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L Björkhem

Publications and source records attributed to L Björkhem.

4 recordsLinked to original sources
PubMed2001

Increased levels of cytosolic thioredoxin reductase activity and mRNA in rat liver nodules.

BACKGROUND/AIMS: Thioredoxin reductase, a redox active enzyme, is induced in several tumors. This study focuses on the presence of and subcellular localisation of thioredoxin reductase in a tumor model where neoplastic lesions are selected by their resistance to the toxic effects of the promotor. METHODS: Liver nodules produced by intermittent feeding of 2-acetylaminofluorene to male Wistar rats were analyzed for thioredoxin reductase (TrxR) activity and mRNA. RESULTS: This activity was increased 3.5-fold in the cytosol but decreased 60% in the mitochondrial fraction compared to the liver of age-matched untreated animals. Only traces of activity were observed in the microsomal, plasma membrane and nuclear fractions from normal liver or nodules. The level of TrxR mRNA was 3-fold higher in nodules than in normal rat liver. Furthermore, the total level of SH groups in homogenates was 2-fold higher in the case of the nodules. CONCLUSIONS: These findings indicate that the thioredoxin system makes an important contribution to the resistant phenotype of the neoplastic liver cell, which conveys a growth advantage of significance for tumor progression.

2-Acetylaminofluorene↗
PubMed2001

[John Bjorkhem and hypnosis].

Hypnosis has been recognised for thousands of years and is believed to have originated from shamanic trance methods. It has always been controversial in medical science. The biography of the Swedish physician John Björkhem and the history of hypnosis in Swedish medicine during the 20th century is intimately related to each other. Björkhem devoted most of his professional life to the phenomenon of hypnosis. He had a unique background for his studies as a priest, physician and psychologist. He always regarded hypnosis to have a great potential both as a therapeutical and as a diagnostic tool. He was fascinated by the mysteric undertones in his results from the hypnotic experiments and he devoted great time to parapsychology. In this essay we describe an outsider in medicine, both with respect to person and topic. In the case of Björkhem the situation was particular complicated because of his multidisciplinary activities with three different faculties involved. Finally the essay deals with the condition of a pioneer, and his struggle for acceptance and understanding. Only future can tell if the visions that Björkhem had about hypnosis as an efficient therapeutic tool in medicine will come true.

History, 20th Century↗
PubMed1997

Selenium and the thioredoxin and glutaredoxin systems.

Thioredoxin (Trx) is a small ubiquitous dithiol protein which together with the FAD-containing enzyme thioredoxin reductase (TR) and NADPH (the Trx system) is a hydrogen donor for ribonucleotide reductase essential for DNA synthesis and a general protein disulfide reductase involved in redox regulation. Selenite, selenodiglutathione (GS-Se-SG) and selenocystine are efficiently reduced by thioredoxins and also directly by NADPH and mammalian TR but not by the E. coli enzyme. Incubation of selenite or GS-Se-SG with the Trx system or with mammalian TR results in a rapid formation of selenide, which by redox cycling with oxygen may cause a large non-stoichiometric oxidation of NADPH. Selenocystine is efficiently reduced into two molecules of the selenol amino acid selenocysteine by mammalian TR with a K(m)-value (6 mumol.L-1) and a high turnover number (kappa cat 3200 min-1) almost identical to the natural substrate Trx-S2. TR also directly reduces lipid hydroperoxides and this peroxidase reaction is strongly stimulated by the presence of catalytic amounts of free selenocysteine. Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione. Selenate is reduced by Grx and Trx in the presence of GSH. The DNA-binding of the transcription factor AP-1 is strongly inhibited by GS-Se-SG and selenite. Furthermore, selenide formed by TR-mediated reduction of selenite and GS-Se-SG inhibits lipoxygenase and changes the electron spin resonance spectrum of the active site iron. Mammalian TR with two subunits of 57 kDa has recently been cloned and shown to be homologous to glutathione reductase. The rat enzyme contains a selenocysteine residue in a unique Cterminal position and a conserved SECIS sequence directing insertion of the selenocysteine. The discovery of selenocysteine in mammalian TR may explain the broad substrate specificity of the enzyme and the requirement of selenium for cell proliferation.

Amino Acid Sequence↗