Search

Your search keyword '"Blanc, L"' showing total 13 results
Start Over Author "Blanc, L" Publisher wiley
13 results on '"Blanc, L"'

2. Expression of Concern: HMGB 1 mediates splenomegaly and expansion of splenic CD 11b+ L y‐6 C high inflammatory monocytes in murine sepsis survivors

Author

Valdés‐Ferrer, S. I., primary, Rosas‐Ballina, M., additional, Olofsson, P. S., additional, Lu, B., additional, Dancho, M. E., additional, Ochani, M., additional, Li, J. H., additional, Scheinerman, J. A., additional, Katz, D. A., additional, Levine, Y. A., additional, Hudson, L. K., additional, Yang, H., additional, Pavlov, V. A., additional, Roth, J., additional, Blanc, L., additional, Antoine, D. J., additional, Chavan, S. S., additional, Andersson, U., additional, Diamond, B., additional, and Tracey, K. J., additional

Published
2013
Full Text
View/download PDF

3. How can quantitative ecology be attractive to young scientists? Balancing computer/desk work with fieldwork

Author

Gimenez, O., primary, Abadi, F., additional, Barnagaud, J‐Y., additional, Blanc, L., additional, Buoro, M., additional, Cubaynes, S., additional, Desprez, M., additional, Gamelon, M., additional, Guilhaumon, F., additional, Lagrange, P., additional, Madon, B., additional, Marescot, L., additional, Papadatou, E., additional, Papaïx, J., additional, Péron, G., additional, and Servanty, S., additional

Published
2012
Full Text
View/download PDF

5. Does the disturbance hypothesis explain the biomass increase in basin‐wide Amazon forest plot data?

Author

GLOOR, M., primary, PHILLIPS, O. L., additional, LLOYD, J. J., additional, LEWIS, S. L., additional, MALHI, Y., additional, BAKER, T. R., additional, LÓPEZ‐GONZALEZ, G., additional, PEACOCK, J., additional, ALMEIDA, S., additional, De OLIVEIRA, A. C. ALVES, additional, ALVAREZ, E., additional, AMARAL, I., additional, ARROYO, L., additional, AYMARD, G., additional, BANKI, O., additional, BLANC, L., additional, BONAL, D., additional, BRANDO, P., additional, CHAO, K.‐J., additional, CHAVE, J., additional, DÁVILA, N., additional, ERWIN, T., additional, SILVA, J., additional, Di FIORE, A., additional, FELDPAUSCH, T. R., additional, FREITAS, A., additional, HERRERA, R., additional, HIGUCHI, N., additional, HONORIO, E., additional, JIMÉNEZ, E., additional, KILLEEN, T., additional, LAURANCE, W., additional, MENDOZA, C., additional, MONTEAGUDO, A., additional, ANDRADE, A., additional, NEILL, D., additional, NEPSTAD, D., additional, VARGAS, P. NÚÑEZ, additional, PEÑUELA, M. C., additional, CRUZ, A. PEÑA, additional, PRIETO, A., additional, PITMAN, N., additional, QUESADA, C., additional, SALOMÃO, R., additional, SILVEIRA, MARCOS, additional, SCHWARZ, M., additional, STROPP, J., additional, RAMÍREZ, F., additional, RAMÍREZ, H., additional, RUDAS, A., additional, Ter STEEGE, H., additional, SILVA, N., additional, TORRES, A., additional, TERBORGH, J., additional, VÁSQUEZ, R., additional, and Van Der HEIJDEN, G., additional

Published
2009
Full Text
View/download PDF

12. Extracellular 20S proteasome secreted via microvesicles can degrade poorly folded proteins and inhibit Galectin-3 agglutination activity.

Author

Bonhoure A, Henry L, Bich C, Blanc L, Bergeret B, Bousquet MP, Coux O, Stoebner PE, and Vidal M

Subjects
Agglutination, Cytoplasm metabolism, Humans, Proteolysis, Galectin 3 metabolism, Proteasome Endopeptidase Complex metabolism
Abstract

Proteasomes are major non-lysosomal proteolytic complexes localized in the cytoplasm and in the nucleus of eukaryotic cells. Strikingly, high levels of extracellular proteasome have also been evidenced in the plasma (p-proteasome) of patients with specific diseases. Here, we examined the process by which proteasomes are secreted, as well as their structural and functional features once in the extracellular space. We demonstrate that assembled 20S core particles are secreted by cells within microvesicles budding from the plasma membrane. Part of the extracellular proteasome pool is also free of membranes in the supernatant of cultured cells, and likely originates from microvesicles leakage. We further demonstrate that this free proteasome released by cells (cc-proteasome for cell culture proteasome) possesses latent proteolytic activity and can degrade various extracellular proteins. Both standard (no immune-subunits) and intermediate (containing some immune-subunits) forms of 20S are observed. Moreover, we show that galectin-3, which displays a highly disordered N-terminal region, is efficiently cleaved by purified cc-proteasome, without SDS activation, likely after its binding to PSMA3 (α7) subunit through its intrinsically disordered region. As a consequence, galectin-3 is unable to induce red blood cells agglutination when preincubated with cc-proteasome. These results highlight potential novel physio- and pathologic functions for the extracellular proteasome., (© 2022 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.)

Published
2022
Full Text
View/download PDF

13. Degradation of AP2 during reticulocyte maturation enhances binding of hsc70 and Alix to a common site on TFR for sorting into exosomes.

Author

Géminard C, De Gassart A, Blanc L, and Vidal M

Subjects
Adaptor Protein Complex alpha Subunits metabolism, Amino Acid Sequence, Animals, Binding Sites, Biotinylation, Chromatography, Affinity, Dimerization, Erythrocytes cytology, Erythrocytes metabolism, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins genetics, Humans, Leupeptins pharmacology, Molecular Sequence Data, Peptide Fragments chemistry, Peptide Fragments metabolism, Protein Binding, Protein Processing, Post-Translational, Rats, Receptors, Transferrin chemistry, Temperature, Adaptor Protein Complex 2 metabolism, Calcium-Binding Proteins metabolism, Carrier Proteins metabolism, Exocytosis, HSP70 Heat-Shock Proteins metabolism, Receptors, Transferrin metabolism, Reticulocytes cytology, Reticulocytes metabolism
Abstract

Reticulocytes release small membrane vesicles termed exosomes during their maturation in erythrocytes. The transferrin receptor (TfR) is completely lost from the red cell surface by its segregation in the secreted vesicles where it interacts with the heat shock cognate 70 kDa protein (hsc70). We have now determined a region of the TfR that can potentially interact with hsc70. The peptide P1 (YTRFSLARQV) from the TfR cytosolic domain: (i). binds to hsc70 (ii). with an increased affinity in oxidative conditions, (iii). competes for binding of an unfolded protein to hsc70, and (iv). inhibits the interaction of hsc70 with a recombinant protein corresponding to the cytosolic domain of the receptor. This peptide encompasses the internalization motif (YTRF) of the receptor, and accordingly an affinity column made with the immobilized peptide retains hsc70 and also the AP2 adaptor complex. On the other hand, we show that AP2 is degraded by the proteasome system during reticulocyte maturation and that the presence of the proteasome inhibitor during in vitro red cell maturation inhibits AP2 degradation and specifically decreases TfR secretion via exosomes. Finally, coimmunoprecipitation of Alix with the exosomal TfR, and binding of P1 peptide to the Alix homolog PalA suggest that Alix also interacts with the YTRF motif and contributes to exosomal TfR sorting.

Published
2004
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results