Rapid adaptation of the intrarenal resistance index after living donor kidney transplantation

Background. Limited data exist concerning changes of renal perfusion directly after kidney transplantation. Colour-coded duplex sonography is the accepted method to assess kidney perfusion after transplantation. A widely used, although unspecific, Doppler parameter is the intrarenal resistance index (RI). The aim of this study was to clarify the influence of different patient- and procedure-related factors on RI before and immediately after living kidney transplantation. Methods. In a prospective study, 80 living kidney transplantation donor-recipient pairs were included. RI was measured in the donor 1 to 3 days before nephrectomy and in the recipient during the first hour after transplantation to examine the influence of age, heart rate, duration of cold and warm ischaemia time and immunosuppressive medications. Results. Mean RI did not differ between donors and recipients. RI correlated with age, both in donors (r = 0.58, P < 0.001) and recipients (r = 0.39, P < 0.001). In recipients, 10 or more years younger than their donors (n = 24), an average decrease of 0.05 in RI compared to the donors' value was observed (P = 0.01). Heart rate, cold and warm ischaemia time and immunosuppressive medications had no influence on the recipient RI. In patients with delayed graft function, a significant increase in RI within 14 days was observed. However, the initial RI was not predictive of graft function. Conclusions. The transplanted kidney seems to be able to adjust its RI within a short time despite several potential harmful factors that can occur during the transplantatio

Effects of percutaneous transluminal angioplasty on muscle BOLD-MRI in patients with peripheral arterial occlusive disease: preliminary results

The purpose was to evaluate the effect of percutaneous transluminal angioplasty (PTA) of the superficial femoral artery (SFA) on the blood oxygenation level-dependent (BOLD) signal change in the calf musculature of patients with intermittent claudication. Ten patients (mean age, 63.4 ± 11.6years) with symptomatic peripheral arterial occlusive disease (PAOD) caused by SFA stenoses were investigated before and after PTA. Patients underwent BOLD-MRI 1 day before and 6 weeks after PTA. A T2*-weighted single-shot multi-echo echo-planar MR-imaging technique was applied. The BOLD measurements were acquired at mid-calf level during reactive hyperaemia at 1.5 T. This transient hyperperfusion of the muscle tissue was provoked by suprasystolic cuff compression. Key parameters describing the BOLD signal curve included maximum T2* (T2*max), time-to-peak to reach T2*max (TTP) and T2* end value (EV) after 600 s of hyperemia. Paired t-tests were applied for statistic comparison. Between baseline and post-PTA, T2*max increased from 11.1 ± 3.6% to 12.3 ± 3.8% (p = 0.51), TTP decreased from 48.5 ± 20.8 s to 35.3 ± 11.6s (p = 0.11) and EV decreased from 6.1 ± 6.4% to 5.0 ± 4.2% (p = 0.69). In conclusion, BOLD-MRI reveals changes of the key parameters T2*max, TTP, and EV after successful PTA of the calf muscles during reactive hyperaemi

Dark state experiments with ultracold, deeply-bound triplet molecules

We examine dark quantum superposition states of weakly bound Rb2 Feshbach molecules and tightly bound triplet Rb2 molecules in the rovibrational ground state, created by subjecting a pure sample of Feshbach molecules in an optical lattice to a bichromatic Raman laser field. We analyze both experimentally and theoretically the creation and dynamics of these dark states. Coherent wavepacket oscillations of deeply bound molecules in lattice sites, as observed in one of our previous experiments, are suppressed due to laser-induced phase locking of molecular levels. This can be understood as the appearance of a novel multilevel dark state. In addition, the experimental methods developed help to determine important properties of our coupled atom / laser system.Comment: 20 pages, 9 figure

Pressure indices in peripheral arterial disease assessed by infrared photosensors

Ankle-brachial index (ABI) assessment by Doppler is operator dependent and limited in calcified arteries. For the detection of peripheral arterial disease (PAD), we evaluated ABI and toe-finger (ToFi) pressures by infrared (IR) sensors at the digits and compared with standard Doppler (Doppler-ABI) in 100 patients with PAD and in 15 controls. Pressure indices were obtained in 86% for Doppler-ABI, 82% for IR-ABI, and 94% for IR-ToFi (P < .01). According to Bland-Altmann analysis, IR-ABI and Doppler-ABI are exchangeable (limits of agreement [loa] -0.30; 0.30, bias -0.003, 95% confidence interval [CI] -0.02; 0.02), whereas IR-ToFi was not (loa -0.23; 0.61, bias of 0.2, 95% CI 0.16; 0.23). The IR-ToFi revealed the best inter- and intrarater agreement (0.92/0.98) followed by IR-ABI (0.74/0.98) and Doppler-ABI (0.66/0.89). Ankle-brachial arterial pressure index can be assessed by IR photosensors. Although toe-finger index is not exchangeable with standard Doppler, it will need further exploration to define its value for the diagnosis of PAD due to its excellent inter- and intrarater agreement

Human AlkB Homologue 5 Is a Nuclear 2-Oxoglutarate Dependent Oxygenase and a Direct Target of Hypoxia-Inducible Factor 1α (HIF-1α)

Human 2-oxoglutarate oxygenases catalyse a range of biological oxidations including the demethylation of histone and nucleic acid substrates and the hydroxylation of proteins and small molecules. Some of these processes are centrally involved in regulation of cellular responses to hypoxia. The ALKBH proteins are a sub-family of 2OG oxygenases that are defined by homology to the Escherichia coli DNA-methylation repair enzyme AlkB. Here we report evidence that ALKBH5 is probably unique amongst the ALKBH genes in being a direct transcriptional target of hypoxia inducible factor-1 (HIF-1) and is induced by hypoxia in a range of cell types. We show that purified recombinant ALKBH5 is a bona fide 2OG oxygenase that catalyses the decarboxylation of 2OG but appears to have different prime substrate requirements from those so far defined for other ALKBH family members. Our findings define a new class of HIF-transcriptional target gene and suggest that ALKBH5 may have a role in the regulation of cellular responses to hypoxia

Controlling a magnetic Feshbach resonance with laser light

The capability to tune the strength of the elastic interparticle interaction is crucial for many experiments with ultracold gases. Magnetic Feshbach resonances are a tool widely used for this purpose, but future experiments would benefit from additional flexibility such as spatial modulation of the interaction strength on short length scales. Optical Feshbach resonances offer this possibility in principle, but suffer from fast particle loss due to light-induced inelastic collisions. Here we show that light near-resonant with a molecular bound-to-bound transition can be used to shift the magnetic field at which a magnetic Feshbach resonance occurs. This makes it possible to tune the interaction strength with laser light and at the same time induce considerably less loss than an optical Feshbach resonance would do

Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth

Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydroxylation of the small ribosomal subunit protein RPS23. Like OGFOD1, Sud1 catalyzes a single prolyl-hydroxylation of RPS23 in contrast to yeast Tpa1p, where Pro-64 dihydroxylation is observed. RNAi-mediated Sud1 knockdown hinders normal growth in different Drosophila tissues. Growth impairment originates from both reduction of cell size and diminution of the number of cells and correlates with impaired translation efficiency and activation of the unfolded protein response in the endoplasmic reticulum. This is accompanied by phosphorylation of eIF2α and concomitant formation of stress granules, as well as promotion of autophagy and apoptosis. These observations, together with those on enzyme homologs described in the companion articles, reveal conserved biochemical and biological roles for a widely distributed ribosomal oxygenase.Fil: Katz, Maximiliano Javier. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Acevedo, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Loenarz, Christoph. University of Oxford; Reino UnidoFil: Galagovsky, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Liu Yi, Phebee. University Of Oxford; Reino UnidoFil: Pérez, Marcelo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Thalhammer, Armin. University of Oxford; Reino UnidoFil: Sekirnik, Rok. University Of Oxford; Reino UnidoFil: Ge, Wei. University of Oxford; Reino UnidoFil: Melani, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Thomas, Maria Gabriela. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Simonetta, Sergio Hernan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Boccaccio, Graciela Lidia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Schofield, Christoper J. University of Oxford; Reino UnidoFil: Cockman, Matthew E. University of Oxford; Reino UnidoFil: Ratcliffe, Peter J. University of Oxford; Reino UnidoFil: Wappner, Pablo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentin

Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth

Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydroxylation of the small ribosomal subunit protein RPS23. Like OGFOD1, Sud1 catalyzes a single prolyl-hydroxylation of RPS23 in contrast to yeast Tpa1p, where Pro-64 dihydroxylation is observed. RNAi-mediated Sud1 knockdown hinders normal growth in different Drosophila tissues. Growth impairment originates from both reduction of cell size and diminution of the number of cells and correlates with impaired translation efficiency and activation of the unfolded protein response in the endoplasmic reticulum. This is accompanied by phosphorylation of eIF2α and concomitant formation of stress granules, as well as promotion of autophagy and apoptosis. These observations, together with those on enzyme homologs described in the companion articles, reveal conserved biochemical and biological roles for a widely distributed ribosomal oxygenase.Fil: Katz, Maximiliano Javier. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Acevedo, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Loenarz, Christoph. University of Oxford; Reino UnidoFil: Galagovsky, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Liu Yi, Phebee. University Of Oxford; Reino UnidoFil: Pérez, Marcelo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Thalhammer, Armin. University of Oxford; Reino UnidoFil: Sekirnik, Rok. University Of Oxford; Reino UnidoFil: Ge, Wei. University of Oxford; Reino UnidoFil: Melani, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Thomas, Maria Gabriela. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Simonetta, Sergio Hernan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Boccaccio, Graciela Lidia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Schofield, Christoper J. University of Oxford; Reino UnidoFil: Cockman, Matthew E. University of Oxford; Reino UnidoFil: Ratcliffe, Peter J. University of Oxford; Reino UnidoFil: Wappner, Pablo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentin