A service model for delivering care closer to home.

Upton Surgery (Worcestershire) has developed a flexible and responsive service model that facilitates multi-agency support for adult patients with complex care needs experiencing an acute health crisis. The purpose of this service is to provide appropriate interventions that avoid unnecessary hospital admissions or, alternatively, provide support to facilitate early discharge from secondary care. Key aspects of this service are the collaborative and proactive identification of patients at risk, rapid creation and deployment of a reactive multi-agency team and follow-up of patients with an appropriate long-term care plan.

Functional and immunocytochemical characterization of the creatine transporter in rat hippocampal neurons.

Creatine uptake by neurons requires a specific creatine transporter (CRT). The purpose of the present work was to investigate the activity and localization of the CRT in primary cultures of hippocampal neurons obtained from 18-day rat embryos. Creatine uptake increased as the neurons differentiated in culture.

Interactions of nitrosylhemoglobin and carboxyhemoglobin with erythrocyte.

Nitrosylhemoglobin (HbFe(II)NO) has been detected in vivo, and its role in NO transport and preservation has been discussed. To gain insight into the potential role of HbFe(II)NO, we performed in vitro experiments to determine the effect of oxygenated red blood cells (RBCs) on the dissociation of cell-free HbFe(II)NO, using carboxyhemoglobin (HbFe(II)CO) as a comparison. Results show that the apparent half-life of the cell-free HbFe(II)CO was reduced significantly in the presence of RBCs at 1% hematocrit.

Selective amino acid substitutions convert the creatine transporter to a gamma-aminobutyric acid transporter.

The creatine transporter (CRT) is a member of a large family of sodium-dependent neurotransmitter and amino acid transporters. The CRT is closely related to the gamma-aminobutyric acid (GABA) transporter, GAT-1, yet GABA is not an effective substrate for the CRT. The high resolution structure of a prokaryotic homologue, LeuT has revealed precise details of the substrate binding site for leucine (Yamashita, A.

Substituted cysteine accessibility of the third transmembrane domain of the creatine transporter: defining a transport pathway.

Twenty-two amino acid residues from transmembrane domain 3 of the creatine transporter were replaced, one at a time, with cysteine. The background for mutagenesis was a C144S mutant retaining approximately 75% of wild-type transport activity but resistant to methanethiosulfonate (MTS) reagents. Each substitution mutant was tested for creatine transport activity and sensitivity to the following MTS reagents: 2-aminoethyl methanethiosulfonate (MTSEA), 2-(trimethylammonium) ethyl methanethiosulfonate (MTSET), and 2-sulfonatoethyl methanethiosulfonate (MTSES).

Purification and characterization of the creatine transporter expressed at high levels in HEK293 cells.

The bovine creatine transporter (CreaT) has been purified from membranes of HEK293 cells stably expressing high levels of the transporter. Membranes were solubilized with decyl maltoside and the CreaT was purified (90% pure) by affinity chromatography on wheat germ agglutinin (WGA)-Sepharose and gel-filtration. The CreaT was shown to be an approximately 70 kDa glycoprotein by SDS-polyacrylamide gel electrophoresis and Western blotting.