Investigation on the coordinate structures of the rare earth metal complexes with edta and cydta ligands

0　IntroductionThegreatattentionhasbeenpaidtorareearthorradioactiverareearthmetalcomplexesfortheirvariousbiologicactivi ties[1 3] .Forexamples,theradioactiverareearthmetal1 53SmⅢ com plexeswerewidelyusedfortumourtherapyofbrain ,liver,lung ,heartandbonetissues[4 5] ;forrareearthmetalEuⅢandTbⅢemitinguniquefluorescence ,theircompoundswereappliedfordiagnosesofvariousdiseases[6 ,7] ;forrareearthmetalGdⅢcontainingthemosthigh spinsingleelectrons,itscomplexeswereusuallyusedforcontrastagentsofmag…     

Iron-mediated inhibition of H+-ATPase in plasma membrane vesicles isolated from wheat roots

The mechanisms of iron-mediated inhibition of the H(+)-ATPase activity of plasma membrane (PM) vesicles isolated from wheat roots were investigated. Both FeSO(4) and FeCl(3) significantly inhibited PM H(+)-ATPase activity, and the inhibition could be reversed by the addition of the metal ion chelator EDTA-Na(2) or a specific Fe(2+) chelator, indicating that the inhibitory effect was due to specific action of Fe(2+) or Fe(3+). Measurement of the extent of lipid peroxidation showed that oxidative damage on the PM caused by Fe(2+) or Fe(3+) seemed to be correlated with the inhibition of PM H(+)-ATPase activity. However, prevention of lipid peroxidation with butylated hydroxytoluene did not affect iron-mediated inhibition in the PM H(+)-ATPase, suggesting that the inhibition of the PM H(+)-ATPase was not a consequence of lipid peroxidation caused by iron. Investigation of the effects of various reactive oxygen species scavengers on the iron-mediated inhibition of H(+)-ATPase activity indicated that hydroxyl radicals (*OH) and hydrogen peroxide (H(2)O(2)) might be involved in the Fe(2+)-mediated decrease in PM H(+)-ATPase activity. Moreover, iron caused a decrease in plasma protein thiol (P-SH), and Fe(3+) brought a higher degree of oxidation in thiol groups than Fe(2+) at the same concentration. Modification of the thiol redox state in the PM suggested that reducing thiol groups were essential to maintain PM H(+)-ATPase activity. Incubation of the specific thiol modification reagent 5,5-dithio-bis(2-nitrobenzoic acid) with the rightside-out and inside-out PM revealed that thiol oxidation occurred at the apoplast side of the PM. Western blotting analysis revealed a decrease in H(+)-ATPase content caused by iron. Taken together, these results suggested that thiol oxidation might account for the inhibition of PM H(+)-ATPase caused by iron, and that *OH and H(2)O(2) were also involved in Fe(2+)-mediated inhibition.     

Dynamic balancing of dual-rotor system with very little rotating speed difference

Unbalanced vibration in dual-rotor rotating machinery was studied with numerical simulations and experiments. A new method is proposed to separate vibration signals of inner and outer rotors for a system with very little difference in rotating speeds. Magnitudes and phase values of unbalance defects can be obtained directly by sampling the vibration signal synchronized with reference signal. The balancing process is completed by the reciprocity influence coefficients of inner and outer rotors method. Results showed the advantage of such method for a dual-rotor system as compared with conventional balancing.     

Homocysteine increases the synthesis of adrenomedullin in vascular fibroblasts of rats

Homocysteine (Hcy), a highly reactive sulfur- containing amino acid, is an intermediate product of methionine metabolism. Elevation of plasma Hcy has been widely studied as an independent risk factor for many cardiovascular diseases such as atherosclerosis, thrombosis, etc.[1]. Inherited hyperhomocysteinemia cases usually suffer from occlusion or thrombosis in arteries and large veins before the age of 20. Hyperhomocysteinemia significantly reduces the survival rate[2] and dilatation functi…     

Single-crystal gallium nitride nanotubes

Since the discovery of carbon nanotubes in 1991 (ref. 1), there have been significant research efforts to synthesize nanometre-scale tubular forms of various solids. The formation of tubular nanostructure generally requires a layered or anisotropic crystal structure. There are reports of nanotubes made from silica, alumina, silicon and metals that do not have a layered crystal structure; they are synthesized by using carbon nanotubes and porous membranes as templates, or by thin-film rolling. These nanotubes, however, are either amorphous, polycrystalline or exist only in ultrahigh vacuum. The growth of single-crystal semiconductor hollow nanotubes would be advantageous in potential nanoscale electronics, optoelectronics and biochemical-sensing applications. Here we report an 'epitaxial casting' approach for the synthesis of single-crystal GaN nanotubes with inner diameters of 30-200 nm and wall thicknesses of 5-50 nm. Hexagonal ZnO nanowires were used as templates for the epitaxial overgrowth of thin GaN layers in a chemical vapour deposition system. The ZnO nanowire templates were subsequently removed by thermal reduction and evaporation, resulting in ordered arrays of GaN nanotubes on the substrates. This templating process should be applicable to many other semiconductor systems.     

Folding at the speed limit

Many small proteins seem to fold by a simple process explicable by conventional chemical kinetics and transition-state theory. This assumes an instant equilibrium between reactants and a high-energy activated state. In reality, equilibration occurs on timescales dependent on the molecules involved, below which such analyses break down. The molecular timescale, normally too short to be seen in experiments, can be of a significant length for proteins. To probe it directly, we studied very rapidly folding mutants of the five-helix bundle protein lambda(6-85), whose activated state is significantly populated during folding. A time-dependent rate coefficient below 2 micro s signals the onset of the molecular timescale, and hence the ultimate speed limit for folding. A simple model shows that the molecular timescale represents the natural pre-factor for transition state models of folding.     

De novo deletions of SNRPN exon 1 in early human and mouse embryos result in a paternal to maternal imprint switch

Prader-Willi syndrome (PWS) is a neurogenetic disease characterized by infantile hypotonia, gonadal hypoplasia, obsessive behaviour and neonatal feeding difficulties followed by hyperphagia, leading to profound obesity. PWS is due to a lack of paternal genetic information at 15q11-q13 (ref. 2). Five imprinted, paternally expressed genes map to the PWS region, MKRN3 (ref. 3), NDN (ref. 4), NDNL1 (ref. 5), SNRPN (refs 6-8 ) and IPW (ref. 9), as well as two poorly characterized framents designated PAR-1 and PAR-5 (ref. 10). Imprinting of this region involves a bipartite 'imprinting centre' (IC), which overlaps SNRPN (refs 10,11). Deletion of the SNRPN promoter/exon 1 region (the PWS IC element) appears to impair the establishment of the paternal imprint in the male germ line and leads to PWS. Here we report a PWS family in which the father is mosaic for an IC deletion on his paternal chromosome. The deletion chromosome has acquired a maternal methylation imprint in his somatic cells. We have made identical findings in chimaeric mice generated from two independent embryonic stem (ES) cell lines harbouring a similar deletion. Our studies demonstrate that the PWS IC element is not only required for the establishment of the paternal imprint, but also for its postzygotic maintenance.     

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. Suppression of nicastrin expression in Caenorhabditis elegans embryos induces a subset of notch/glp-1 phenotypes similar to those induced by simultaneous null mutations in both presenilin homologues of C. elegans (sel-12 and hop-1). Nicastrin also binds carboxy-terminal derivatives of beta-amyloid precursor protein (betaAPP), and modulates the production of the amyloid beta-peptide (A beta) from these derivatives. Missense mutations in a conserved hydrophilic domain of nicastrin increase A beta42 and A beta40 peptide secretion. Deletions in this domain inhibit A beta production. Nicastrin and presenilins are therefore likely to be functional components of a multimeric complex necessary for the intramembranous proteolysis of proteins such as Notch/GLP-1 and betaAPP.     

A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae

Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here.