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7 results on '"Aguennoz M"'

1. P01 LACTATE TRAFFICKING INHIBITION RESTORES SENSITIVITY TO PROTEASOME INHIBITHORS AND ORCHESTRATES IMMUNOMICROENVIRONMENT IN MULTIPLE MYELOMA

Author

Giallongo, C., primary, Zuppelli, T., additional, Scandura, G., additional, La Spina, E., additional, Dulcamare, I., additional, Cambria, D., additional, Giallongo, S., additional, Romano, A., additional, Parrinello, N., additional, Del Fabro, V., additional, Aguennoz, M., additional, Li Volti, G., additional, Palumbo, G.A., additional, Di Raimondo, F., additional, and Tibullo, D., additional

Published
2023
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6. Early onset calpainopathy with normal non-functional calpain 3 level

Author

F. Vitale, M. Aguennoz, Vincenzo Nigro, Robert Lanzillo, Lucia Santoro, S. Aurino, Marina Fanin, E. Del Giudice, Chiara Fiorillo, Lanzillo, R, Aurino, S, Fanin, M, Aguennoz, M, Vitale, F, Fiorillo, C, DEL GIUDICE, E, Nigro, Vincenzo, Santoro, L., Lanzillo, Roberta, DEL GIUDICE, Ennio, Nigro, V, and Santoro, Lucio

Subjects
Pathology, medicine.medical_specialty, Blotting, Western, DNA Mutational Analysis, Muscle Proteins, Compound heterozygosity, Polymerase Chain Reaction, Asymptomatic, Diagnosis, Differential, Developmental Neuroscience, Western blot, medicine, Humans, Point Mutation, Chromatography, High Pressure Liquid, Loss function, Muscle biopsy, medicine.diagnostic_test, biology, Calpain, Exons, medicine.disease, Isoenzymes, CALPAINOPATHY, GIRDLE MUSCULAR-DYSTROPHY, PROTEIN EXPRESSION, LGMD2A, MUSCLE, MUTATIONS, GENES 2A, Muscular Dystrophies, Limb-Girdle, Child, Preschool, Pediatrics, Perinatology and Child Health, biology.protein, Female, Neurology (clinical), medicine.symptom, Limb-girdle muscular dystrophy
Abstract

Limb girdle muscular dystrophy 2A (LGMD2A), caused by calpain 3 deficiency, is currently diagnosed through the immunodetection of muscle protein by Western blot (WB) analysis . However, WB may provide normal results in patients with LGMD2A. The case of a female (3y 6mo of age) is described. She was found to be affected by asymptomatic hypercreatine-kinaesaemia during routine biochemical analysis at 10 months of age and had developed myopathic signs at the last neurological assessment. The WB of muscle biopsy performed at 28 months of age showed a normal quantity and pattern of bands for calpain 3. Despite this finding, on molecular analysis she was found to be a compound heterozygote for two mutations of the calpain 3 (CAPN3) gene (R110X and G222R). Autocatalytic activity assay showed a loss of function of calpain 3. This is the first genetically confirmed case of very early onset calpainopathy with a normal amount of protein at WB. Molecular analysis is also suggested in very young patients with normal WB.

Published
2006

7. Lactate trafficking inhibition restores sensitivity to proteasome inhibitors and orchestrates immuno-microenvironment in multiple myeloma.

Author

Barbato A, Giallongo C, Giallongo S, Romano A, Scandura G, Concetta S, Zuppelli T, Lolicato M, Lazzarino G, Parrinello N, Del Fabro V, Fontana P, Aguennoz M, Li Volti G, Palumbo GA, Di Raimondo F, and Tibullo D

Subjects
Humans, Lactic Acid metabolism, Proteasome Inhibitors pharmacology, Cell Line, Tumor, Tumor Microenvironment, Multiple Myeloma drug therapy, Symporters genetics, Symporters metabolism
Abstract

Metabolic changes of malignant plasma cells (PCs) and adaptation to tumour microenvironment represent one of the hallmarks of multiple myeloma (MM). We previously showed that MM mesenchymal stromal cells are more glycolytic and produce more lactate than healthy counterpart. Hence, we aimed to explore the impact of high lactate concentration on metabolism of tumour PCs and its impact on the efficacy of proteasome inhibitors (PIs). Lactate concentration was performed by colorimetric assay on MM patient's sera. The metabolism of MM cell treated with lactate was assessed by seahorse and real time Polymerase Chain Reaction (PCR). Cytometry was used to evaluate mitochondrial reactive oxygen species (mROS), apoptosis and mitochondrial depolarization. Lactate concentration resulted increased in MM patient's sera. Therefore, PCs were treated with lactate and we observed an increase of oxidative phosphorylation-related genes, mROS and oxygen consumption rate. Lactate supplementation exhibited a significant reduction in cell proliferation and less responsive to PIs. These data were confirmed by pharmacological inhibition of monocarboxylate transporter 1 (MCT1) by AZD3965 which was able to overcame metabolic protective effect of lactate against PIs. Consistently, high levels of circulating lactate caused expansion of Treg and monocytic myeloid derived suppressor cells and such effect was significantly reduced by AZD3965. Overall, these findings showed that targeting lactate trafficking in TME inhibits metabolic rewiring of tumour PCs, lactate-dependent immune evasion and thus improving therapy efficacy., (© 2023 The Authors. Cell Proliferation published by Beijing Institute for Stem Cell and Regenerative Medicine and John Wiley & Sons Ltd.)

Published
2023
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