This study aimed to determine factors favoring home death for cancer patients in a context of coordinated home care. A retrospective study was conducted among patients followed up by the home care coordinating unit of the cancer center of Lyon. The main endpoint was place of death. Univariate analysis included general characteristics (age, gender, rural or urban residence, disease), Karnofsky Index (KI), type of care at referral (chemotherapy, palliative care, or other supportive care), and coordinating medical oncologist (MCO) home visits. Significant factors were used in a logistic regression analysis. Of 250 patients, 90 (36%) had home death. Low KI and MCO home visit were correlated with home death (odds ratio, respectively, 2.1 and 3.1). These results indicate that health care support favors home death. A hospital-based home care unit is effective for bridging the gap between community and hospital. MCO home visits offer concrete support to health care professionals, patients, and relatives.

The y-D-glutamyl-(L)meso-diaminopimelate endopeptidase, or endopeptidase I, from Bacillus sphaericus 9602 was purified to apparent protein homogeneity. The purification was achieved by a six-step procedure: ammonium sulfate fractionation, phenyl-Sepharose chromatography, two consecutive DEAE-Trisacryl chromatographies, chromatofocusing and Sephacryl S-200 permeation chromatography. The enzyme was purified 5000-fold with a 38% recovery of lytic activity. It is an acidic protein (PI 5.4) of hydrophobic nature. Kinetic studies have shown a K , value of 0.57 mM and an apparent V,,, of 8.3 pmol min-' (mg enzyme)-' with N-acetylmuramyl-~-alanyl-y-~-glutamyl-(~)meso-diaminopimelyl(~)-~-[ ''C]alanine as substrate. The enzyme was inhibited by o-phenanthroline and EDTA and was reactivated by zinc, cobalt and manganese ions; thus endopeptidase I is a metallo enzyme, probably a zinc enzyme. Moreover it is a heat-stable protein with an apparent inactivation temperature of 8 0 T . , in which the meso-diaminopimelic acid residues have free o-NH2 and o-COOH groups [6]: It acts on monomeric substrates (peptides and MurNAc-glycopeptides or GlcNAc-MurNAc-glycopeptides) [6] and also on the non-cross-linked peptide chains of the peptidoglycans [7]. The enzymic activity is closely related to sporulation [8]. Apart from its unique action on y-D-glutamyl linkages, the interest in endopeptidase I is due to two of its uses: these are firstly the location of the amide group on the meso-diaminopimelic acid or on the D-glutamic acid residues in monoamidated tetrapeptides of bacterial cell wall peptidoglycans [9] and secondly the preparation of an immunostimulant, GlcNAc-MurNAc-L-Ala-D-Glu-NH2 [lo]. Two forms of the enzyme have been identified: an extracellular one in the sporulation medium [I 11 and a membrane-bound one in the integuments of the forespores and of the spores 131. Whether the soluble and membrane-bound enzymes are different entities or only one enzyme with different localization has not been demonstrated. To elucidate this, we report in this paper the purification and the partial characterization of the extracellular endopeptidase I in order to allow comparison with the membrane-bound enzyme.Correspondence to M. Guinand, Laboratoire de Biochimie Microbienne, Universite Claude Bernard, Lyon I, 43 Boulevard du Onze Novembre 191 8, F-69622 Villeurbanne Cedex, FranceAbbreviations. ms-A2pm, meso-diaminopimelic acid, Glu-NH2, isoglutamine, MurNAc, N-acetylmuramic acid; GlcNAc, N-acetylglucosamine; SDS, sodium dodecyl sulfate; PAGE, polyacrylamide gel electrophoresis.A part of this study, concerning the electrophoretic behavior of the purified endopeptidase I in denaturing and non-denaturing conditions, has been reported recently [ 121. MATERIALS AND METHODSCrude extracellular endopeptidase I Bacillus sphaericus NCTC 9602 was grown as previously described [13] and the crude extracellular enzyme was obtained as recommended in [14]. Briefly cells of a B. sphaericus culture (67 1) were harvested at the beginning of sporulation (2 -5% ...

We calculated the incidence of nosocomial infection in 2 intensive care units (ICUs) on the basis of prevalence data recorded from 1997 through 2002 and compared these estimates to cumulative incidences measured in the 2 ICUs during the same period to investigate the feasibility and the reliability of converting prevalence data to incidence estimates. Decreases in the calculated and measured incidences over time in the ICUs were found to be statistically significantly related.

High-dose chemotherapy and autologous marrow or peripheral stem cell support offers the best chance of cure in some subgroups of patients with non-Hodgkin's lymphoma (NHL). Less is known about the role of a second course of myeloablative chemotherapy in patients who relapse after a first autologous transplant. The aim of this retrospective study was to evaluate the disease outcome, morbidity and mortality associated with second autologous transplantation in patients with NHL. Between 1985 and 2001, 225 patients who had received autologous transplantation for NHL in two institutions in Lyon relapsed. Of these 225 patients 18 underwent a second autologous transplantation. The median age at second transplant was 41 years. There were six indolent lymphomas and 12 aggressive lymphomas. The median follow-up from the second transplant was 42 months. The OS rate at 2 and 5 years were 58 and 27%, respectively. The PFS rate at 2 and 5 years was 36%. Five patients are alive without disease 20 to 100 months after the second transplant. Seven patients died of disease recurrence. Four (22%) toxic deaths occurred: one of pulmonary fibrosis, one of fungal infection and cardiac failure and two of acute leukaemia. A minority of patients with NHL recurrence after a first transplant can be cured by a second course of myeloablative chemotherapy at the cost however of high-risk toxic death.

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