| 1. |
- Agardh, Elisabet, et al.
(författare)
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Normal eyes in type 1 diabetics stay normal after one year of treatment with continuous subcutaneous insulin pump
- 1986
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Ingår i: Acta Ophthalmologica. - 0001-639X. ; 64:5, s. 530-532
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Tidskriftsartikel (refereegranskat)abstract
- Seven patients with type 1 diabetes mellitus were restored to near normoglycaemia by treatment with continuous subcutaneous insulin infusion pumps (CSII). The patients were examined with ophthalmoscopy, fundus photography and fluorescein angiography before and one year after the start of CSII treatment. In addition, ophthalmoscopy was performed after 6 months of treatment. All 14 eyes were normal prior to the CSII treatment and none had developed any signs of retinopathy after 6 months or 1 year. It is concluded that metabolic control can be near normalized with CSII treatment without any risk for development of diabetic microangiopathy in type 1 diabetics with normal eyes.
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| 2. |
- Bauer, Karolina, 1975-
(författare)
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Diazotrophy and diversity of benthic cyanobacteria in tropical coastal zones
- 2007
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Discoveries in recent years have disclosed the importance of marine cyano-bacteria in the context of primary production and global nitrogen cycling. It is hypothesized here that microbial mats in tropical coastal habitats harbour a rich diversity of previously uncharacterized cyanobacteria and that benthic marine nitrogen fixation in coastal zones is substantial.A polyphasic approach was used to investigate cyanobacterial diversity in three tropical benthic marine habitats of different characters; an intertidal sand flat and a mangrove forest floor in the Indian Ocean, and a beach rock in the Pacific Ocean. In addition, nitrogenase activity was measured over diel cycles at all sites. The results revealed high cyanobacterial diversity, both morphologically and genetically. Substantial nitrogenase activity was observed, with highest rates at daytime where heterocystous species were present. However, the three habitats were dominated by non-heterocystous and unicellular genera such as Microcoleus, Lyngbya, Cyanothece and a large group of thin filamentous species, identified as members of the Pseudanabaenaceae family. In these consortia nocturnal nitrogenase activities were highest and nifH sequencing also revealed presence of non-cyanobacterial potential diazotrophs. A conclusive phylogenetic analysis of partial nifH sequences from the three sites and sequences from geographi-cally distant microbial mats revealed new clusters of benthic potentially ni-trogen-fixing cyanobacteria. Further, the non-heterocystous cyanobacterium Lyngbya majuscula was subjected to a physiological characterization to gain insights into regulatory aspects of its nitrogen fixation. The data demon-strated that nitrogenase activity is restricted to darkness, which called upon a re-evaluation of its diazotrophic behaviour.
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| 6. |
- Bauer, Mikael, et al.
(författare)
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Zn2+ binding to human calbindin D(28k) and the role of histidine residues.
- 2008
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Ingår i: Protein Science. - : Wiley. - 1469-896X .- 0961-8368. ; 17:4, s. 760-767
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Tidskriftsartikel (refereegranskat)abstract
- We have studied the binding of Zn2+ to the hexa EF-hand protein, calbindin D(28k)-a strong Ca2+-binder involved in apoptosis regulation-which is highly expressed in brain tissue. By use of radioblots, isothermal titration calorimetry, and competition with a fluorescent Zn2+ chelator, we find that calbindin D(28k) binds Zn2+ to three rather strong sites with dissociation constants in the low micromolar range. Furthermore, we conclude based on spectroscopic investigations that the Zn2+-bound state is structurally distinct from the Ca2+-bound state and that the two forms are incompatible, yielding negative allosteric interaction between the zinc- and calcium-binding events. ANS titrations reveal a change in hydrophobicity upon binding Zn2+. The binding of Zn2+ is compatible with the ability of calbindin to activate myo-inositol monophosphatase, one of the known targets of calbindin. Through site-directed mutagenesis, we address the role of cysteine and histidine residues in the binding of Zn2+. Mutation of all five cysteines into serines has no effect on Zn2+-binding affinity or stoichiometry. However, mutating histidine 80 into a glutamine reduces the binding affinity of the strongest Zn2+ site, indicating that this residue is involved in coordinating the Zn2+ ion in this site. Mutating histidines 5, 22, or 114 has significantly smaller effects on Zn2+-binding affinity.
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| 7. |
- Behnen, Petra, et al.
(författare)
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Calcium-Dependent Interaction of Calmodulin with Human 80S Ribosomes and Polyribosomes.
- 2012
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 51:34, s. 6718-6727
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Tidskriftsartikel (refereegranskat)abstract
- Ribosomes are the protein factories of every living cell. The process of protein translation is highly complex and tightly regulated by a large number of diverse RNAs and proteins. Earlier studies indicate that Ca(2+) plays a role in protein translation. Calmodulin (CaM), a ubiquitous Ca(2+)-binding protein, regulates a large number of proteins participating in many signaling pathways. Several 40S and 60S ribosomal proteins have been identified to interact with CaM, and here, we report that CaM binds with high affinity to 80S ribosomes and polyribosomes in a Ca(2+)-dependent manner. No binding is observed in buffer with 6 mM Mg(2+) and 1 mM EGTA that chelates Ca(2+), suggesting high specificity of the CaM-ribosome interaction dependent on the Ca(2+) induced conformational change of CaM. The interactions between CaM and ribosomes are inhibited by synthetic peptides comprising putative CaM-binding sites in ribosomal proteins S2 and L14. Using a cell-free in vitro translation system, we further found that these synthetic peptides are potent inhibitors of protein synthesis. Our results identify an involvement of CaM in the translational activity of ribosomes.
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| 10. |
- Eksandh, Louise, et al.
(författare)
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Different clinical expressions in two families with Stargardt's macular dystrophy (STGD1)
- 2001
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Ingår i: Acta Ophthalmologica Scandinavica. - : Wiley. - 1395-3907. ; 79:5, s. 524-530
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Tidskriftsartikel (refereegranskat)abstract
- Purpose: To describe the clinical expressions, with emphasis on electrophysiological examinations, in two Swedish families with Stargardt's macular dystrophy (STGD1). Methods. Two pairs of siblings with STGD1, for whom diagnosis had been confirmed by genetic linkage to the ABCA4 gene region, were examined regarding visual acuity, kinetic perimetry, fundus photography, full-field ERG and multifocal ERG (MERG). Possible disease-causing mutations were screened for by DNA sequencing of selected regions of the ABCA4 gene. Results. All STGD1 patients, had visual acuity 0.07-0.1. The two families presented different fundus appearances, MERGs and implicit times on. 30 Hz flicker white light full-field ERGs. Genetic analysis revealed one unique sequence variation in exon 19 of the ABCA4 gene, in one allele from the patients of one of the families. This point mutation causes the amino acid substitution T972N in the ABCR protein. Conclusion. Two pairs of siblings with STGD1 presented two different expressions of the disease regarding the distribution of the retinal dysfunction. One possible molecular explanation to the different clinical expressions may be the T972N substitution present in the ABCR protein in one of the STGD1 families investigated.
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