Research and analysis of 74 bloodstream infection cases of Acinetobacter baumannii and drug resistance.

OBJECTIVE: We aimed at investigating the clinical and bacteriological features and drug resistance of bloodstream infection of Acinetobacter baumannii, so as to provide new evidence for treatment of bloodstream infection of Acinetobacter baumannii. PATIENTS AND METHODS: Statistical analysis was carried out for the clinical and bacteriological features and drug sensitivity of 74 bloodstream infection cases of Acinetobacter baumannii who were admitted to this hospital between July 2016 and June 2017. RESULTS: Among 74 patients, about 72.0% of them were admitted to the ICU and Respiratory Department; the average age of these patients was 63 years old. Among 74 patients, 62 patients stayed in the hospital for over 2 weeks (83.8%), and 35 for over 1 month (47.3%); 72.0% of patients experienced intrusive operation, in which 28.0% of patients dead. The experiment of drug sensitivity showed that tigecycline had the highest sensitivity (100%), sequentially followed by amikacin (over 90.0%) and other anti-bacterial drugs (less than 40.0%). Pan-drug resistance was identified in 42 patients, accounting for 56.8%. Comparison between the pan-drug resistant and non-pan-drug resistant patients showed that in the first two weeks before the positive blood culture, there were statistically significant differences in administration of carbapenem antibiotics and intrusive operation (p<0.05). Among the patients, the lowest resistance to carbapenem antibiotics was 8.16%, while the rate of resistance to other 12 antibiotics was more than 40.00%. Multiple-resistant strain mainly originated from the ICU and the burn center. CONCLUSIONS: In patients with bloodstream infection of Acinetobacter baumannii, the pan-drug resistant strains account for a vast majority with a high mortality rate. Age, intrusive operation and length of stay in hospital longer than 2 weeks are the common susceptible factors, while the administration of carbapenem antibiotics and intrusive operations might be the high-risk factors leading to pan-drug resistant cases.

Structural and magnetic properties of ZnO nanocrystals in (Zn, Al)O films using pulse laser deposition.

In this manuscript, we reported that the room temperature ferromagnetism was observed in (Zn0.70, Al0.30)O film, which was fabricated by a novel physical method (pulse laser deposition (PLD)). The film was deposited from (Zn0.80, Al0.20)O ceramic target onto quartz (110) substrate by PLD at 400 degrees C under an oxygen partial pressure of 10(-4) torr. TEM result shows ZnO NCs with diameter of 4-5 nm and they are quite uniformly embedded into amorphous ZnO-Al2O3 phase. The SAED shows clearly that ZnO NCs possess polycrystalline structure. The SQUID measurement shows that the film has room temperature ferromagnetism (saturation magnetization = 3.6 emu/cm3) with Curie temperature above 300 K. The magnitude of magnetic moment of the films can be changed by tuning ZnO NCs size. Both oxygen partial pressure and film thickness studies show that the origin of ferromagnetism is possibly related to the oxygen defects at the surface of ZnO NCs.

Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14.

Urotensin-II (U-II) is a vasoactive 'somatostatin-like' cyclic peptide which was originally isolated from fish spinal cords, and which has recently been cloned from man. Here we describe the identification of an orphan human G-protein-coupled receptor homologous to rat GPR14 and expressed predominantly in cardiovascular tissue, which functions as a U-II receptor. Goby and human U-II bind to recombinant human GPR14 with high affinity, and the binding is functionally coupled to calcium mobilization. Human U-II is found within both vascular and cardiac tissue (including coronary atheroma) and effectively constricts isolated arteries from non-human primates. The potency of vasoconstriction of U-II is an order of magnitude greater than that of endothelin-1, making human U-II the most potent mammalian vasoconstrictor identified so far. In vivo, human U-II markedly increases total peripheral resistance in anaesthetized non-human primates, a response associated with profound cardiac contractile dysfunction. Furthermore, as U-II immunoreactivity is also found within central nervous system and endocrine tissues, it may have additional activities.

Melanin-concentrating hormone is the cognate ligand for the orphan G-protein-coupled receptor SLC-1.

The underlying causes of obesity are poorly understood but probably involve complex interactions between many neurotransmitter and neuropeptide systems involved in the regulation of food intake and energy balance. Three pieces of evidence indicate that the neuropeptide melanin-concentrating hormone (MCH) is an important component of this system. First, MCH stimulates feeding when injected directly into rat brains; second, the messenger RNA for the MCH precursor is upregulated in the hypothalamus of genetically obese mice and in fasted animals; and third, mice lacking MCH eat less and are lean. MCH antagonists might, therefore, provide a treatment for obesity. However, the development of such molecules has been hampered because the identity of the MCH receptor has been unknown until now. Here we show that the 353-amino-acid human orphan G-protein-coupled receptor SLC-1 expressed in HEK293 cells binds MCH with sub-nanomolar affinity, and is stimulated by MCH to mobilize intracellular Ca2+ and reduce forskolin-elevated cyclic AMP levels. We also show that SLC-1 messenger RNA and protein is expressed in the ventromedial and dorsomedial nuclei of the hypothalamus, consistent with a role for SLC-1 in mediating the effects of MCH on feeding.

Orexins and orexin receptors: a family of hypothalamic neuropeptides and G protein-coupled receptors that regulate feeding behavior.

The hypothalamus plays a central role in the integrated control of feeding and energy homeostasis. We have identified two novel neuropeptides, both derived from the same precursor by proteolytic processing, that bind and activate two closely related (previously) orphan G protein-coupled receptors. These peptides, termed orexin-A and -B, have no significant structural similarities to known families of regulatory peptides. prepro-orexin mRNA and immunoreactive orexin-A are localized in neurons within and around the lateral and posterior hypothalamus in the adult rat brain. When administered centrally to rats, these peptides stimulate food consumption. prepro-orexin mRNA level is up-regulated upon fasting, suggesting a physiological role for the peptides as mediators in the central feedback mechanism that regulates feeding behavior.