| 1. |
- Berglund, Gunilla, et al.
(författare)
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"Between Men" : A psychosocial rehabilitation programme for men with prostate cancer
- 2007
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Ingår i: Acta Oncologica. - : Informa UK Limited. - 0284-186X .- 1651-226X. ; 46:1, s. 83-89
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Tidskriftsartikel (refereegranskat)abstract
- The aim of this study was to evaluate the effect of psychosocial rehabilitation on newly diagnosed prostate cancer patients. The “Between Men” programme consisted of seven weekly sessions of physical training (Phys) alone, information (Info) alone or physical training plus information (PhysInfo). After diagnoses, patients (n =211) were consecutively included, stratified and randomised to one of four groups: Phys, Info, PhysInfo or standard care control (C). A nurse specialised in urology, an urologist and a physiotherapist performed the interventions. Patients were followed up during one year with mailed standardised questionnaires. It could not be assumed that the “Between Men” programme had any effect on patients’ anxiety and depression (HADS). Health-related quality of life (HRQOL) was associated with stage of disease but not with psychosocial intervention. Thus, Physical Function (PF), Role Function (RF) and Fatigue (FA) were inferior among patients with, than without, metastases of prostate cancer both at baseline and at the 12-month follow-up. This randomized study did not demonstrate any significant effect of psychosocial rehabilitation among prostate cancer patients. Considering the low rate (1/2), of included/eligible patients a less complicated design (intervention versus control) would have been preferred in order to increase power.
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| 2. |
- Dijken, Jan W.V. van, 1947-, et al.
(författare)
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Samarbete breddar forskning : Oral Biomaterialgruppen, Umeå
- 2008
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Ingår i: Tandläkartidningen. - : Sveriges Tandläkarförbund. ; 100:5, s. 74-79
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Tidskriftsartikel (populärvet., debatt m.m.)abstract
- Vid institutionen för odontologi vid Umeå Universitet finns en lång tradition av biomaterialforskning. För drygt två år sedan samlades större delen av den forskningen i ett vetenskapligt nätverk. Här beskrivs ett axplock av det breda forskningsarbetet.
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| 3. |
- Amisten, Stefan, et al.
(författare)
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Increased risk of acute myocardial infarction and elevated levels of C-reactive protein in carriersof the Thr-87 variant of the ATP receptor P2Y11.
- 2007
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Ingår i: European Heart Journal. - : Oxford University Press (OUP). - 1522-9645 .- 0195-668X. ; 28:1, s. 13-18
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Tidskriftsartikel (refereegranskat)abstract
- Aims Extracellular ATP acting on the P2Y(11) receptor regulates inflammatory cells. We hypothesized that polymorphisms in the receptor could influence the risk of acute myocardial infarction (AMI). Methods and results In the Malmo diet and cancer AMI case-control study (n = 3732) the P2Y(11) gene Thr-87 polymorphism was present in 19.8% of the controls and 22.9% in AMI patients (OR 1.21; P = 0.03). Stronger associations were found in patients with family history (FH) of AMI, 1.32; early-onset (EO) AMI, 1.43; or EO AMI combined with FH, 1.50; supporting a genetic mechanism. The Thr-87 homozygotes had an even greater risk of AMI, 1.94 (P = 0.04); and 2.48 in the EO AMI subgroup, suggesting a genetic dosage effect. In the cardiovascular risk factor group (n = 6055), 21.3% carried the Thr-87 allele. C-reactive protein was elevated in Thr-87 carriers: 1.6 mg/L vs. 1.3 mg/L (P = 0.001). No difference was seen for blood pressure, lipids, body mass index, smoking, or diabetes mellitus. Conclusion The common Ala-87-Thr polymorphism of the P2Y(11) receptor is associated with AMI and increased levels of C-reactive protein. We hypothesize that an inflammatory mechanism might be involved. The P2Y(11) receptor is a promising new drug target in the prevention of AMI.
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| 4. |
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| 5. |
- Berglund, Anders, et al.
(författare)
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Dimensional change of a calcium aluminate cement for posterior restorations in aqueous and dry media.
- 2006
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Ingår i: Dental Materials. - : Elsevier BV. - 0109-5641 .- 1879-0097. ; 22:5, s. 470-476
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Tidskriftsartikel (refereegranskat)abstract
- OBJECTIVES: A calcium aluminate cement has recently been developed, with claims of being an alternative to dental amalgam and resin composites in posterior cavities. However, its' mechanical properties are not well evaluated and the aim of the study was therefore, to evaluate its' dimensional stability over time. METHODS: The dimensional changes of the cement, Doxadent, and two composite resins, Esthet-X and InTen-S, were tested during 360 d. The specimens were stored at 37+/-1 degrees C either in 100% air humidity (dry) or immersed in distilled water (wet), except for the first 24h when all specimens were stored at 100% air humidity and 37+/-1 degrees C. RESULTS: During the first 24h, Doxadent decreased in volume with 0.04%, while InTen-S and Esthet-X decreased with 1.60 and 1.75%, respectively. From d 1-360, the dry Doxadent specimens increased in volume with 2.0% and in weight with 5.5%, while the corresponding increase for the wet specimens were 4.1 and 6.3%, respectively. The volume of both composites increased 0.8% or less in dry and wet conditions, while the increase in weight for InTen-S was 1.2% for the wet specimens and 0.6% for the dry. The corresponding figures for Esthet-X were 0.7 and 0.2%. SIGNIFICANCE: Doxadent was less dimensionally stable than the composites tested. Doxadent increased 2 times more in volume immersed in water than in 100% air humidity, while the increase in weight was almost similar. The clinical implications of the results found in the present study are uncertain. A material that continues to absorb water during prolonged periods and continues to react is questionable for clinical use.
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| 6. |
- Berglund, Anna-Karin, et al.
(författare)
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Civilsamhällets lokala genuskontrakt
- 2005
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Ingår i: Med periferien i sentrum. - Alta, Norge : Norut NIBR Finnmark. - 8275711479 ; , s. 235-255
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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| 7. |
- Berglund, Anna-Karin, et al.
(författare)
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Defining the Determinants for Dual Targeting of Amino Acyl-tRNA Synthetases to Mitochondria and Chloroplasts
- 2009
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Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 393:4, s. 803-814
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Tidskriftsartikel (refereegranskat)abstract
- Most of the organellar amino acyl-tRNA synthetases (aaRSs) are dually targeted to both mitochondria and chloroplasts using dual targeting peptides (dTPs). We have investigated the targeting properties and domain structure of dTPs of seven aaRSs by studying the in vitro and in vivo import of N-terminal deleted constructs of dTPs fused to green fluorescent protein. The deletion constructs were designed based on prediction programs, TargetP and Predotar, as well as LogoPlots derived from organellar proteomes in Arabidopsis thaliana. In vitro import was performed either into a single isolated organelle or as dual import (i.e., into a mixture of isolated mitochondria and chloroplasts followed by reisolation of the organelles). In vivo import was investigated as transient expression of the green fluorescent protein constructs in Nicotiana benthamiana protoplasts. Characterization of recognition determinants showed that the N-terminal portions of TyrRS-, ValRS- and ThrRS-dTPs (27, 22 and 23 amino acids, respectively) are required for targeting into both mitochondria and chloroplasts. Surprisingly, these N-terminal portions contain no or very few arginines (or lysines) but very high number of hydroxylated residues (26–51%). For two aaRSs, a domain structure of the dTP became evident. Removal of 20 residues from the dTP of ProRS abolished chloroplastic import, indicating that the N-terminal region was required for chloroplast targeting, whereas deletion of 16 N-terminal amino acids from AspRS-dTP inhibited the mitochondrial import, showing that in this case, the N-terminal portion was required for the mitochondrial import. Finally, deletion of N-terminal regions of dTPs for IleRS and LysRS did not affect dual targeting. In summary, it can be concluded that there is no general rule for how the determinants for dual targeting are distributed within dTPs; in most cases, the N-terminal portion is essential for import into both organelles, but in a few cases, a domain structure was observed.
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| 8. |
- Berglund, Anna-Karin, 1979-
(författare)
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Dual Targeting of Proteins to Mitochondria and Chloroplasts
- 2009
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- The vast majority of mitochondrial and chloroplastic proteins are nuclear encoded, synthesized in the cytosol and imported into the respective organelle using an N-terminal extension, the targeting peptide (TP). After import into the organelle, the TP is cleaved off and degraded by the Presequence protease (PreP). The import process is thought to be highly specific, however there is a group of proteins that are localised to both mitochondria and chloroplasts, using an ambiguous, dual targeting peptide (dTP). The aim of this thesis was to investigate targeting properties of dTPs. Analysis of the amino acid content of all currently known dually targeted proteins revealed that the dTPs are enriched in hydroxylated, hydrophobic and positively charged residues, lacking acidic residues, whereas the content of serine, arginine and proline is intermediary in comparison to the mitochondrial and chloroplastic TPs. dTPs do not form amphiphilic a-helices, characteristic of the mitochondrial TPs, but the helical structure can be induced in membrane mimetic environment, as revealed by spectroscopic studies of a dTP of an aminoacyl- tRNA-synthetase (aaRS). In vitro and in vivo import experiments of fusion constructs containing N-terminal truncations of seven aaRS-dTPs coupled to green fluorescent protein (GFP) demonstrated different organisation of targeting determinants showing that the N-terminal portion of dTPs was crucial for import into both organelles or at least one organelle for different constructs. In addition, studies of targeting capacity of the TPs of PreP homologues from plant, mammal and yeast (AtPreP, hPreP and Mop112) showed species dependent intra-mitochondrial localisation of the coupled GFP and demonstrated functional complementation of an intermembrane space located Mop112 with a matrix located AtPreP. The studies presented here contribute to understanding of the intracellular and intra-mitochondrial sorting process of proteins in the eukaryotic cell.
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| 9. |
- Berglund, Anna-Karin, et al.
(författare)
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Dual Targeting to Mitochondria and Chloroplasts : Characterization of Thr–tRNA Synthetase Targeting Peptide
- 2009
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Ingår i: Molecular Plant. - Shanghai : Oxford University Press. - 1674-2052. ; 2:6, s. 1298-1309
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Tidskriftsartikel (refereegranskat)abstract
- There is a group of proteins that are encoded by a single gene, expressed as a single precursor protein and dually targeted to both mitochondria and chloroplasts using an ambiguous targeting peptide. Sequence analysis of 43 dual targeted proteins in comparison with 385 mitochondrial proteins and 567 chloroplast proteins of Arabidopsis thaliana revealed an overall significant increase in phenylalanines, leucines, and serines and a decrease in acidic amino acids and glycine in dual targeting peptides (dTPs). The N-terminal portion of dTPs has significantly more serines than mTPs. The number of arginines is similar to those in mTPs, but almost twice as high as those in cTPs. We have investigated targeting determinants of the dual targeting peptide of Thr-tRNA synthetase (ThrRS-dTP) studying organellar import of N- and C-terminal deletion constructs of ThrRS-dTP coupled to GFP. These results show that the 23 amino acid long N-terminal portion of ThrRS-dTP is crucial but not sufficient for the organellar import. The C-terminal deletions revealed that the shortest peptide that was capable of conferring dual targeting was 60 amino acids long. We have purified the ThrRS-dTP(2-60) to homogeneity after its expression as a fusion construct with GST followed by CNBr cleavage and ion exchange chromatography. The purified ThrRS-dTP(2-60) inhibited import of pF(1)beta into mitochondria and of pSSU into chloroplasts at mu M concentrations showing that dual and organelle-specific proteins use the same organellar import pathways. Furthermore, the CD spectra of ThrRS-dTP(2-60) indicated that the peptide has the propensity for forming alpha-helical structure in membrane mimetic environments; however, the membrane charge was not important for the amount of induced helical structure. This is the first study in which a dual targeting peptide has been purified and investigated by biochemical and biophysical means.
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