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2. Upgrade of the Fast Beam Intensity Measurement System for the CERN PS Complex

Author

Allica, JC, Andersen, M, Andreazza, W, Belohrad, D, Favre, G, Favre, N, Jensen, L, Lenardon, F, and Vollenberg, W

Subjects
Physics::Instrumentation and Detectors, Physics::Accelerator Physics, Accelerators and Storage Rings
Abstract

The CERN Proton Synchrotron complex (CPS) has been operational for over 50 years. During this time the Fast Beam Current Transformers (FBCTs) have only been repaired when they ceased to function, or individually modified to cope with new requests. This strategy resulted in a large variation of designs, making their maintenance difficult and limiting the precision with which comparisons could be made between transformers for the measurement of beam intensity transmission. During the first long shutdown of the CERN LHC and its injectors (LS1) these systems have undergone a major consolidation, with detectors and acquisition electronics upgraded to provide a uniform measurement system throughout the PS complex. This paper discusses the solutions used and analyses the first beam measurement results.

Published
2014

4. Immunization of mice with phosphatidylcholine drastically reduces the parasitaemia of subsequent Plasmodium chabaudi chabaudi blood-stage infections

Author

Bordmann, G, Rudin, W, and Favre, N

Subjects
Mice, Inbred ICR, animal diseases, Phosphatidylethanolamines, Immunization, Passive, Antibodies, Protozoan, chemical and pharmacologic phenomena, biochemical phenomena, metabolism, and nutrition, Th1 Cells, Parasitemia, Tuberculin, Malaria, Mice, Th2 Cells, Immunoglobulin M, Plasmodium chabaudi, Immunoglobulin G, parasitic diseases, Phosphatidylcholines, bacteria, Animals, Cytokines, Female, Immunization, Research Article
Abstract

It has been suggested that phospholipids and antibodies directed against phospholipids are important in the pathology of malaria. We have investigated the influence of immunizations with phospholipids on the course of subsequent blood-stage Plasmodium chabaudi chabaudi infections in ICR inbred mice. We observed a significant reduction in the parasitaemia following immunization with phosphatidylcholine (PC), but not with phosphatidylethanolamine (PE) immunization. At the peak of the infection, PC-immunized mice displayed a T-helper 2 (Th2)-type cytokine production pattern, whereas PE-immunized or non-treated controls displayed a cytokine production pattern of the T-helper 1 (Th1) type. Serum immunoglobulin transfer from PC-immunized mice protected naive mice in a similar fashion to PC-immunization, demonstrating that the observed reduction of parasitaemia was caused by the presence of PC-specific antibodies.

Published
1998

7. Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones.

Author

Garrido C, Fromentin A, Bonnotte B, Favre N, Moutet M, Arrigo AP, Mehlen P, and Solary E

Subjects
Adenocarcinoma immunology, Animals, Apoptosis physiology, Cell Death physiology, Clone Cells, Colonic Neoplasms immunology, Heat-Shock Proteins physiology, Mice, Mice, Nude, Rats, Rats, Inbred Strains, Tumor Cells, Cultured, Adenocarcinoma metabolism, Adenocarcinoma pathology, Colonic Neoplasms metabolism, Colonic Neoplasms pathology, Heat-Shock Proteins biosynthesis
Abstract

The REG and PRO cell clones were obtained from a colon adenocarcinoma induced in a BDIX rat by 1,2-dimethylhydrazine. When injected s.c. into syngeneic hosts, REG cells induce tumors that regress in less than 3 weeks, whereas PRO cells, like parental cells, induce progressive tumors. Here, we show that compared to PRO cells, REG cells are more sensitive to cell death induced by anticancer drugs. The small heat shock protein (HSP) 27 is not expressed or inducible in REG clones, whereas it is abundantly expressed and inducible by heat shock in PRO clones. The expression of HSP27 in REG cells increases their resistance to apoptosis in vitro and dramatically enhances their tumorigenicity when injected s.c. into syngeneic rats. HSP27 expression in REG cells both increases tumor size and delays tumor regression. This increased tumorigenicity is associated with a substantial decrease of in vivo tumor cell apoptosis. We conclude that HSP27 expression in malignant cells increases their tumorigenicity in syngeneic animals. In combination with the role of HSP27 in tumor cell resistance to cytotoxic agents, its contribution to tumorigenicity makes this protein a potential target for antitumoral therapy.

Published
1998

8. Cancer cell sensitization to fas-mediated apoptosis by sodium butyrate.

Author

Bonnotte B, Favre N, Reveneau S, Micheau O, Droin N, Garrido C, Fontana A, Chauffert B, Solary E, and Martin F

Subjects
Animals, Carrier Proteins metabolism, Colonic Neoplasms metabolism, Fas Ligand Protein, Fas-Associated Death Domain Protein, Flow Cytometry, Humans, In Situ Nick-End Labeling, Interferon-gamma pharmacology, Microscopy, Phase-Contrast, Proto-Oncogene Proteins metabolism, Proto-Oncogene Proteins c-bcl-2 metabolism, Rats, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha pharmacology, bcl-2-Associated X Protein, bcl-X Protein, Adaptor Proteins, Signal Transducing, Apoptosis drug effects, Butyric Acid pharmacology, Membrane Glycoproteins genetics
Abstract

Cancer cells often resist Fas-mediated apoptosis even when the Fas receptor is expressed at the cell surface. We show here that human and rat colon cancer cells undergo massive apoptosis when they are exposed to soluble Fas ligand in the presence of sodium butyrate, an agent that induces by itself only a low rate of apoptosis. Sodium butyrate potentiates Fas-dependent apoptosis in seven out of eight colon cancer cell lines. Sodium butyrate does not increase Fas receptor cell surface expression and does not modify cell levels of Bcl-2, Bcl-xL, Bcl-xS and Bax. Sodium butyrate also induces tumor cell sensitization to the apoptotic effect of the combination of TNF-alpha and IFN-gamma, but it does not modify the level of the FADD/Mort1 adaptator molecule, at the connection between Fas- and TNF-dependent apoptosis pathways. Because the clinical toxicity of butyrate is low, its ability to enhance Fas-signal delivery in cancer cells could be of therapeutic interest.

Published
1998
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