Background

Hyperbranched polymers represent a new class of drug delivery vehicle that can be used to prepare nanoparticles with uniform size distribution.

Methods

In this study we prepared covalent conjugates between the photosensitizer chlorin(e6) and hyperbranched poly(ether-ester), HPEE. HPEE-ce6 nanoparticles were synthesized by carbodiimide-mediated reaction between HPEE and ce6, and characterized by ultraviolet-visible absorption spectroscopy (UV-Vis), and transmission electron microscopy (TEM). The uptake and phototoxicity of HPEE-ce6 nanoparticles towards human oral tongue cancer CAL-27 cells was detected by confocal laser scanning microscopy (CLSM) and MTT assay respectively.

Results

The absorption peak of HPEE-ce6 nanoparticles was red-shifted 12-nm compared with ce6, and TEM showed uniform nanoparticles with a diameter of 50-nm. HPEE-ce6 nanoparticles were taken up by CAL-27 cells after 4 hour incubation and localized in the cytoplasm. The MTT assay showed a significantly (P<0.05) higher phototoxicity compared to free ce6 after 12 J/cm2 of 660-nm laser illumination.

Conclusions

This is the first time to our knowledge that hyperbranched polymers have been used in PDT drug delivery.

The crystal structure of the title compound, C16H20BrNO3, contains three chiral centers in the configuration 1R,2S,6R. The cyclo­hexane ring is in a chair conformation. In the crystal, mol­ecules are linked by weak C—H⋯O inter­actions, forming chains along the a-axis direction.

Background

Sepsis is a common syndrome in critically ill patients and easily leads to the occurrence of acute kidney injury (AKI), with high mortality rates. This study aimed to investigate the diagnostic value of urine soluble CD163 (sCD163) for identification of sepsis, severity of sepsis, and for secondary AKI, and to assess the patients’ prognosis.

Methods

We enrolled 20 cases with systemic inflammatory response syndrome (SIRS), 40 cases with sepsis (further divided into 17 sepsis cases and 23 severe sepsis cases) admitted to the intensive care unit (ICU), and 20 control cases. Results for urine sCD163 were recorded on the day of admission to the ICU, and AKI occurrence was noted.

Results

On the day of ICU admission, the sepsis group exhibited higher levels of urine sCD163 (74.8 ng/ml; range: 47.9-148.3 ng/ml) compared with those in the SIRS group (31.9 ng/ml; 16.8-48.0, P < 0.001). The area under the curve (AUC) was 0.83 (95% confidence interval [CI]: 0.72-0.94, P < 0.001) the sensitivity was 0.83, and the specificity was 0.75 (based on a cut-off point of 43.0 ng/ml). Moreover, the severe sepsis group appeared to have a higher level of sCD163 compared with that in the sepsis group (76.2; 47.2-167.5 ng/ml vs. 74.2; 46.2-131.6 ng/ml), but this was not significant. For 15 patients with AKI, urine sCD163 levels at AKI diagnosis were significantly higher than those of the remaining 35 sepsis patients upon ICU admission (121.0; 74.6-299.1 ng/ml vs. 61.8; 42.8-128.3 ng/ml, P = 0.049). The AUC for urine sCD163 was 0.688 (95% CI: 0.51-0.87, P = 0.049). Sepsis patients with a poor prognosis showed a higher urine sCD163 level at ICU admission (98.6; 50.3-275.6 ng/ml vs. 68.0; 44.8-114.5 ng/ml), but this was not significant. Patients with AKI with a poor prognosis had higher sCD163 levels than those in patients with a better prognosis (205.9; 38.6-766.0 ng/ml vs. 80.9; 74.9-141.0 ng/ml), but this was not significant.

Conclusions

This study shows, for the first time, the potential value of urine sCD163 levels for identifying sepsis and diagnosing AKI, as well as for assessment of patients’ prognosis.

Trial Registration

ChiCTR-ONC-10000812

Background

The purpose of this study was to explore the diagnostic value of soluble triggering receptor expressed on myeloid cells 1 (sTREM-1), procalcitonin (PCT), and C-reactive protein (CRP) serum levels for differentiating sepsis from SIRS, identifying new fever caused by bacteremia, and assessing prognosis when new fever occurred.

Methods

We enrolled 144 intensive care unit (ICU) patients: 60 with systemic inflammatory response syndrome (SIRS) and 84 with sepsis complicated by new fever at more than 48 h after ICU admission. Serum sTREM-1, PCT, and CRP levels were measured on the day of admission and at the occurrence of new fever (>38.3°C) during hospitalization. Based on the blood culture results, the patients were divided into a blood culture-positive bacteremia group (33 patients) and blood culture-negative group (51 patients). Based on 28-day survival, all patients, both blood culture-positive and -negative, were further divided into survivor and nonsurvivor groups.

Results

On ICU day 1, the sepsis group had higher serum sTREM-1, PCT, and CRP levels compared with the SIRS group (P <0.05). The areas under the curve (AUC) for these indicators were 0.868 (95% CI, 0.798–0.938), 0.729 (95% CI, 0.637–0.821), and 0.679 (95% CI, 0.578–0.771), respectively. With 108.9 pg/ml as the cut-off point for serum sTREM-1, sensitivity was 0.83 and specificity was 0.81. There was no statistically significant difference in serum sTREM-1 or PCT levels between the blood culture-positive and -negative bacteremia groups with ICU-acquired new fever. However, the nonsurvivors in the blood culture-positive bacteremia group had higher levels of serum sTREM-1 and PCT (P <0.05), with a prognostic AUC for serum sTREM-1 of 0.868 (95% CI, 0.740–0.997).

Conclusions

Serum sTREM-1, PCT, and CRP levels each have a role in the early diagnosis of sepsis. Serum sTREM-1, with the highest sensitivity and specificity of all indicators studied, is especially notable. sTREM-1, PCT, and CRP levels are of no use in determining new fever caused by bacteremia in ICU patients, but sTREM-1 levels reflect the prognosis of bacteremia.

Trial registration

ClinicalTrial.gov identifier NCT01410578

Background and Aims

The family of MADS box genes is involved in a number of processes besides controlling floral development. In addition to supplying homeotic functions defined by the ABC model, they influence flowering time and transformation of vegetative meristem into inflorescence meristem, and have functions in roots and leaves. Three Gerbera hybrida At-SOC1-like genes (Gh-SOC1–Gh-SOC3) were identified among gerbera expressed sequence tags.

Methods

Evolutionary relationships between SOC1-like genes from gerbera and other plants were studied by phylogenetic analysis. The function of the gerbera gene Gh-SOC1 in gerbera floral development was studied using expression analysis, protein–protein interaction assays and reverse genetics. Transgenic gerbera lines over-expressing or downregulated for Gh-SOC1 were obtained using Agrobacterium transformation and investigated for their floral phenotype.

Key Results

Phylogenetic analysis revealed that the closest paralogues of At-SOC1 are Gh-SOC2 and Gh-SOC3. Gh-SOC1 is a more distantly related paralogue, grouping together with a number of other At-SOC1 paralogues from arabidopsis and other plant species. Gh-SOC1 is inflorescence abundant and no expression was seen in vegetative parts of the plant. Ectopic expression of Gh-SOC1 did not promote flowering, but disturbed the development of floral organs. The epidermal cells of ray flower petals appeared shorter and their shape was altered. The colour of ray flower petals differed from that of the wild-type petals by being darker red on the adaxial side and greenish on the abaxial surface. Several protein–protein interactions with other gerbera MADS domain proteins were identified.

Conclusions

The At-SOC1 paralogue in gerbera shows a floral abundant expression pattern. A late petal expression might indicate a role in the final stages of flower development. Over-expression of Gh-SOC1 led to partial loss of floral identity, but did not affect flowering time. Lines where Gh-SOC1 was downregulated did not show a phenotype. Several gerbera MADS domain proteins interacted with Gh-SOC1.

The asymmetric unit of the title compound, [ZnCl2(C14H14N4)]n, contains a ZnII ion situated on a twofold rotation axis and one-half of a 1-{4-[(1H-imidazol-1-yl)meth­yl]benz­yl}-1H-imidazole (L) ligand with the benzene ring situated on an inversion center. The ZnII ion is coordinated by two chloride anions and two N atoms from two L ligands in a distorted tetra­hedral geometry. The L ligands bridge ZnCl2 fragments into polymeric chains parallel to [20-1].

AIM

To describe the characteristics of modulation transfer function (MTF) of anterior corneal surface, and obtain the the normal reference range of MTF at different spatial frequencies and optical zones of the anterior corneal surface in myopes.

METHODS

Four hundred eyes from 200 patients were examined under SIRIUS corneal topography system. Phoenis analysis software was applied to simulate the MTF curves of anterior corneal surface at vertical and horizontal meridians at the 3, 4, 5, 6, 7mm optical zones of cornea. The MTF values at spatial frequencies of 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55 and 60 cycles/degree (c/d) were selected.

RESULTS

The MTF curve of anterior corneal surface decreased rapidly from low to intermediate frequency (0-15cpd) at various optical zones of cornea, the value decreased to 0 slowly at higher frequency (>15cpd). With the increase of the optical zones of cornea, MTF curve decreased gradually. 3) In the range of 3 mm- 6 mm optical zones of the cornea, the MTF values measured at horizontal meridian were greater than the corresponding values at horizontal meridian of each spatial frequency, the difference was statistically significant (P<0.05). At 7 mm optical zones of cornea, the MTF values measured at horizontal meridian were less than the corresponding values at vertical meridian at 10-60 spatial frequencies(cpd), and the difference was statistically significant in 25, 30, 35, 40, 45, 50 cpd (P<0.05).

CONCLUSION

MTF can be used to describe the imaging quality of optical systems at anterior corneal surface objectively in detail.

In the title compound, [ZnCl2(C20H18N4)]n, the ZnII ion lies on a twofold rotation axis and is four-coordinated in a tetra­hedral geometry defined by two Cl anions and two N atoms from two 4,4′-bis­[(imidazol-1-yl)meth­yl]biphenyl ligands. The mid-point of the ligand is located on an inversion center, and shows a trans conformation. The ligands link the ZnII ions, forming a chain structure along [10-1].

In the title hetero-dinuclear complex, [CuSm(C22H24N2O4)Cl3(CH3OH)2], the CuII cation is N,N′,O,O′-chelated by a 6,6′-dimeth­oxy-2,2′-[cyclo­hexane-1,2-diylbis(nitrilo­methanylyl­idene)]diphenolate ligand, and one Cl− anion further coordinates to the CuII cation to complete the distorted square-pyramidal coordination geometry, while the SmIII cation is chelated by four O atoms from the same ligand, and is further coordinated by two methanol mol­ecules and two Cl− anions in an bicapped trigonal–prismatic geometry. Intra- and inter­molecular O—H⋯Cl hydrogen bonds are present in the structure.

In the anion of the title salt, C6H16N+·C18H13O8 −, one of the carboxyl groups is deprotonated. Its O atoms are involved in inter­molecular hydrogen bonding with the carboxyl group of an adjacent anion and the amino group of an adjacent cation. The two benzoyloxy rings are oriented with respect to each other at a dihedral angle of 79.46 (6)°.

The title complex, [Er(C32H16N8)(C5H7O2)(C12H8N2)], possesses a mirror plane and the asymmetric unit is half of the mol­ecule. The ErIII cation, lying on the mirror plane, is eight-coordinated by two O atoms from acetyl­acetone, two N (Nphen) atoms from 1,10-phenanthroline and four isoindole N (Niso) atoms from the phthalocyanine ligand in an anti­prismatic geometry. The Er—N distances are in the range 2.376 (5)–2.529 (4) Å and the Er—O distance is 2.272 (3) Å. Notably, the Er—Niso bonds are shorter than the Er—Nphen bonds, but longer than the Er—O bonds.

In the centrosymmetric tetra­nuclear title complex, [Ni4(C12H15NO3)2(CH3COO)2(N3)2(CH3OH)2]·2CH3OH, the asymmetric unit comprises half of a complex mol­ecule and a methanol solvent mol­ecule. The NiII ions display two different coordination environments: (i) two O atoms from the Schiff base ligand, two O atoms from symmetry-related methanol mol­ecules and an O atom from an acetate group, one N atom from the azide group, and (ii) two O atoms and one N atom from the Schiff base, one O atom from methanol, one O atom from the acetate anion, and one N atom from the azide group. Four coplanar NiII ions are connected by two μ2-bridging O atoms from the two deprotonated Schiff bases, two μ3-O atoms from methanol mol­ecules, two μ1,1-N atoms from two azide ions, and four O atoms from acetate groups. The shortest Ni⋯Ni distance in the tetra­nuclear unit is 2.962 (2) Å. O—H⋯O hydrogen bonds between the methanol solvent mol­ecule and an acetate O atom feature in the crystal packing.

In the title complex, [Co(C22H18N2O4)(CN)(H2O)]·0.5CH3CN, the CoIII cation is N,N′,O,O′-chelated by a 6,6′-dimeth­oxy-2,2′-[1,2-phenyl­enebis(nitrilo­methanylyl­idene)]diphenolate dianion, and is further coordinated by a cyanide anion and a water mol­ecule in the axial sites, completing a distorted octa­hedral coordination geometry. In the crystal, pairs of bifurcated O—H⋯(O,O) hydrogen bonds link adjacent mol­ecules, forming centrosymmetric dimers. The acetonitrile solvent mol­ecule shows 0.5 occupancy.

In the title compound, [KYb(C2O4)2(H2O)4]n, the YbIII ion lies on a site of symmetry in a dodeca­hedral environment defined by eight O atoms from four oxalate ligands. The K atom lies on a different axis and is coordinated by four O atoms from four oxalate ligands and four water O atoms. The oxalate ligand has an inversion center at the mid-point of the C—C bond. The metal ions are linked by the oxalate ligands into a three-dimensional framework. O—H⋯O hydrogen bonding is present in the crystal structure.

Introduction

We explored the diagnostic value of a urine soluble triggering receptor expressed on myeloid cells-1 (sTREM-1) for early sepsis identification, severity and prognosis assessment, and for secondary acute kidney injury (AKI). We compared this with white blood cell (WBC) counts, serum C-reactive protein (CRP), serum procalcitonin (PCT), urine output, creatinine clearance (CCr), serum creatinine (SCr), and blood urea nitrogen (BUN).

Methods

We enrolled 104 subjects admitted to the ICU: 16 cases with systemic inflammatory response syndrome (SIRS); 35 with sepsis and 53 with severe sepsis. Results for urine sTREM-1, WBC, serum CRP and serum PCT were recorded on days 1, 3, 5, 7, 10, and 14. For 17 sepsis cases diagnosed with secondary AKI, comparisons between their urine sTREM-1, urine output, CCr, SCr and BUN at diagnosis and 48 h before diagnosis were made.

Results

On the day of admission to the ICU, and compared with the SIRS group, the sepsis group exhibited higher levels of urine sTREM-1 and Acute Physiologic Assessment and Chronic Health Evaluation II (APACHE II) scores (P < 0.05). Areas under the curve (AUC) shaped by the scores were 0.797 (95% CI 0.711 to 0.884) and 0.722 (95% CI 0.586 to 0.858), respectively. On days 1, 3, 5, 7, 10, and 14, urine sTREM-1, serum PCT and WBC levels registered higher in the severe sepsis group in contrast to the sepsis group (P < 0.05). Urine sTREM-1 and serum PCT levels continuously increased among non-survivors, while WBC and serum CRP levels in both groups declined. For 17 patients with AKI, urine sTREM-1, SCr and BUN levels at 48 h before AKI diagnosis were higher, and CCr level was lower than those for non-AKI subjects (P < 0.05). AUC for urine sTREM-1 was 0.922 (95% CI 0.850 to 0.995), the sensitivity was 0.941, and the specificity was 0.76 (based on a cut-off point of 69.04 pg/ml). Logistic regression analysis showed that urine sTREM-1 and severity were risk factors related to AKI occurrence.

Conclusions

Besides being non-invasive, urine sTREM-1 testing is more sensitive than testing WBC, serum CRP, and serum PCT for the early diagnosis of sepsis, as well as for dynamic assessments of severity and prognosis. It can also provide an early warning of possible secondary AKI in sepsis patients.

Trial Registration

ClinicalTrial.gov identifier NCT01333657

In the title compound, [KLu(C2O4)2(H2O)4]n, the LuIII ion lies on a site of symmetry in a dodeca­hedron defined by eight O atoms from four oxalate ligands. The K atom lies on another site of the same symmetry and is coordinated by four oxalate O atoms and four O water atoms. The mid-point of the C—C bond of the oxalate group lies on an inversion center. In the packing structure, each oxalate ligand links two Lu(III) and two K atoms, forming a three-dimensional open framework with channels running along [001]. Inter­molecular O—H⋯O hydrogen bonds occur.

In the heterodinuclear title complex, [GdZn(C22H18N2O4)(CH3COO)3], the ZnII ion is five-coordinated in a square-pyramidal environment defined by two O atoms and two N atoms from the ligand, forming the square plane, and one acetate O atom serving as the apex, while the GdIII ion is nine-coordinated in an approximate mono-capped tetra­gonal–anti­prismatic environment defined by four O atoms from the ligand and five acetate O atoms.

In the title complex, [Co(C22H18N2O4)(CN)(H2O)]·CH3CN, the CoIII ion is six-coordinated in a distorted octa­hedral environment defined by two N atoms and two O atoms from a salen ligand in the equatorial plane and one O atom from a water mol­ecule and one C atom from a cyanide group at the axial positions. O—H⋯O hydrogen bonds connect adjacent complex mol­ecules into dimers. C—H⋯N hydrogen bonds and π–π inter­actions between the benzene rings [centroid–centroid distances = 3.700 (2) and 3.845 (2) Å] are also present.

In the title heterodinuclear salen-type complex, [CuDy(C19H20N2O4)(NO3)3]·CH3OH, the copper(II) ion is tetra­coordinated by two imino N atoms [Cu—N = 1.961 (4) and 1.968 (4) Å] and two phenolate O atoms [Cu—O = 1.931 (3) and 1.938 (3) Å] in a planar geometry. The ten-coordin­ate DyIII ion is ligated by six O atoms of three nitrate groups and four O atoms from the ligand [Dy—O = 2.368 (3)–2.601 (3) Å]. In the crystal, complex mol­ecules and solvent mol­ecules are linked by inter­molecular O—H⋯O hydrogen bonds.

Human primary fibroblasts are a popular type of somatic cells for the production of induced pluripotent stem (iPS) cells. Here we characterized biological properties of primary fibroblasts in terms of cell-growth rate, cytogenetic stability, and the number of inactive X chromosomes during long-term passaging. We produced eight lines of female human dermal fibroblasts (HDFs) and found normal karyotype and expected pattern of X chromosome inactivation (XCI) at low passages (Passage P1-5). However, four out of the eight HDF lines at high passage numbers (≥ P10) exhibited duplicated hallmarks of inactive X chromosome including two punctuate signals of histone H3 lysine 27 trimethylation (H3K27me3) and X inactive-specific transcript (XIST) RNA signals in approximately 8.5–18.5% of the cells. Our data suggest that the copy number of inactive X chromosomes in a subset of female HDF is increased by a two-fold. Consistently, DNA fluorescent in situ hybridization (FISH) identified 3-4 copies of X chromosomes in one nucleus in this subset of cells with two inactive Xs. We conclude that female HDF cultures exhibit a higher risk of genetic anomalies such as carrying an increased number of X chromosomes including both active and inactive X chromosomes at a high passage (≥ P10).

In the title dinuclear CuII–LuIII salen-type complex, [CuLu(C22H24N2O4)(NO3)3], with the ligand 6,6′-dimeth­oxy-2,2′-[cyclo­hexane-1,2-diylbis(nitrilo­methyl­idyne)]diphenolate, the irregular nine-coordinate LuIII coordination sphere comprises four O atoms from the ligand and five O atoms from three nitrate groups, two bidentate and one monodentate [Lu—O = 2.230 (3)–2.621 (4) Å]. The slightly distorted square-planar four-coordinate CuII atom comprises two imine N atoms [Cu—N = 1.903 (4) and 1.912 (4) Å] and two phenolate O atoms from the ligand mol­ecule [Cu—O = 1.897 (3) and 1.906 (3) Å]. All atoms of the cyclo­hexane ring of the ligand mol­ecule are disordered over two sets of sites with equal occupancy.

In the title mononuclear salen-type complex, [Eu(NO3)3(C22H26N2O4)]·CH3OH, the EuIII ion is ten-coordinated by three bidentate nitrate counter-ions and one organic salen-type ligand, which acts in a bis-bidentate chelating mode through its phenolate and meth­oxy O atoms. The protonated imine groups are involved in intra­molecular N—H⋯O hydrogen bonds to the phenolate O atomss, emphasizing the zwitterionic nature of the ligand. An O—H⋯O hydrogen bond links the complex and solvent mol­ecules.

In the title dinuclear salen-type complex, [CuEu(C22H24N2O4)(NO3)3(CH3OH)], the CuII ion is five-coordinated to two imine N atoms and two phenolate O atoms and one O from the bridging nitrate group. The EuIII ion is ligated to three nitrate groups, four O atoms from the salen-type ligand and one methanol mol­ecule, leading to a distorted tenfold coordination for the rare earth cation. One of the three nitrate anions is disordered over two positions in a 0.66 (5):0.34 (5) ratio.