Background: The presence of high-density starry dots around the intracerebral hemorrhage (ICH), which we termed as a satellite sign, is occasionally observed in CT. The relationship between ICH with a satellite sign and its functional outcome has not been identified. This study aimed to determine whether the presence of a satellite sign could be an independent prognostic factor for patients with ICH. Methods: Patients with acute spontaneous ICH were retrospectively identified and their initial CT scans were reviewed. A satellite sign was defined as scattered high-density lesions completely separate from the main hemorrhage in at least the single axial slice. Functional outcome was evaluated using the modified Rankin Scale (mRS) at discharge. Poor functional outcome was defined as mRS scores of 3-6. Univariate and multivariate logistic regression analyses were applied to assess the presence of a satellite sign and its association with poor functional outcome. Results: A total of 241 patients with ICH were enrolled in the study. Of these, 98 (40.7%) had a satellite sign. Patients with a satellite sign had a significantly higher rate of poor functional outcome (95.9%) than those without a satellite sign (55.9%, p < 0.0001). Multivariate logistic regression analysis revealed that higher age (OR 1.06; 95% CI 1.03-1.10; p = 0.00016), large hemorrhage size (OR 1.06; 95% CI 1.03-1.11; p = 0.00015), and ICH with a satellite sign (OR 13.5; 95% CI 4.42-53.4; p < 0.0001) were significantly related to poor outcome. A satellite sign was significantly related with higher systolic blood pressure (p = 0.0014), higher diastolic blood pressure (p = 0.0117), shorter activated partial thromboplastin time (p = 0.0427), higher rate of intraventricular bleeding (p < 0.0001), and larger main hemorrhage (p < 0.0001). Conclusions: The presence of a satellite sign in the initial CT scan is associated with a significantly worse functional outcome in ICH patients.

Edited by Miguel De la RosaKeywords: Malaria Apicoplast Heme degradation Ferredoxin Heme oxygenase Double-barreled enzyme a b s t r a c tThe metabolic pathways in apicoplasts of human malaria parasites are promising drug targets. The apicomplexan parasites exhibit delayed cell death when their apicoplast is impaired, but the metabolic pathways within apicoplasts are poorly understood. A nuclear-encoded heme oxygenase (HO)-like protein with an apicoplast-targeted bipartite transit peptide was identified in the Plasmodium falciparum genome. Purified mature recombinant PfHO protein converted heme into bilirubin IXa as confirmed by high-performance liquid chromatography. In addition, PfHO required an iron chelator such as deferoxamine for complete activity. These observations lead to the conclusion that a novel enzymatic heme degradation system is present in human malaria parasites.

(E)-4-Hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE), which catalyzes the conversion of 2-Cmethyl-D-erythritol cyclodiphosphate (MEcPP) into (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP), is an essential enzyme of the non-mevalonate (2-C-methyl-D-erythritol-4-phosphate (MEP)) pathway for isoprenoid biosynthesis. The terminal steps of the MEP pathway are still not fully understood, although this pathway is necessary for survival in various organisms such as cyanobacteria, plastids of algae and higher plants, and the apicoplast of human malaria parasites. To determine the efficient redox partner for thermophilic cyanobacterial GcpE, We have expressed the gcpE and petF genes in Escherichia coli and studied the protein-protein interaction of GcpE protein with ferredoxin I (PetF) from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. Recombinant GcpE protein was purified by an N-terminal His 6 tag and reconstituted as a [4Fe-4S] 2؉ metalloprotein. GcpE was shown to interact strongly with PetF via the bacterial two-hybrid system designed to detect protein-protein interactions. Moreover, a direct protein-protein interaction between PetF and GcpE was confirmed in an in vitro glutathione Stransferase (GST) pull-down assay. To investigate electron transfer activity from PetF to GcpE, we also constructed a NADPH-dependent reducing shuttle system with purified recombinant ferredoxin-NADP ؉ oxidoreductase (PetH) and PetF. The result demonstrated that PetF has the ability to transfer electrons to GcpE. Thus, the combined data provide the first evidence that GcpE is a ferredoxin-dependent enzyme in T. elongatus BP-1.

Edited by Richard Cogdell Keywords:Phycobilin biosynthesis Ferredoxin-dependent enzyme Heme oxygenase Phycocyanobilin:ferredoxin oxidoreductase 1:2 Complex Gel mobility shift assay a b s t r a c tThe HO1 and PcyA genes, encoding heme oxygenase-1 (HO1) and phycocyanobilin (PCB):ferredoxin (Fd) oxidoreductase (PcyA), respectively, are required for chromophore synthesis in photosynthetic light-harvesting complexes, photoreceptors, and circadian clocks. In the PCB biosynthetic pathway, heme first undergoes cleavage to form biliverdin. I confirmed that Fd1 induced the formation of a stable and functional HO1 complex by the gel mobility shift assay. Furthermore, analysis by a chemical cross-linking technique designed to detect protein-protein interactions revealed that HO1 and PcyA directly interact with Fd in a 1:2 ratio. Thus, Fd1, a one-electron carrier protein in photosynthesis, drives the phycobilin biosynthetic pathway.

Intracoronary nicorandil reduced microvascular dysfunction after primary PCI more effectively than did nitroglycerin in patients with STEMI, probably via its KATP channel-opening effect.