(η5-Penta­methyl­cyclo­penta­dien­yl)(η6-4-phenyl­butan-2-one)ruthenium(II) tetra­phenyl­borate

The title compound, [Ru(C10H15)(C10H12O)][B(C6H5)4], crystallizes as discrete (η5-penta­methyl­cyclo­penta­dien­yl)Ru(η6-4-phenyl­butan-2-one)]+ cations and [BPh4]− anions. In the cation, the non-H atoms of the butan-2-one group are approximately planar (r.m.s. deviation = 0.056 Å) and lie nearly perpendicular to the plane of the phenyl ring with a dihedral angle between the two planes of 69.3 (1)°. No significant C—H⋯O inter­actions are observed between the methyl and phenyl H atoms and the carbonyl O atom

(η6-Isopropyl N-phenyl­carbamate)(η5-penta­methyl­cyclo­penta­dien­yl)ruthenium(II) tetra­phenyl­borate acetone monosolvate

The title complex, [Ru(C10H15)(C10H13NO2)](C24H20B)·C3H6O, is related to the analogous O-methyl complex. The average Ru—C distance to the penta­methyl­cyclo­penta­dienyl (Cp*) group is 2.19 (3) Å, and 2.21 (1) Å to the ortho, meta and para C atoms of the arene ring. The Ru—Cipso bond length of 2.272 (3) Å is significantly longer, reflecting movement of the Ru atom away from the C atoms with electronegative substituents attached. The amide H atom in the cation forms an inter­molecular N—H⋯O hydrogen bond with the carbonyl O atom of the acetone solvent mol­ecule. A C—H⋯O inter­action also occurs

4-(Benzyl­ideneamino)benzene­sulfonamide

The title compound, C13H12N2O2S, formed by Schiff base condensation of benzaldehyde with sulfanilamide, crystallizes as discrete mol­ecular species linked by N—H⋯N and N—H⋯O hydrogen bonds between the sulfamide nitro­gen H atoms and the aza­methine N and one sulfamide O atom, respectively, forming a two-dimensional array in the bc plane. The aza­methine group is rotated slightly out of the benzaldehyde benzene plane [C—C—C—N torsion angle = 8.1 (3)°], while the dihedral angle between the two benzene rings is 30.0 (1)°

(η6-Benzophenone)(η5-penta­methyl­cyclo­penta­dien­yl)ruthenium(II) tetra­phenyl­borate

The structure of the title compound, [Ru(C10H15)(C13H10O)](C24H20B), consists of discrete [Cp*Ru(II)benzophenone] cations and tetra­phenyl­borate anions (Cp* = penta­methyl­cyclo­penta­dien­yl). Tethering the Cp*Ru group to one aryl ring of benzophenone results in average values of 1.42 (1) and 1.38 (1) Å for the C—C bond lengths in the Ru-tethered and untethered phenyl rings, respectively. The dihedral angle between the benzene and phenyl rings of the benzophenone group is 50.5 (1)°

(η5-Penta­methyl­cyclo­penta­dien­yl)(η6-p-toluene­sulfonamide)ruthenium(II) tetra­phenyl­borate

The crystal structure of the title compound, [Ru(C10H15)(C7H9NO2S)]C24H20B, has been determined as part of our investigation into the structural and biological properties of organometallic RuII–arene–Cp* complex salts of the type [R-PhRuCp*]+·X − (where Cp* is penta­methyl­cyclo­penta­diene). Tethering the RuCp* group to the benzene ring of p-toluene­sulfonamide results in only minor changes to the mol­ecular geometry of the sulfonamide, but, together with crystallization as the [BPh4]− salt, effectively blocks involvement of the sulfonamide group in N—H⋯O hydrogen-bonding networks

T. brucei cathepsin-L increases arrhythmogenic sarcoplasmic reticulum-mediated calcium release in rat cardiomyocytes

Aims: African trypanosomiasis, caused by Trypanosoma brucei species, leads to both neurological and cardiac dysfunction and can be fatal if untreated. While the neurological-related pathogenesis is well studied, the cardiac pathogenesis remains unknown. The current study exposed isolated ventricular cardiomyocytes and adult rat hearts to T. brucei to test whether trypanosomes can alter cardiac function independent of a systemic inflammatory/immune response. Methods and results: Using confocal imaging, T. brucei and T. brucei culture media (supernatant) caused an increased frequency of arrhythmogenic spontaneous diastolic sarcoplasmic reticulum (SR)-mediated Ca2+ release (Ca2+ waves) in isolated adult rat ventricular cardiomyocytes. Studies utilising inhibitors, recombinant protein and RNAi all demonstrated that this altered SR function was due to T. brucei cathepsin-L (TbCatL). Separate experiments revealed that TbCatL induced a 10–15% increase of SERCA activity but reduced SR Ca2+ content, suggesting a concomitant increased SR-mediated Ca2+ leak. This conclusion was supported by data demonstrating that TbCatL increased Ca2+ wave frequency. These effects were abolished by autocamtide-2-related inhibitory peptide, highlighting a role for CaMKII in the TbCatL action on SR function. Isolated Langendorff perfused whole heart experiments confirmed that supernatant caused an increased number of arrhythmic events. Conclusion: These data demonstrate for the first time that African trypanosomes alter cardiac function independent of a systemic immune response, via a mechanism involving extracellular cathepsin-L-mediated changes in SR function

Postfledging Survival, Movements, and Dispersal of Ring Ouzels (Turdus torquatus)

We thank Invercauld Estate for cooperation with access to Glen Clunie. S. Redpath, J. Wilson, and S. Roos provided valuable comments on the manuscript. This study was funded by the Royal Society for the Protection of Birds, Scottish Natural Heritage, and the Cairngorms National Park Authority. J.L.L. was supported by the Natural Environment Research Council.Peer reviewedPublisher PD

Gene therapy with Angiotensin-(1-9) preserves left ventricular systolic function after myocardial infarction

BACKGROUND: Angiotensin-(1-9) [Ang-(1-9)] is a novel peptide of the counter-regulatory axis of the renin angiotensin system previously demonstrated to have therapeutic potential in hypertensive cardiomyopathy when administered via osmotic minipump in mice. Here, we investigate whether gene transfer of Ang-(1-9) is cardioprotective in a murine model of myocardial infarction (MI). OBJECTIVES: To evaluate effects of Ang-(1-9) gene therapy on myocardial structural and functional remodeling post infarction. METHODS: C57BL/6 mice underwent permanent left anterior descending coronary artery ligation and cardiac function was assessed using echocardiography for 8 weeks followed by a terminal measurement of left ventricular (LV) pressure-volume loops. Ang-(1-9) was delivered by adeno-associated viral vector via single tail vein injection immediately following induction of MI. Direct effects of Ang-(1-9) on cardiomyocyte excitation–contraction coupling and cardiac contraction were evaluated in isolated mouse and human cardiomyocytes and in an ex vivo Langendorff perfused whole heart model. RESULTS: Gene delivery of Ang-(1-9) significantly reduced sudden cardiac death post-MI. Pressure–volume measurements revealed complete restoration of end systolic pressure, ejection fraction, end systolic volume and the end diastolic pressure–volume relationship by Ang-(1-9) treatment. Stroke volume and cardiac output were significantly increased versus sham. Histological analysis revealed only mild effects on cardiac hypertrophy and fibrosis, but a significant increase in scar thickness. Direct assessment of Ang-(1-9) on isolated cardiomyocytes demonstrated a positive inotropic effect via increasing calcium transient amplitude and increasing contractility. Ang-(1-9) increased contraction in the Langendorff model through a protein kinase A-dependent mechanism. CONCLUSIONS: Our novel findings show that Ang-(1-9) gene therapy preserves LV systolic function post-MI, restoring cardiac function. Furthermore, Ang-(1-9) has a direct effect on cardiomyocyte 3 calcium handling through a protein kinase A-dependent mechanism. These data highlight Ang-(1-9) gene therapy as a potential new strategy in the context of MI

Bis[cis-bis­(diphenyl­phosphino)ethene-κ 2 P,P′]copper(I) tetra­fluoridoborate ethanol solvate

In the title compound [Cu(C26H22P2)2]BF4·C2H5OH, a disordered ethanol solvate molecule and the anions are located in well defined channels along the c axis. The four-coordinate Cu(P—P)2 core of the cation adopts approximately D 2 point group symmetry with the Cu—P bond lengths spanning a narrow range from 2.272 (1) to 2.285 (1) Å