Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Christiane Levrat"'
Autor:
Galina D. Mironova, Elena Gritsenko, Odile Gateau-Roesch, Christiane Levrat, Alexey Agafonov, Konstantin Belosludtsev, Annie France Prigent, Danina Muntean, Madeleine Dubois, Michel Ovize
Publikováno v:
Journal of Bioenergetics and Biomembranes. 36:171-178
A possible role of palmitic acid/Ca2+ (PA/Ca2+) complexes in the cyclosporin-insensitive permeability transition in mitochondria has been studied. It has been shown that in the presence of Ca2+, PA induces a swelling of mitochondria, which is not inh
Publikováno v:
Cytokine. 13:257-263
From the hypothesis that in TNF-alpha-resistant cells the activity of mitochondrial phospholipase A2 could be reversed by a lysophospholipid acyltransferase, we report that the mitochondrial reacylation of phosphatidylcholine as phosphatidylethanolam
Autor:
Galina D. Mironova, Elena Limarenko, Christiane Levrat, Odile Gateau-Roesch, Catherine Rey, E. N. Gritsenko, Evgeny Pavlov, Pierre Louisot, Nils Erik L. Saris, Alissa V. Lazareva
Publikováno v:
Journal of Bioenergetics and Biomembranes. 33:319-331
A mitochondrial hydrophobic component that forms Ca2+-induced nonspecific ion channels in black-lipid membranes (Mironova et al., 1997) has been purified and its nature elucidated. It consists of long-chain saturated fatty acids--mainly palmitic and
Autor:
Odile Gateau-Roesch, E. Pavlov, Alisa V. Lazareva, Pierre Louisot, Nils-Erik L. Saris, E. A. Limarenko, Galina D. Mironova, Christiane Levrat
Publikováno v:
Journal of Bioenergetics and Biomembranes. 32:105-110
A hydrophobic, low-molecular weight component extracted from mitochondria forms aCa2+-activated ion channel in black-lipid membranes (Mironova et al., 1997). At pH 8.3–8.5, thecomponent has a high-affinity binding site for Ca2+ with a Kd of 8 × 10
Autor:
Christiane Levrat, Pierre Louisot
Publikováno v:
Biochemical and Biophysical Research Communications. 221:531-538
We have previously reported that TNF induced changes in mitochondrial enzymes, one of which, succinate-dehydrogenase, is specifically activated in various TNF-sensitive cell lines. In an attempt to further characterize the mechanism of trans-membrane
Publikováno v:
Life Sciences. 49:1731-1737
We have studied TNF-induced changes in mitochondrial enzymes. One enzyme, succinate dehydrogenase (SDH), is specifically activated in TNF sensitive cells including U937 (human monocytic), WEHI-164 (murine fibrosarcoma), and ME-180 (human cervical car
Publikováno v:
Journal of Biological Chemistry. 265:18797-18802
Two membrane fractions of intermediate density between inner and outer mitochondrial membranes were isolated by density gradient centrifugation from osmotically lysed mitochondria and mitoplasts of liver. These fractions were characterized by the pre
Autor:
Pierre Louisot, Christiane Levrat
Publikováno v:
Biochemical and biophysical research communications. 183(2)
Mitochondria were fractionated according to a procedure which allowed to get free outer and inner membrane plus two distinct contact sites between the two membranes. The data indicate that phospholipase A2 is localized in outer membrane contact sites
Publikováno v:
The International journal of biochemistry. 22(3)
1. 1. Glycosylation of endogenous dolichol acceptors was higher in mitochondria than in C 30,000 g (Golgi apparatus-rich fraction) and C 100.000 g (endoplasmic reticulum-rich fraction). 2. 2. In mitochondria, N-glycoprotein biosynthesized were compos
Publikováno v:
Journal of Bioenergetics & Biomembranes; Apr2004, Vol. 36 Issue 2, p171-178, 8p