Regulation of blood and lymphatic vascular separation by signaling proteins SLP-76 and Syk

Lymphatic vessels develop from specialized endothelial cells in preexisting blood vessels, but the molecular signals that regulate this separation are unknown. Here we identify a failure to separate emerging lymphatic vessels from blood vessels in mice lacking the hematopoietic signaling protein SLP-76 or Syk. Blood-lymphatic connections lead to embryonic hemorrhage and arteriovenous shunting. Expression of slp-76 could not be detected in endothelial cells, and blood-filled lymphatics also arose in wild-type mice reconstituted with SLP-76-deficient bone marrow. These studies reveal a hematopoietic signaling pathway required for separation of the two major vascular networks in mammals.     

Single crystal metals encapsulated in carbon nanoparticles

Single-domain microcrystals of LaC(2) encapsulated within nanoscale polyhedral carbon particles have been synthesized in a carbon arc. Typical particle sizes are on the order of 20 to 40 nanometers. The stoichiometry and phase of the La-containing crystals have been assigned from characteristic lattice spacings observed by high-resolution transmission electron microscopy and energy dispersive spectroscopy (EDS). EDS spectra show that La and C are the only elements present. Characteristic interatomic distances of 3.39 and 2.78 angstroms identify the compound inside the nanoparticle cavities as alpha-LaC(2), the phase of LaC(2) that is stable at room temperature. Bulk alpha-LaC(2) is metallic and hydrolytic. Observation of crystals of pure encapsulated alpha-LaC(2) that were exposed to air for several days before analysis indicates that the LaC(2) is protected from degradation bythe carbon polyhedral shells of the nanoparticles. A high percentage of the carbon nanoparticles have encapsulated LaC(2) single crystals. These carbon-coated metal crystals form a new class of materials that can be protected in their pure or carbide forms and may have interesting and useful properties.     

An amylose antiparallel double helix at atomic resolution

In the crystal structure of the polyiodide complex (p-nitrophenyl-alpha-maltohexaose(2)) . Ba(I(3))(2) . 22H(2)O, the maltohexaose units form an antiparallel, left-handed double helix with O-2 ... O-3 and O-6 ... O-6 hydrogen bonding and a central cavity that encloses two triiodide units. This structure contrasts with the parallel, left-handed double helix with no central cavity proposed for the A-and B-starch helix and the left-handed single helix in V-amylose and may be relevant for the stabilization of glycogen Structure.