source records attributed to K Kristiansen.

At least 109 records · Page 6Linked to original sources
PubMed1982

Worldwide survey of neurosurgical training requirements and certifying mechanisms: report of the Committee on Neurosurgical Education of the World Federation of Neurosurgical Societies.

This is the report of the Committee on Neurosurgical Education of the World Federation of Neurosurgical Societies, which report was presented at the Seventh International Congress of Neurological Surgery in Munich in July 1981. The Committee was charged to conduct a survey of neurosurgical training requirements and certifying mechanisms throughout the world. These data are summarized in the tables in this report.

Certification↗
PubMed1981

Combined modality therapy of operated astrocytomas grade III and IV. Confirmation of the value of postoperative irradiation and lack of potentiation of bleomycin on survival time: a prospective multicenter trial of the Scandinavian Glioblastoma Study Group.

In a controlled, prospective, randomized investigation, started in 1974, 118 patients with supratentorial astrocytoma Grade III--IV were divided into three groups. Groups 1 and 2 received 45 Gy postoperatively to the whole supratentorial brain. Bleomycin in 15-mg doses and a total dose of 180 mg or placebo was given intravenously three times a week, one hour prior to radiotherapy, during weeks 1, 2, 4 and 5. Group 3 received conventional care but no radiotherapy or chemotherapy. Median survival rates of patients were 10.8 months in Groups 1 and 2, and 5.2 months in Groups 3, a statistically significant difference. With regard to performance, the patients in Group 3 deteriorated faster than patients in Groups 1 and 2. Bleomycin had no positive or negative influence on survival.

Adult↗
PubMed1981

Subarachnoid hemorrhage and cerebrovascular spasm. Morphological study of intracranial arteries based on animal experiments and human autopsies.

Artificial subarachnoid hemorrhage (SAH) produced by injection of autologous blood into the cisterna magna in dogs gave rise to considerable narrowing or spasm of the basilar artery and its branches, including the posterior cerebral arteries, as demonstrated by cerebral angiography. Repeated cisternal injections of blood at various intervals produced more severe spasm than a single injection. After perfusion-fixation of the brain, the cerebral arteries were examined by light and electron microscopy. None of the animals showed abnormalities in the intima or media of the vessel walls. Previously reported findings of morphological changes due to spasm could not be confirmed. Postmortem examination of brain vessels from nine patients with SAH and arterial spasm showed no specific changes that could be ascribed to spasm.

Angiography↗
PubMed1980

[Gallstones].

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Adult↗
PubMed1978

Ribosomal proteins in growing and starved Tetrahymena pyriformis. Starvation-induced phosphorylation of ribosomal proteins.

The complements of ribosomal proteins in growing and starved cells of Tetrahymena pyriformis strain GL were examined by two-dimensional gel electrophoresis. In growing cells, the 40-S ribosomal subunit contained 30 proteins, 4 of which migrated toward the anode at pH 8.6, while the 60-S ribosomal subunit contained 46 proteins, 9 of which migrated toward the anode at pH 8.6. When exponentially growing cells were transferred into a non-nutrient medium pronounced phosphorylation of a single 40-S ribosomal subunit protein, S6, was induced. The phosphorylation was very specific; more than 99.5% of the [32P]phosphate incorporated into ribosomal proteins was associated with S6. Phosphate was incorporated into S6 as O-phosphoserine and O-phosphothreonine. Two-dimensional gel electrophoresis indicated that the complement of proteins associated with the ribosomes isolated from starved cells differed from that of growing cells. Careful examination, however, suggested that except for the phosphorylation of certain ribosomal proteins in starved cells, the observed differences did not reflect starvation-induced changes in vivo, but most probably different levels of artifactual modifications (limited proteolysis) during the preparation of the ribosomes.

Animals↗
PubMed1978

Conservation of active ribosomes in acetone-treated cells of Tetrahymena pyriformis.

The preparation of an acetone powder of cells of Tetrahymena pyriformis GL is described. A comparison of ribosomal particles isolated from acetone-treated and untreated cells shows that structurally and functionally intact ribosomes can be isolated from acetone-treated cells. Fully active ribosomes have been isolated from acetone powder of Tetrahymena that had been stored for more than 6 months at 4 degrees C. Thus, this procedure allows easy storage of large quantities of cells for the bulk preparation of active ribosomes.

Acetone↗
PubMed1978

Phosphorylation in vivo of Ribosomes in Tetrahymena pyriformis.

Phosphorylation of ribosomal proteins in vivo was studied in exponentially growing and starved cells of the ciliated protozoan, Tetrahymena pyriformis. No phosphorylation of ribosomal proteins could be demonstrated in cells growing exponentially in complex nutrient media. However, when Tetrahymena cells were transferred into a non-nutrient medium, pronounced phosphorylation of a single ribosomal protein was observed. During two-dimensional polyacrylamide gel electrophoresis the phosphorylated ribosomal protein migrated in a manner virtually identical to that of the phosphorylated ribosomal protein S6 of rat liver. The phosphorylated ribosomal protein has a molecular weight of 38000 as estimated by dodecylsulfate polyacrylamide gel electrophoresis. Thus, the phosphorylated ribosomal protein found in starved Tetrahymena is apparently homologous with the ribosomal protein which is predominantly phosphorylated in higher eukaryotes. When phosphorylated ribosomes were dissociated by treatment with high concentration of KCl, the phosphorylated protein was found only on the small subunit. If dissociation was achieved by dialysis against a buffer low in MgCl2, the phosphorylated protein was distributed almost equally between the two subunits. This indicates that the phosphorylated ribosomal protein is located at the interface between the two subunits.

Animals↗