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9 results on '"Herbi, Linda"'

1. Supporting Information Homotrimerization Approach in the Design of Thrombospondin-1 Mimetic Peptides with Improved Potency in Triggering Regulated Cell Death of Cancer Cells

Author

Denèfle, Thomas, Pramil, Elodie, Gómez-Morales, Luis, Levasseur, Mikail, Lardé, Eva, Newton, Clara, Herry, Kenny, Herbi, Linda, Lamotte, Yann, Odile, Estelle, Ancellin, Nicolas, Grondin, Pascal, Martinez-Torres, Ana-Carolina, Viviani, Fabrice, Merle-Béral, Hélène, Lequin, Olivier, Susin, Santos, Karoyan, Philippe, Sorbonne Université (SU), Laboratoire des biomolécules (LBM UMR 7203), Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Département de Chimie - ENS Paris, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Chimie Moléculaire de Paris Centre (FR 2769), Institut de Chimie du CNRS (INC)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris sciences et lettres (PSL), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Universidad Autonoma de Nuevo Leon [Mexique] (UANL), Oncodesign [Dijon], Laboratoires Oncodesign [Villebon-sur-Yvette], and Centre de Recherches François Hyafil [Villebon-sur-Yvette]

Subjects
[SDV]Life Sciences [q-bio]
Abstract

International audience; In order to optimize the potency of the first serum-stable peptide agonist of CD47 (PKHB1) in triggering regulated cell death of cancer cells, we designed a maturation process aimed to mimic the trimeric structure of the thrombospondin-1/CD47 binding epitope. For that purpose, an N-methylation scan of the PKHB1 sequence was realized to prevent peptide aggregation. Structural and pharmacological analyses were conducted in order to assess the conformational impact of these chemical modifications on the backbone structure and the biological activity. This structure–activity relationship study led to the discovery of a highly soluble N-methylated peptide that we termed PKT16. Afterward, this monomer was used for the design of a homotrimeric peptide mimic that we termed [PKT16]3, which proved to be 10-fold more potent than its monomeric counterpart. A pharmacological evaluation of [PKT16]3 in inducing cell death of adherent (A549) and nonadherent (MEC-1) cancer cell lines was also performed.

Published
2019

2. Supporting Information Homotrimerization Approach in the Design of Thrombospondin-1 Mimetic Peptides with Improved Potency in Triggering Regulated Cell Death of Cancer Cells

Author

Gómez-Morales, Luis, Merle-Béral, Hélène, Denèfle, Thomas, Pramil, Elodie, Luis Gómez-Morales, , Levasseur, Mikail, Lardé, Eva, Newton, Clara, Herry, Kenny, Herbi, Linda, Lamotte, Yann, Odile, Estelle, Ancellin, Nicolas, Grondin, Pascal, Martinez-Torres, Ana-Carolina, Viviani, Fabrice, Merle-Beral, Hélène, Lequin, Olivier, Susin, Santos, Karoyan, Philippe, Universidad Autonoma de Nuevo Leon [Mexique] (UANL), Sorbonne Université (SU), Laboratoire des biomolécules (LBM UMR 7203), Chimie Moléculaire de Paris Centre (FR 2769), École normale supérieure - Paris (ENS Paris)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP)-ESPCI ParisTech-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP)-ESPCI ParisTech-Centre National de la Recherche Scientifique (CNRS)-Département de Chimie - ENS Paris, École normale supérieure - Paris (ENS Paris)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Paris (ENS Paris), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), and OncoDesign

Subjects
[SDV]Life Sciences [q-bio]
Abstract

International audience; In order to optimize the potency of the first serum-stable peptide agonist of CD47 (PKHB1) in triggering regulated cell death of cancer cells, we designed a maturation process aimed to mimic the trimeric structure of the thrombospondin-1/CD47 binding epitope. For that purpose, an N-methylation scan of the PKHB1 sequence was realized to prevent peptide aggregation. Structural and pharmacological analyses were conducted in order to assess the conformational impact of these chemical modifications on the backbone structure and the biological activity. This structure–activity relationship study led to the discovery of a highly soluble N-methylated peptide that we termed PKT16. Afterward, this monomer was used for the design of a homotrimeric peptide mimic that we termed [PKT16]3, which proved to be 10-fold more potent than its monomeric counterpart. A pharmacological evaluation of [PKT16]3 in inducing cell death of adherent (A549) and nonadherent (MEC-1) cancer cell lines was also performed.

Published
2019

3. CD47 agonist peptides induce programmed cell death in refractory chronic lymphocytic leukemia B cells via PLC[gamma]1 activation: evidence from mice and humans

Author

Martinez-Torres, Ana-Carolina, Quiney, Claire, Attout, Tarik, Boullet, Heloise, Herbi, Linda, Vela, Laura, Barbier, Sandrine, Chateau, Danielle, Chapiro, Elise, Nguyen-Khac, Florence, Davi, Frederic, Le Garff-Tavernier, Magali, Moumne, Roba, Sarfati, Marika, Karoyan, Philippe, Merle-Beral, Helene, Launay, Pierre, and Susin, Santos A.

Subjects
B cells -- Health aspects, Phospholipases -- Health aspects, Peptides -- Health aspects, Cell death -- Identification and classification, Chronic lymphocytic leukemia -- Physiological aspects, Biological sciences
Abstract

Background Chronic lymphocytic leukemia (CLL), the most common adulthood leukemia, is characterized by the accumulation of abnormal [CD5.sup.+] B lymphocytes, which results in a progressive failure of the immune system. Despite intense research efforts, drug resistance remains a major cause of treatment failure in CLL, particularly in patients with dysfunctional TP53. The objective of our work was to identify potential approaches that might overcome CLL drug refractoriness by examining the pro-apoptotic potential of targeting the cell surface receptor CD47 with serum-stable agonist peptides. Methods and Findings In peripheral blood samples collected from 80 patients with CLL with positive and adverse prognostic features, we performed in vitro genetic and molecular analyses that demonstrate that the targeting of CD47 with peptides derived from the C-terminal domain of thrombospondin-1 efficiently kills the malignant CLL B cells, including those from high-risk individuals with a dysfunctional TP53 gene, while sparing the normal T and B lymphocytes from the CLL patients. Further studies reveal that the differential response of normal B lymphocytes, collected from 20 healthy donors, and leukemic B cells to CD47 peptide targeting results from the sustained activation in CLL B cells of phospholipase C gamma-1 (PLC[gamma]1), a protein that is significantly over-expressed in CLL. Once phosphorylated at tyrosine 783, PLC[gamma]1 enables a [Ca.sup.2+]-mediated, caspase-independent programmed cell death (PCD) pathway that is not down-modulated by the lymphocyte microenvironment. Accordingly, down-regulation of PLC[gamma]1 or pharmacological inhibition of PLC[gamma]1 phosphorylation abolishes CD47-mediated killing. Additionally, in a CLL-xenograft model developed in NOD/scid gamma mice, we demonstrate that the injection of CD47 agonist peptides reduces tumor burden without inducing anemia or toxicity in blood, liver, or kidney. The limitations of our study are mainly linked to the affinity of the peptides targeting CD47, which might be improved to reach the standard requirements in drug development, and the lack of a CLL animal model that fully mimics the human disease. Conclusions Our work provides substantial progress in (i) the development of serum-stable CD47 agonist peptides that are highly effective at inducing PCD in CLL, (ii) the understanding of the molecular events regulating a novel PCD pathway that overcomes CLL apoptotic avoidance, (iii) the identification of PLC[gamma]1 as an over-expressed protein in CLL B cells, and (iv) the description of a novel peptide-based strategy against CLL., Introduction Chronic lymphocytic leukemia (CLL), a human malignancy caused by an imbalance between proliferation and programmed cell death (PCD) [1], is the most common form of leukemia in adults. CLL [...]

Published
2015
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4. Homotrimerization Approach in the Design of Thrombospondin-1 Mimetic Peptides with Improved Potency in Triggering Regulated Cell Death of Cancer Cells

Author

Denèfle, Thomas, primary, Pramil, Elodie, additional, Gómez-Morales, Luis, additional, Levasseur, Mikail D., additional, Lardé, Eva, additional, Newton, Clara, additional, Herry, Kenny, additional, Herbi, Linda, additional, Lamotte, Yann, additional, Odile, Estelle, additional, Ancellin, Nicolas, additional, Grondin, Pascal, additional, Martinez-Torres, Ana-Carolina, additional, Viviani, Fabrice, additional, Merle-Beral, Hélène, additional, Lequin, Olivier, additional, Susin, Santos A., additional, and Karoyan, Philippe, additional

Published
2019
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5. Homotrimerization Approach in the Design of Thrombospondin-1 Mimetic Peptides with Improved Potency in Triggering Regulated Cell Death of Cancer Cells

Author

Denèfle, Thomas, Pramil, Elodie, Gómez-Morales, Luis, Levasseur, Mikail D., Lardé, Eva, Newton, Clara, Herry, Kenny, Herbi, Linda, Lamotte, Yann, Odile, Estelle, Ancellin, Nicolas, Grondin, Pascal, Martinez-Torres, Ana-Carolina, Viviani, Fabrice, Merle-Beral, Hélène, Lequin, Olivier, Susin, Santos A., and Karoyan, Philippe

Abstract

In order to optimize the potency of the first serum-stable peptide agonist of CD47 (PKHB1) in triggering regulated cell death of cancer cells, we designed a maturation process aimed to mimic the trimeric structure of the thrombospondin-1/CD47 binding epitope. For that purpose, an N-methylation scan of the PKHB1 sequence was realized to prevent peptide aggregation. Structural and pharmacological analyses were conducted in order to assess the conformational impact of these chemical modifications on the backbone structure and the biological activity. This structure–activity relationship study led to the discovery of a highly soluble N-methylated peptide that we termed PKT16. Afterward, this monomer was used for the design of a homotrimeric peptide mimic that we termed [PKT16]3, which proved to be 10-fold more potent than its monomeric counterpart. A pharmacological evaluation of [PKT16]3in inducing cell death of adherent (A549) and nonadherent (MEC-1) cancer cell lines was also performed.

Published
2024
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6. Thrombospondin-1 Mimetic Agonist Peptides Induce Selective Death in Tumor Cells: Design, Synthesis, and Structure–Activity Relationship Studies

Author

Denèfle, Thomas, primary, Boullet, Héloise, additional, Herbi, Linda, additional, Newton, Clara, additional, Martinez-Torres, Ana-Carolina, additional, Guez, Alexandre, additional, Pramil, Elodie, additional, Quiney, Claire, additional, Pourcelot, Marilyne, additional, Levasseur, Mikail D., additional, Lardé, Eva, additional, Moumné, Roba, additional, Ogi, François-Xavier, additional, Grondin, Pascal, additional, Merle-Beral, Hélène, additional, Lequin, Olivier, additional, Susin, Santos A., additional, and Karoyan, Philippe, additional

Published
2016
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7. Ublituximab, an Optimized Anti-CD20 Monoclonal Antibody, Demonstrates Greater NK-Mediated ADCC Than Rituximab in Waldenstrom's Macroglobulinemia Patients Supporting a Therapeutic Strategy with Ublituximab

Author

Le Garff-Tavernier, Magali, primary, Herbi, Linda, additional, de Romeuf, Christophe, additional, Prost, Jean-Francois, additional, Debré, Patrice, additional, Urbain, Rémi, additional, Leblond, Véronique, additional, Vieillard, Vincent, additional, and Merle-Béral, Hélène, additional

Published
2012
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8. Bone Marrow Microenvironment in an In Vitro Model of Gaucher Disease: Consequences of Glucocerebrosidase Deficiency

Author

Lecourt, Séverine, primary, Vanneaux, Valérie, additional, Cras, Audrey, additional, Freida, Delphine, additional, Heraoui, Djazia, additional, Herbi, Linda, additional, Caillaud, Catherine, additional, Chomienne, Christine, additional, Marolleau, Jean-Pierre, additional, Belmatoug, Nadia, additional, and Larghero, Jérôme, additional

Published
2012
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9. The optimized anti-CD20 monoclonal antibody ublituximab bypasses natural killer phenotypic features in Waldenström macroglobulinemia.

Author

Le Garff-Tavernier M, Herbi L, de Romeuf C, Azar N, Roos-Weil D, Bonnemye P, Urbain R, Leblond V, Merle-Beral H, and Vieillard V

Subjects
Antibodies, Monoclonal, Murine-Derived pharmacology, Antigens, CD20 metabolism, Antineoplastic Agents pharmacology, Cytotoxicity, Immunologic, Humans, Immunologic Factors pharmacology, Killer Cells, Natural metabolism, Lymphocyte Subsets drug effects, Lymphocyte Subsets immunology, Lymphocyte Subsets metabolism, Rituximab, Antibodies, Monoclonal, Murine-Derived therapeutic use, Antineoplastic Agents therapeutic use, Immunologic Factors therapeutic use, Killer Cells, Natural drug effects, Killer Cells, Natural immunology, Waldenstrom Macroglobulinemia drug therapy, Waldenstrom Macroglobulinemia immunology
Published
2015
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