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2. Nlrp2 deletion ameliorates kidney damage in a mouse model of cystinosis

Author

Rossi, Marianna Nicoletta, primary, Matteo, Valentina, additional, Diomedi-Camassei, Francesca, additional, De Leo, Ester, additional, Devuyst, Olivier, additional, Lamkanfi, Mohamed, additional, Caiello, Ivan, additional, Loricchio, Elena, additional, Bellomo, Francesco, additional, Taranta, Anna, additional, Emma, Francesco, additional, De Benedetti, Fabrizio, additional, and Prencipe, Giusi, additional

Published
2024
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3. Intrinsic Bone Defects in Cystinotic Mice

Author

Battafarano, Giulia, Rossi, Michela, Rega, Laura R., Di Giovamberardino, Gianna, Pastore, Anna, D'Agostini, Matteo, Porzio, Ottavia, Nevo, Nathalie, Emma, Francesco, Taranta, Anna, and Del Fattore, Andrea

Published
2019
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5. Genistein improves renal disease in a mouse model of nephropathic cystinosis: a comparison study with cysteamine

Author

De Leo, Ester, primary, Taranta, Anna, additional, Raso, Roberto, additional, Polishchuk, Elena, additional, D’Oria, Valentina, additional, Pezzullo, Marco, additional, Goffredo, Bianca Maria, additional, Cairoli, Sara, additional, Bellomo, Francesco, additional, Battafarano, Giulia, additional, Camassei, Francesca Diomedi, additional, Del Fattore, Andrea, additional, Polishchuk, Roman, additional, Emma, Francesco, additional, and Rega, Laura Rita, additional

Published
2022
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6. Multisystem involvement, defective lysosomes and impaired autophagy in a novel rat model of nephropathic cystinosis

Author

UCL - SSS/IREC/NEFR - Pôle de Néphrologie, Krohn, Patrick, Rega, Laura Rita, Harvent, Marianne, Festa, Beatrice Paola, Taranta, Anna, Luciani, Alessandro, Dewulf, Joseph P., Cremonesi, Alessio, Camassei, Francesca Diomedi, Hanson, James V M, Gerth-Kahlert, Christina, Emma, Francesco, Berquez, Marine, Devuyst, Olivier, UCL - SSS/IREC/NEFR - Pôle de Néphrologie, Krohn, Patrick, Rega, Laura Rita, Harvent, Marianne, Festa, Beatrice Paola, Taranta, Anna, Luciani, Alessandro, Dewulf, Joseph P., Cremonesi, Alessio, Camassei, Francesca Diomedi, Hanson, James V M, Gerth-Kahlert, Christina, Emma, Francesco, Berquez, Marine, and Devuyst, Olivier

Published
2022

7. Multisystem involvement, defective lysosomes, and impaired autophagy in a novel rat model of Nephropathic Cystinosis

Author

Krohn, Patrick; https://orcid.org/0000-0001-5821-9919, Rega, Laura Rita; https://orcid.org/0000-0003-4847-366X, Harvent, Marianne, Festa, Beatrice Paola; https://orcid.org/0000-0002-2243-6054, Taranta, Anna; https://orcid.org/0000-0002-7606-9085, Luciani, Alessandro; https://orcid.org/0000-0001-7219-3719, Dewulf, Joseph; https://orcid.org/0000-0001-7223-2706, Cremonesi, Alessio; https://orcid.org/0000-0002-1524-4169, Camassei, Francesca Diomedi; https://orcid.org/0000-0003-2829-2407, Hanson, James V M; https://orcid.org/0000-0003-3383-4856, Gerth-Kahlert, Christina; https://orcid.org/0000-0001-6298-615X, Emma, Francesco; https://orcid.org/0000-0002-0383-3468, Berquez, Marine; https://orcid.org/0000-0001-6909-2060, Devuyst, Olivier; https://orcid.org/0000-0003-3744-4767, Krohn, Patrick; https://orcid.org/0000-0001-5821-9919, Rega, Laura Rita; https://orcid.org/0000-0003-4847-366X, Harvent, Marianne, Festa, Beatrice Paola; https://orcid.org/0000-0002-2243-6054, Taranta, Anna; https://orcid.org/0000-0002-7606-9085, Luciani, Alessandro; https://orcid.org/0000-0001-7219-3719, Dewulf, Joseph; https://orcid.org/0000-0001-7223-2706, Cremonesi, Alessio; https://orcid.org/0000-0002-1524-4169, Camassei, Francesca Diomedi; https://orcid.org/0000-0003-2829-2407, Hanson, James V M; https://orcid.org/0000-0003-3383-4856, Gerth-Kahlert, Christina; https://orcid.org/0000-0001-6298-615X, Emma, Francesco; https://orcid.org/0000-0002-0383-3468, Berquez, Marine; https://orcid.org/0000-0001-6909-2060, and Devuyst, Olivier; https://orcid.org/0000-0003-3744-4767

Abstract

Recessive mutations in the CTNS gene encoding the lysosomal transporter cystinosin cause cystinosis, a lysosomal storage disease leading to kidney failure and multisystem manifestations. A Ctns knock-out mouse model recapitulates features of cystinosis, but the delayed onset of kidney manifestations, phenotype variability, and strain effects limit its use for mechanistic and drug development studies. To provide a better model for cystinosis, we generated a Ctns knock-out rat model using CRISPR/Cas9 technology. The Ctns-/- rats display progressive cystine accumulation and crystal formation in multiple tissues including kidney, liver and thyroid. They show an early onset and progressive loss of urinary solutes, indicating generalized proximal tubule dysfunction, with development of typical swan-neck lesions, tubulointerstitial fibrosis and kidney failure, and decreased survival. The Ctns-/- rats also present crystals in the cornea, and bone and liver defects, like in patients. Mechanistically, the loss of cystinosin induces a phenotype switch associating abnormal proliferation and dedifferentiation, loss of apical receptors and transporters, and defective lysosomal activity and autophagy in the cells. Primary cultures of proximal tubule cells derived from the Ctns-/- rat kidneys confirmed the key changes caused by cystine overload, including reduced endocytic uptake, increased proliferation and defective lysosomal dynamics and autophagy. The novel Ctns-/- rat model and derived proximal tubule cell system provide invaluable tools to investigate the pathogenesis of cystinosis and to accelerate drug discovery.

Published
2022

9. Multisystem involvement, defective lysosomes and impaired autophagy in a novel rat model of nephropathic cystinosis

Author

Krohn, Patrick, primary, Rega, Laura Rita, additional, Harvent, Marianne, additional, Festa, Beatrice Paola, additional, Taranta, Anna, additional, Luciani, Alessandro, additional, Dewulf, Joseph, additional, Cremonesi, Alessio, additional, Camassei, Francesca Diomedi, additional, Hanson, James V M, additional, Gerth-Kahlert, Christina, additional, Emma, Francesco, additional, Berquez, Marine, additional, and Devuyst, Olivier, additional

Published
2022
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10. Multisystem involvement, defective lysosomes, and impaired autophagy in a novel rat model of Nephropathic Cystinosis

Author

Krohn, Patrick, Rega, Laura Rita, Harvent, Marianne, Festa, Beatrice Paola, Taranta, Anna, Luciani, Alessandro, Dewulf, Joseph, Cremonesi, Alessio, Camassei, Francesca Diomedi, Hanson, James V M, Gerth-Kahlert, Christina, Emma, Francesco, Berquez, Marine, Devuyst, Olivier, University of Zurich, and UCL - SSS/IREC/NEFR - Pôle de Néphrologie

Subjects
10018 Ophthalmology Clinic, Cystinosis, 610 Medicine & health, General Medicine, Fanconi Syndrome, Rats, 10052 Institute of Physiology, Mice, Amino Acid Transport Systems, Neutral, 10036 Medical Clinic, Autophagy, Genetics, Animals, Cystine, Renal Insufficiency, Lysosomes, Molecular Biology, Genetics (clinical)
Abstract

Recessive mutations in the CTNS gene encoding the lysosomal transporter cystinosin cause cystinosis, a lysosomal storage disease leading to kidney failure and multisystem manifestations. A Ctns knockout mouse model recapitulates features of cystinosis, but the delayed onset of kidney manifestations, phenotype variability and strain effects limit its use for mechanistic and drug development studies. To provide a better model for cystinosis, we generated a Ctns knockout rat model using CRISPR/Cas9 technology. The Ctns−/− rats display progressive cystine accumulation and crystal formation in multiple tissues including kidney, liver and thyroid. They show an early onset and progressive loss of urinary solutes, indicating generalized proximal tubule dysfunction, with development of typical swan-neck lesions, tubulointerstitial fibrosis and kidney failure, and decreased survival. The Ctns−/− rats also present crystals in the cornea, and bone and liver defects, as observed in patients. Mechanistically, the loss of cystinosin induces a phenotype switch associating abnormal proliferation and dedifferentiation, loss of apical receptors and transporters, and defective lysosomal activity and autophagy in the cells. Primary cultures of proximal tubule cells derived from the Ctns−/− rat kidneys confirmed the key changes caused by cystine overload, including reduced endocytic uptake, increased proliferation and defective lysosomal dynamics and autophagy. The novel Ctns−/− rat model and derived proximal tubule cell system provide invaluable tools to investigate the pathogenesis of cystinosis and to accelerate drug discovery.

Published
2022
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11. Benefits and Toxicity of Disulfiram in Preclinical Models of Nephropathic Cystinosis

Author

Taranta, Anna, elmonem, mohamed a, Bellomo, Francesco, Leo, Ester De, Boenzi, Sara, Janssen, Manoe J., Jamalpoor, Amer, Cairoli, Sara, Pastore, Anna, Stefanis, Cristiano De, Colucci, Manuela, Rega, Laura R., giovannoni, isabella, Francalanci, Paola, Heuvel, Lambertus P. van den, Dionisi-Vici, Carlo, Goffredo, Bianca M., Masereeuw, Rosalinde, Levtchenko, Elena, Emma, Francesco, Afd Pharmacology, Pharmacology, Afd Pharmacology, and Pharmacology

Subjects
Embryo, Nonmammalian, mice, QH301-705.5, Cystinosis, Cystine, disulfiram, Apoptosis, Pharmacology, Article, Mice, chemistry.chemical_compound, All institutes and research themes of the Radboud University Medical Center, cystinosis, zebrafish, Nephropathic Cystinosis, Toxicity Tests, Disulfiram, medicine, Animals, Humans, Disulfides, Biology (General), Zebrafish, Mice, Knockout, Medicine(all), business.industry, General Medicine, medicine.disease, Acetylcysteine, Disease Models, Animal, Renal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11], Cystinosin, chemistry, Larva, Symporter, Toxicity, Kidney Diseases, Cysteamine, business, medicine.drug
Abstract

Nephropathic cystinosis is a rare disease caused by mutations of the CTNS gene that encodes for cystinosin, a lysosomal cystine/H+ symporter. The disease is characterized by early-onset chronic kidney failure and progressive development of extra-renal complications related to cystine accumulation in all tissues. At the cellular level, several alterations have been demonstrated, including enhanced apoptosis, altered autophagy, defective intracellular trafficking, and cell oxidation, among others. Current therapy with cysteamine only partially reverts some of these changes, highlighting the need to develop additional treatments. Among compounds that were identified in a previous drug-repositioning study, disulfiram (DSF) was selected for in vivo studies. The cystine depleting and anti-apoptotic properties of DSF were confirmed by secondary in vitro assays and after treating Ctns-/- mice with 200 mg/kg/day of DSF for 3 months. However, at this dosage, growth impairment was observed. Long-term treatment with a lower dose (100 mg/kg/day) did not inhibit growth, but failed to reduce cystine accumulation, caused premature death, and did not prevent the development of renal lesions. In addition, DSF also caused adverse effects in cystinotic zebrafish larvae. DSF toxicity was significantly more pronounced in Ctns-/- mice and zebrafish compared to wild-type animals, suggesting higher cell toxicity of DSF in cystinotic cells. ispartof: CELLS vol:10 issue:12 ispartof: location:Switzerland status: published

Published
2021

12. Drug Repurposing in Rare Diseases: An Integrative Study of Drug Screening and Transcriptomic Analysis in Nephropathic Cystinosis

Author

Bellomo, Francesco, primary, De Leo, Ester, additional, Taranta, Anna, additional, Giaquinto, Laura, additional, Di Giovamberardino, Gianna, additional, Montefusco, Sandro, additional, Rega, Laura Rita, additional, Pastore, Anna, additional, Medina, Diego Luis, additional, Di Bernardo, Diego, additional, De Matteis, Maria Antonietta, additional, and Emma, Francesco, additional

Published
2021
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16. Human and animal fertility studies in cystinosis reveal signs of obstructive azoospermia, an altered blood‐testis barrier and a subtherapeutic effect of cysteamine in testis

Author

Reda, Ahmed, primary, Veys, Koenraad, additional, Kadam, Prashant, additional, Taranta, Anna, additional, Rega, Laura Rita, additional, Goffredo, Bianca M., additional, Camps, Chelsea, additional, Besouw, Martine, additional, Cyr, Daniel, additional, Albersen, Maarten, additional, Spiessens, Carl, additional, de Wever, Liesbeth, additional, Hamer, Robert, additional, Janssen, Mirian C.H., additional, D'Hauwers, Kathleen, additional, Wetzels, Alex, additional, Monnens, Leo, additional, van den Heuvel, Lambertus, additional, Goossens, Ellen, additional, and Levtchenko, Elena, additional

Published
2021
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17. Benefits and Toxicity of Disulfiram in Preclinical Models of Nephropathic Cystinosis

Author

Afd Pharmacology, Pharmacology, Taranta, Anna, elmonem, mohamed a, Bellomo, Francesco, Leo, Ester De, Boenzi, Sara, Janssen, Manoe J., Jamalpoor, Amer, Cairoli, Sara, Pastore, Anna, Stefanis, Cristiano De, Colucci, Manuela, Rega, Laura R., giovannoni, isabella, Francalanci, Paola, Heuvel, Lambertus P. van den, Dionisi-Vici, Carlo, Goffredo, Bianca M., Masereeuw, Rosalinde, Levtchenko, Elena, Emma, Francesco, Afd Pharmacology, Pharmacology, Taranta, Anna, elmonem, mohamed a, Bellomo, Francesco, Leo, Ester De, Boenzi, Sara, Janssen, Manoe J., Jamalpoor, Amer, Cairoli, Sara, Pastore, Anna, Stefanis, Cristiano De, Colucci, Manuela, Rega, Laura R., giovannoni, isabella, Francalanci, Paola, Heuvel, Lambertus P. van den, Dionisi-Vici, Carlo, Goffredo, Bianca M., Masereeuw, Rosalinde, Levtchenko, Elena, and Emma, Francesco

Published
2021

22. Identification and subcellular localization of a new cystinosin isoform

Author

Taranta, Anna, Petrini, Stefania, Palma, Alessia, Mannucci, Liliana, Wilmer, Martijn J., De Luca, Veronica, Diomedi-Camassei, Francesca, Corallini, Serena, Bellomo, Francesco, van den Heuvel, Lambert P., Levtchenko, Elena N., and Emma, Francesco

Subjects
Cystine -- Properties, Cystinosis -- Physiological aspects, Genetic disorders -- Physiological aspects, Kidneys -- Properties, Physiological research, Biological sciences
Abstract

Nephropathic cystinosis is a lysosomal disorder caused by functional defects of cystinosin, which mediates cystine efflux into the cytosol. The protein sequence contains at least two signals that target the protein to the lysosomal compartment, one of which is located at the carboxy terminal tail (GYDQL). We have isolated from a human kidney eDNA library a cystinosin isoform, which is generated by an alternative splicing of exon 12 that removes the GYDQL motif. Based on its last three amino acids, we have termed this protein cystinosin-LKG. Contrary to the lysosomal cystinosin isoform, expression experiments performed by transient transfection of green fluorescent protein fusion plasmids in HK2 cells showed that cystinosin-LKG is expressed in the plasma membrane, in lysosomes, and in other cytosolic structures. This subcellular localization of the protein was confirmed by transmission electron microscopy. In addition, immunogold labeling was observed in the endoplasmic reticulum and in the Golgi apparatus. Expression of the protein in renal tubular structures was also directly demonstrated by immunostaining of normal human kidney sections. The plasma membrane localization of cystinosin-LKG was directly tested by [[sup.35]S]cystine flux experiments in COS-1 cells. In the presence of a proton gradient, a marked enhancement of intracellular cystine transport was observed in cells overexpressing this isoform. These data indicate that the expression of the gene products encoded by the CTNS gene is not restricted to the lysosomal compartment. These finding may help elucidate the mechanisms of cell dysfunction in this disorder. genetic disease; nephropathic cystinosis; cystine transport

Published
2008

24. Genetic risk factors in typical haemolytic uraemic syndrome

Author

Taranta, Anna, Gianviti, Alessandra, Palma, Alessia, De Luca, Veronica, Mannucci, Liliana, Procaccino, Maria Antonietta, Ghiggeri, Gian Marco, Caridi, Gianluca, Fruci, Doriana, Ferracuti, Silvia, Ferretti, Alfonso, Pecoraro, Carmine, Gaido, Maurizio, Penza, Rosa, Edefonti, Alberto, Murer, Luisa, Tozzi, Alberto E., and Emma, Francesco

Published
2009

25. Unraveling the origin of azoospermia in male cystinosis patients

Author

Reda, Ahmed, Veys, Koenraad, Kadam, Prashant, Camps, Carlo, Taranta, Anna, Rega, Laura R, Cyr, Daniel G, Emma, Francesco, van den Heuvel, Lambert P., Goossens, Ellen, Elena, Levtchenko, Courcelles, Michel, and Oxford

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

Study question:Is azoospermia in male cystinosis patients obstructive or nonobstructive in origin?Summary answer: Azoospermia in male cystinosis patients is obstructive in origin.What is known already: Cystinosis is a rare autosomal recessive metabolic disorder caused by mutations in the lysosomal membrane protein cystinosin (CTNS), which leads to intracellular lysosomal cystine accumulation. Depending on the disease severity, three forms are distinguished: infantile (most severe), juvenile (intermediate), and ocular (benign) form. The main clinical presentation in infantile cystinosis is the renal Fanconi syndrome, leading to end stage renal disease (ESRD) by the age of ten, if the patient is left untreated. Cysteamine, a cystine-depleting agent, beside renal replacement therapy, has improved the life expectancy of cystinosis patients. In contrast to females, male infantile cystinosis patients suffer from infertility.Study design, size, duration: Three groups were included in a prospective case control study; adult cystinosis patients (three infantile, two juvenile, and one ocular male patients), control group (seven adult fertile male subjects), and a positive control group for obstructive azoospermia (ten adult vasectomized males who underwent vasectomy 4-8 weeks prior to enrollment). In addition, clinical data and testicular sections for five adult infantile male cystinosis patients were retrospectively included in the study (in total, eight infantile cystinosis patients).Participants/materials, setting,methods:Scrotal ultrasound for screening for soft biomarkers of obstruction and semen analysis were performed in all prospectively included subjects, while sexual hormonal levels were evaluated only in the cystinosis patients. In addition, clinical data, semen analysis results, percutaneous epididymal sperm aspiration (PESA) results, sexual hormonal profile, and testicular sections from the retrospectively included cystinosis patients were analyzed. For the testicular sections, morphological evaluation and immunohistochemistry were performed.Main results and the role of chance:All testicular sections taken from three infantile cystinosis patients (3/3) showed the presence of testicular sperm and normal spermatogenesis, with a Johnsen’s score of 7 to 9. Besides, epididymal sperm was present in two other infantile cystinosis patients (2/2), obtained by PESA procedure, which was only performed in those two patients. Hence, all of the five investigated infantile cystinosis patients showed either testicular or epididymal sperm (5/5 or 100%), indicating that testicular function was preserved in those patients. In contrast, seven out of the total eight infantile cystinosis patients underwent semen analysis, and they all presented with azoospermia (7/7 or 100%), including four out of the five patients that showed testicular or epididymal sperm, while a semen sample from one infantile patient, who underwent testicular biopsy, could not be retrieved. Meanwhile, the two juvenile cystinosis patients (2/2) showed a reduced sperm count (15.9 and 6.4 million/ml), and the ocular cystinosis patient (1/1) showed normal sperm count (71.6 million/ml). Remarkably, the scrotal ultrasound results revealed a significant higher epididymis caput diameter (normalized to the testis volume) in infantile cystinosis group compared with healthy controls (1.63±0.66 mm/cm3 for infantile cystinosis vs 0.50±0.18 mm/cm3 for controls, p

Published
2019

28. Activation of the transcription factor EB rescues lysosomal abnormalities in cystinotic kidney cells

Author

Rega, Laura R, Polishchuk, Elena, Montefusco, Sandro, Napolitano, Gennaro, Tozzi, Giulia, Zhang, Jinzhong, Bellomo, Francesco, Taranta, Anna, Pastore, Anna, Polishchuk, Roman, Piemonte, Fiorella, Medina, Diego L., Catz, Sergio D., Emma, Francesco, MEDINA SANABRIA, Diego Luis, BALLABIO, ANDREA, Rega, Laura R, Polishchuk, Elena, Montefusco, Sandro, Napolitano, Gennaro, Tozzi, Giulia, Zhang, Jinzhong, Bellomo, Francesco, Taranta, Anna, Pastore, Anna, Polishchuk, Roman, Piemonte, Fiorella, Medina, Diego L., Catz, Sergio D., Ballabio, Andrea, Emma, Francesco, and MEDINA SANABRIA, Diego Luis

Subjects
0301 basic medicine, medicine.medical_specialty, Cystinosis, Biology, Cell Line, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, cystinosi, pediatric nephrology, Nephropathic Cystinosis, renal pathology, Internal medicine, proximal tubule, Lysosomal storage disease, medicine, Humans, Cell Nucleus, Kidney, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Fanconi syndrome, medicine.disease, Amino Acid Transport Systems, Neutral, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, Cystinosin, chemistry, Nephrology, Cystine, TFEB, Cysteamine, Lysosomes, 030217 neurology & neurosurgery
Abstract

Nephropathic cystinosis is a rare autosomal recessive lysosomal storage disease characterized by accumulation of cystine into lysosomes secondary to mutations in the cystine lysosomal transporter, cystinosin. The defect initially causes proximal tubular dysfunction (Fanconi syndrome) which in time progresses to end-stage renal disease. Cystinotic patients treated with the cystine-depleting agent, cysteamine, have improved life expectancy, delayed progression to chronic renal failure, but persistence of Fanconi syndrome. Here, we have investigated the role of the transcription factor EB (TFEB), a master regulator of the autophagy-lysosomal pathway, in conditionally immortalized proximal tubular epithelial cells derived from the urine of a healthy volunteer or a cystinotic patient. Lack of cystinosin reduced TFEB expression and induced TFEB nuclear translocation. Stimulation of endogenous TFEB activity by genistein, or overexpression of exogenous TFEB lowered cystine levels within 24 hours in cystinotic cells. Overexpression of TFEB also stimulated delayed endocytic cargo processing within 24 hours. Rescue of other abnormalities of the lysosomal compartment was observed but required prolonged expression of TFEB. These abnormalities could not be corrected with cysteamine. Thus, these data show that the consequences of cystinosin deficiency are not restricted to cystine accumulation and support the role of TFEB as a therapeutic target for the treatment of lysosomal storage diseases, in particular of cystinosis.

Published
2016

32. Activation of the transcription factor EB rescues lysosomal abnormalities in cystinotic kidney cells

Author

Rega, Laura R., primary, Polishchuk, Elena, additional, Montefusco, Sandro, additional, Napolitano, Gennaro, additional, Tozzi, Giulia, additional, Zhang, Jinzhong, additional, Bellomo, Francesco, additional, Taranta, Anna, additional, Pastore, Anna, additional, Polishchuk, Roman, additional, Piemonte, Fiorella, additional, Medina, Diego L., additional, Catz, Sergio D., additional, Ballabio, Andrea, additional, and Emma, Francesco, additional

Published
2016
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33. Cysteamine treatment restores the in vitro ability to differentiate along the osteoblastic lineage of mesenchymal stromal cells isolated from bone marrow of a cystinotic patient

Author

Conforti, Antonella, primary, Taranta, Anna, additional, Biagini, Simone, additional, Starc, Nadia, additional, Pitisci, Angela, additional, Bellomo, Francesco, additional, Cirillo, Valentina, additional, Locatelli, Franco, additional, Bernardo, Maria Ester, additional, and Emma, Francesco, additional

Published
2015
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34. Gender-related effects on urine l-cystine metastability

Author

Masotti, Andrea, primary, Laurenzi, Chiara, additional, Boenzi, Sara, additional, Pastore, Anna, additional, Taranta, Anna, additional, Bellomo, Francesco, additional, Muraca, Maurizio, additional, Dionisi-Vici, Carlo, additional, Bertucci, Pierfrancesco, additional, Strologo, Luca Dello, additional, and Emma, Francesco, additional

Published
2013
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35. Polymorphisms of the CLCN7 gene are associated with BMD in women.

Author

Pettersson, Ulrika, Albagha, Omar M E, Mirolo, Max, Taranta, Anna, Frattini, Annalisa, McGuigan, Fiona E A, Vezzoni, Paolo, Teti, Anna, van Hul, Wim, Reid, David M, Villa, Anna, Ralston, Stuart H, Pettersson, Ulrika, Albagha, Omar M E, Mirolo, Max, Taranta, Anna, Frattini, Annalisa, McGuigan, Fiona E A, Vezzoni, Paolo, Teti, Anna, van Hul, Wim, Reid, David M, Villa, Anna, and Ralston, Stuart H

Abstract

UNLABELLED: Here we show that a common polymorphism causing a valine to methionine amino acid substitution at codon 418 (V418M) in the CLCN7 gene is associated with femoral neck BMD in women. Our study adds to accumulating evidence that shows that common allelic variants in monogenic bone disease genes often contribute to BMD regulation in normal subjects. INTRODUCTION: The CLCN7 gene is a strong candidate for regulation of BMD, because mutations in CLCN7 cause some forms of osteopetrosis, a disease characterized by impaired osteoclast function and increased BMD. In this study, we sought to determine whether common allelic variation within CLCN7 was associated with BMD in the normal population. MATERIALS AND METHODS: We conducted mutation screening of the exons and intron-exon boundaries in CLCN7 by DNA sequencing in 50 normal subjects. We conducted an association study between common polymorphisms in CLCN7 and haplotypes defined by these polymorphisms and BMD values at the lumbar spine and femoral neck in a population-based cohort study of 1077 Scottish women 45-55 years of age. RESULTS: We identified 24 polymorphisms, but most were rare and only 4 had allele frequencies of >5%. These were a conservative single nucleotide polymorphism (SNP) in exon 1 (rs3751884), a 50-bp tandem repeat polymorphism within intron 8, and two SNPs within exon 15 (rs12926089 and rs12926669), of which one (rs12926669) predicts an amino acid change from valine to methionine at codon 418 (V418M). The exon 15 SNPs were in strong linkage disequilibrium and were both associated with femoral neck BMD (p = 0.001-0.003). None of the other polymorphisms were associated with BMD, and long-range haplotypes showed a much weaker association with BMD than the exon 15 SNPs. The V418M polymorphism was an independent predictor of femoral neck BMD on multiple regression analysis accounting for 1% of the variance in BMD at this site. CONCLUSIONS: Our study indicates that the V418M polymorphism of CLCN7

Published
2005
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36. Stem Cell Microvesicles Transfer Cystinosin to Human Cystinotic Cells and Reduce Cystine Accumulation In Vitro

Author

Iglesias, Diana M., primary, El-Kares, Reyhan, additional, Taranta, Anna, additional, Bellomo, Francesco, additional, Emma, Francesco, additional, Besouw, Martine, additional, Levtchenko, Elena, additional, Toelen, Jaan, additional, van den Heuvel, Lambertus, additional, Chu, LeeLee, additional, Zhao, Jing, additional, Young, Yoon Kow, additional, Eliopoulos, Nicoletta, additional, and Goodyer, Paul, additional

Published
2012
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39. Cystinosin-LKG rescues cystine accumulation and decreases apoptosis rate in cystinotic proximal tubular epithelial cells

Author

Taranta, Anna, Bellomo, Francesco, Petrini, Stefania, Polishchuk, Elena, De Leo, Ester, Rega, Laura Rita, Pastore, Anna, Polishchuk, Roman, De Matteis, Maria Antonietta, and Emma, Francesco

Abstract

Background:Nephropathic cystinosis is a lysosomal storage disease that is caused by mutations in the CTNS gene encoding a cystine/proton symporter cystinosin and an isoform cystinosin-LKG which is generated by an alternative splicing of exon 12. We have investigated the physiological role of the cystinosin-LKG that is widely expressed in epithelial tissues.Methods:We have analyzed the intracellular localization and the function of the cystinosin-LKG conjugated with DsRed (cystinosin-LKG-RFP) in Madin-Darby canine kidney cells (MDCK II) and in proximal tubular epithelial cells carrying a deletion of the CTNS gene (cystinotic PTEC), respectively.Results:Cystinosin-LKG-RFP colocalized with markers of lysosomes, late endosomes and was also expressed on the apical surface of polarized MDCK II cells. Moreover, immune-electron microscopy images of MDCK II cells overexpressing cystinosin-LKG-RFP showed stacked lamellar membranes inside perinuclear lysosomal structures. To study the role of LKG-isoform, we have investigated cystine accumulation and apoptosis that have been described in cystinotic cells. Cystinosin-LKG decreased cystine levels by approximately 10-fold similarly to cystinosin-RFP. The levels of TNFα- and actinomycin D-inducted apoptosis dropped in cystinotic cells expressing LKG-isoform. This effect was also similar to the main isoform.Conclusion:Our results suggest that cystinosin-LKG and cystinosin move similar functional activities in cells.

Published
2017
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41. Polymorphisms of the CLCN7 Gene Are Associated With BMD in Women

Author

Pettersson, Ulrika, primary, Albagha, Omar ME, additional, Mirolo, Max, additional, Taranta, Anna, additional, Frattini, Annalisa, additional, McGuigan, Fiona EA, additional, Vezzoni, Paolo, additional, Teti, Anna, additional, Van Hul, Wim, additional, Reid, David M, additional, Villa, Anna, additional, and Ralston, Stuart H, additional

Published
2005
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42. Imbalance of Osteoclastogenesis‐Regulating Factors in Patients With Celiac Disease

Author

Taranta, Anna, primary, Fortunati, Dario, additional, Longo, Maurizio, additional, Rucci, Nadia, additional, Iacomino, Enzo, additional, Aliberti, Ferdinando, additional, Facciuto, Enzo, additional, Migliaccio, Silvia, additional, Bardella, Maria Teresa, additional, Dubini, Antonella, additional, Borghi, Maria Orietta, additional, Saraifoger, Silvia, additional, Teti, Anna, additional, and Bianchi, Maria Luisa, additional

Published
2004
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43. TCIRG1-dependent recessive osteopetrosis: Mutation analysis, functional identification of the splicing defects, andin vitro rescue by U1 snRNA

Author

Susani, Lucia, primary, Pangrazio, Alessandra, additional, Sobacchi, Cristina, additional, Taranta, Anna, additional, Mortier, Geert, additional, Savarirayan, Ravi, additional, Villa, Anna, additional, Orchard, Paul, additional, Vezzoni, Paolo, additional, Albertini, Alberto, additional, Frattini, Annalisa, additional, and Pagani, Franco, additional

Published
2004
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44. Reduction of c-Src activity by substituted 5,7-diphenyl-pyrrolo[2,3-d]-pyrimidines induces osteoclast apoptosis in vivo and in vitro. Involvement of ERK1/2 pathway

Author

Recchia, Irene, primary, Rucci, Nadia, additional, Funari, Alessia, additional, Migliaccio, Silvia, additional, Taranta, Anna, additional, Longo, Maurizio, additional, Kneissel, Michaela, additional, Šuša, Mira, additional, Fabbro, Doriano, additional, and Teti, Anna, additional

Published
2004
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46. Genotype-Phenotype Relationship in Human ATP6i-Dependent Autosomal Recessive Osteopetrosis

Author

Taranta, Anna, primary, Migliaccio, Silvia, additional, Recchia, Irene, additional, Caniglia, Maurizio, additional, Luciani, Matteo, additional, De Rossi, Giulio, additional, Dionisi-Vici, Carlo, additional, Pinto, Rita M., additional, Francalanci, Paola, additional, Boldrini, Renata, additional, Lanino, Edoardo, additional, Dini, Giorgio, additional, Morreale, Giuseppe, additional, Ralston, Stuart H., additional, Villa, Anna, additional, Vezzoni, Paolo, additional, Del Principe, Domenico, additional, Cassiani, Flaminia, additional, Palumbo, Giuseppe, additional, and Teti, Anna, additional

Published
2003
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50. Mechanisms of Osteoclast Dysfunction in Human Osteopetrosis: Abnormal Osteoclastogenesis and Lack of Osteoclast-Specific Adhesion Structures

Author

Teti, Anna, primary, Migliaccio, Silvia, additional, Taranta, Anna, additional, Bernardini, Silvia, additional, De Rossi, Giulio, additional, Luciani, Matteo, additional, Iacobini, Metello, additional, De Felice, Lidia, additional, Boldrini, Renata, additional, Bosman, Cesare, additional, Corsi, Alessandro, additional, and Bianco, Paolo, additional

Published
1999
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