[Operational management in our hospice ward-from the viewpoint of supporting a patient's recuperation at home].

Although many terminally ill cancer patients desire to receive medical treatment in palliative care units(PCUs or hospices), very few patients are actually able to receive such treatment. Our aim is to provide palliative care to as many people as possible. We have practiced palliative care in general wards and prioritized care according to the patient's prognosis on admission to our hospice. From April 2007 to March 2011, 87% patients were admitted to our hospital in accordance with their wishes. By adequate management of hospital wards, including PCUs, and unitizing the health resources of the area, terminally ill cancer patients may be able to spend more time at home prior to hospitalization.

[The role of percutaneous endoscopic gastrostomy(PEG)in palliative care].

The role of percutaneous endoscopic gastrostomy(PEG)in palliative care has not been well discussed. With the evolution of endoscopic techniques and PEG devices, we can perform PEG more safely, even in difficult cases. Actually, PEG is very useful in home care of cancer patients. We should discuss the indications of PEG in the field of palliative medicine. We suggest the following indications for PEG: 1.Difficulty in ingestion of sufficient quantities of food and water because of pain on swallowing, or an obstruction caused by cancer. 2.Normal gastrointestinal function. 3.Expected survival time of more than four weeks in addition to absence of cachexia. 4.Patient's consent for PEG.

Construction and structural analysis of tethered lipid bilayer containing photosynthetic antenna proteins for functional analysis.

The construction and structural analysis of a tethered planar lipid bilayer containing bacterial photosynthetic membrane proteins, light-harvesting complex 2 (LH2), and light-harvesting core complex (LH1-RC) is described and establishes this system as an experimental platform for their functional analysis. The planar lipid bilayer containing LH2 and/or LH1-RC complexes was successfully formed on an avidin-immobilized coverglass via an avidin-biotin linkage. Atomic force microscopy (AFM) showed that a smooth continuous membrane was formed there. Lateral diffusion of these membrane proteins, observed by a fluorescence recovery after photobleaching (FRAP), is discussed in terms of the membrane architecture. Energy transfer from LH2 to LH1-RC within the tethered membrane was observed by steady-state fluorescence spectroscopy, indicating that the tethered membrane can mimic the natural situation.

Lateral organization of a membrane protein in a supported binary lipid domain: direct observation of the organization of bacterial light-harvesting complex 2 by total internal reflection fluorescence microscopy.

A unique method is described for directly observing the lateral organization of a membrane protein (bacterial light-harvesting complex LH2) in a supported lipid bilayer using total internal reflection fluorescence (TIRF) microscopy. The supported lipid bilayer consisted of anionic 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1'-glycerol)] (DOPG) and 1,2-distearoly-sn-3-[phospho-rac-(1'-glycerol)] (DSPG) and was formed through the rupture of a giant vesicle on a positively charged coverslip. TIRF microscopy revealed that the bilayer was composed of phase-separated domains. When a suspension of cationic phospholipid (1,2-dioleoyl-sn-glycero-3-ethylphosphocholine: EDOPC) vesicles (approximately 400 nm in diameter), containing LH2 complexes (EDOPC/LH2 = 1000/1), was put into contact with the supported lipid bilayer, the cationic vesicles immediately began to fuse and did so specifically with the fluid phase (DOPG-rich domain) of the supported bilayer. Fluorescence from the incorporated LH2 complexes gradually (over approximately 20 min) spread from the domain boundary into the gel domain (DSPG-rich domain). Similar diffusion into the domain-structured supported lipid membrane was observed when the fluorescent lipid (1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-lissamine-rhodamine B sulfonyl: N-Rh-DOPE) was incorporated into the vesicles instead of LH2. These results indicate that vesicles containing LH2 and lipids preferentially fuse with the fluid domain, after which they laterally diffuse into the gel domain. This report describes for first time the lateral organization of a membrane protein, LH2, via vesicle fusion and subsequent lateral diffusion of the LH2 from the fluid to the gel domains in the supported lipid bilayer. The biological implications and applications of the present study are briefly discussed.