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1. Dysfunctional LAT2 Amino Acid Transporter Is Associated With Cataract in Mouse and Humans

Author

Knöpfel, Emilia Boiadjieva, Vilches, Clara, Camargo, Simone MR, Errasti-Murugarren, Ekaitz, Stäubli, Andrina, Mayayo, Clara, Munier, Francis L, Miroshnikova, Nataliya, Poncet, Nadège, Junza, Alexandra, Bhattacharya, Shomi S, Prat, Esther, Berry, Vanita, Berger, Wolfgang, Heon, Elise, Moore, Anthony T, Yanes, Óscar, Nunes, Virginia, Palacín, Manuel, Verrey, Francois, and Kloeckener-Gruissem, Barbara

Subjects
Biomedical and Clinical Sciences, Ophthalmology and Optometry, Eye Disease and Disorders of Vision, Aging, Congenital Structural Anomalies, Pediatric, Genetics, 2.1 Biological and endogenous factors, Aetiology, amino acid transporters LAT2 and TAT1, gene expression, cataract, ocular tissues, mouse model, patient screen, Physiology, Medical Physiology, Psychology, Biochemistry and cell biology, Medical physiology
Abstract

Cataract, the loss of ocular lens transparency, accounts for ∼50% of worldwide blindness and has been associated with water and solute transport dysfunction across lens cellular barriers. We show that neutral amino acid antiporter LAT2 (Slc7a8) and uniporter TAT1 (Slc16a10) are expressed on mouse ciliary epithelium and LAT2 also in lens epithelium. Correspondingly, deletion of LAT2 induced a dramatic decrease in lens essential amino acid levels that was modulated by TAT1 defect. Interestingly, the absence of LAT2 led to increased incidence of cataract in mice, in particular in older females, and a synergistic effect was observed with simultaneous lack of TAT1. Screening SLC7A8 in patients diagnosed with congenital or age-related cataract yielded one homozygous single nucleotide deletion segregating in a family with congenital cataract. Expressed in HeLa cells, this LAT2 mutation did not support amino acid uptake. Heterozygous LAT2 variants were also found in patients with cataract some of which showed a reduced transport function when expressed in HeLa cells. Whether heterozygous LAT2 variants may contribute to the pathology of cataract needs to be further investigated. Overall, our results suggest that defects of amino acid transporter LAT2 are implicated in cataract formation, a situation that may be aggravated by TAT1 defects.

Published
2019

2. Dysfunctional LAT2 Amino Acid Transporter Is Associated With Cataract in Mouse and Humans

Author

Knöpfel, Emilia Boiadjieva, primary, Vilches, Clara, additional, Camargo, Simone M. R., additional, Errasti-Murugarren, Ekaitz, additional, Stäubli, Andrina, additional, Mayayo, Clara, additional, Munier, Francis L., additional, Miroshnikova, Nataliya, additional, Poncet, Nadège, additional, Junza, Alexandra, additional, Bhattacharya, Shomi S., additional, Prat, Esther, additional, Berry, Vanita, additional, Berger, Wolfgang, additional, Heon, Elise, additional, Moore, Anthony T., additional, Yanes, Óscar, additional, Nunes, Virginia, additional, Palacín, Manuel, additional, Verrey, Francois, additional, and Kloeckener-Gruissem, Barbara, additional

Published
2019
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3. Dysfunctional LAT2 Amino Acid Transporter Is Associated With Cataract in Mouse and Humans

Author

Boiadjieva Knöpfel, Emilia, Vilches, Clara, Camargo, Simone M R, Errasti-Murugarren, Ekaitz, Stäubli, Andrina, Mayayo, Clara, Munier, Francis L, Miroshnikova, Nataliya, Poncet, Nadège, Junza, Alexandra, Bhattacharya, Shomi S, Prat, Esther, Berry, Vanita, Berger, Wolfgang, Heon, Elise, Moore, Anthony T, Yanes, Óscar, Nunes, Virginia, Palacín, Manuel, Verrey, Francois, Kloeckener-Gruissem, Barbara, Boiadjieva Knöpfel, Emilia, Vilches, Clara, Camargo, Simone M R, Errasti-Murugarren, Ekaitz, Stäubli, Andrina, Mayayo, Clara, Munier, Francis L, Miroshnikova, Nataliya, Poncet, Nadège, Junza, Alexandra, Bhattacharya, Shomi S, Prat, Esther, Berry, Vanita, Berger, Wolfgang, Heon, Elise, Moore, Anthony T, Yanes, Óscar, Nunes, Virginia, Palacín, Manuel, Verrey, Francois, and Kloeckener-Gruissem, Barbara

Abstract

Cataract, the loss of ocular lens transparency, accounts for ∼50% of worldwide blindness and has been associated with water and solute transport dysfunction across lens cellular barriers. We show that neutral amino acid antiporter LAT2 ) and uniporter TAT1 () are expressed on mouse ciliary epithelium and LAT2 also in lens epithelium. Correspondingly, deletion of LAT2 induced a dramatic decrease in lens essential amino acid levels that was modulated by TAT1 defect. Interestingly, the absence of LAT2 led to increased incidence of cataract in mice, in particular in older females, and a synergistic effect was observed with simultaneous lack of TAT1. Screening in patients diagnosed with congenital or age-related cataract yielded one homozygous single nucleotide deletion segregating in a family with congenital cataract. Expressed in HeLa cells, this LAT2 mutation did not support amino acid uptake. Heterozygous LAT2 variants were also found in patients with cataract some of which showed a reduced transport function when expressed in HeLa cells. Whether heterozygous LAT2 variants may contribute to the pathology of cataract needs to be further investigated. Overall, our results suggest that defects of amino acid transporter LAT2 are implicated in cataract formation, a situation that may be aggravated by TAT1 defects.

Published
2019

4. Dysfunctional LAT2 amino acid transporter is associated with cataract in mouse and humans

Author

Hartmann Müller Foundation for Medical Research, Novartis Foundation for Sustainable Development, Swiss National Science Foundation, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), European Commission, Instituto de Salud Carlos III, Generalitat de Catalunya, Centro de Investigación Biomédica en Red Enfermedades Raras (España), Wellcome Trust, National Institute for Health Research (UK), Knöpfel, Emilia Boiadjieva, Vilches, Clara, Camargo, Simone M. R., Errasti-Murugarren, Ekaitz, Stäubli, Andrina, Mayayo, Clara, Munier, Francis L., Miroshnikova, Nataliya, Poncet, Nadège, Junza, Alexandra, Bhattacharya, Shom Shanker, Prat, Esther, Berry, Vanita, Berger, Wolfgang, Heon, Elise, Moore, Anthony T., Yanes, Óscar, Nunes, Virginia, Palacín, Manuel, Verrey, Francois, Kloeckener-Gruissem, Barbara, Hartmann Müller Foundation for Medical Research, Novartis Foundation for Sustainable Development, Swiss National Science Foundation, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), European Commission, Instituto de Salud Carlos III, Generalitat de Catalunya, Centro de Investigación Biomédica en Red Enfermedades Raras (España), Wellcome Trust, National Institute for Health Research (UK), Knöpfel, Emilia Boiadjieva, Vilches, Clara, Camargo, Simone M. R., Errasti-Murugarren, Ekaitz, Stäubli, Andrina, Mayayo, Clara, Munier, Francis L., Miroshnikova, Nataliya, Poncet, Nadège, Junza, Alexandra, Bhattacharya, Shom Shanker, Prat, Esther, Berry, Vanita, Berger, Wolfgang, Heon, Elise, Moore, Anthony T., Yanes, Óscar, Nunes, Virginia, Palacín, Manuel, Verrey, Francois, and Kloeckener-Gruissem, Barbara

Abstract

Cataract, the loss of ocular lens transparency, accounts for ~50% of worldwide blindness and has been associated with water and solute transport dysfunction across lens cellular barriers. We show that neutral amino acid antiporter LAT2 (Slc7a8) and uniporter TAT1 (Slc16a10) are expressed on mouse ciliary epithelium and LAT2 also in lens epithelium. Correspondingly, deletion of LAT2 induced a dramatic decrease in lens essential amino acid levels that was modulated by TAT1 defect. Interestingly, the absence of LAT2 led to increased incidence of cataract in mice, in particular in older females, and a synergistic effect was observed with simultaneous lack of TAT1. Screening SLC7A8 in patients diagnosed with congenital or age-related cataract yielded one homozygous single nucleotide deletion segregating in a family with congenital cataract. Expressed in HeLa cells, this LAT2 mutation did not support amino acid uptake. Heterozygous LAT2 variants were also found in patients with cataract some of which showed a reduced transport function when expressed in HeLa cells. Whether heterozygous LAT2 variants may contribute to the pathology of cataract needs to be further investigated. Overall, our results suggest that defects of amino acid transporter LAT2 are implicated in cataract formation, a situation that may be aggravated by TAT1 defects.

Published
2019

5. El proceso de sucesión en la empresa familiar

Author

Berdié Mayayo, Clara, Universitat Abat Oliba CEU. Departament de Ciències Econòmiques i Socials, and Corona Ramón, Juan Francisco

Subjects
65 - Gestió i organització. Administració i direcció d'empreses. Publicitat. Relacions públiques. Mitjans de comunicació de masses, Empreses familiars, Dret de successió
Abstract

La majoria dels experts coincideixen en definir l’empresa familiar com l’empresa a la que el capital, la gestió y el govern estan en mans de una o mes famílies que exerceixen control sobre ella. El punt mes important que diferencia l’empresa familiar de la no familiar es el propòsit de la continuïtat, que es dona en a les empreses familiars, a través de l’entrada de les successives generacions. Aquesta continuïtat es materialitza amb l’èxit del procés successori que dona lloc a la nova generació. La complexitat d’aquest tipus d’empreses deriva de la unió de les dos entitats que la formen, empresa i família. Aquesta unió suposa la combinació d’assumptes purament empresarials amb altres de caràcter més personal. La unió de tots dos interessos dins de l’empresa suposa una important font de conflictes i problemes per a l’organització. A mesura que la família es fa més gran els problemes també creixen, i les relacions entre la família i la empresa es fan més difícils i complicades. Es per això que l’empresa ha d’actuar amb temps i avançar-se a les futures dificultats que puguin presentar-se a l’organització, tractant d’evitar-les, fent servir les eines de que disposa. Per assegurar el èxit del procés successori i evitar futurs problemes interns, l’empresa, i sobretot el predecessor, han de manejar i definir de forma correcta el marc legal i el marc familiar que emmarquen les seves relacions. En primer lloc, el marc legal ha d’assegurar la bona comunicació entre la família i l’empresa, per així, evitar futurs malentesos. A través d’òrgans com el Consell d’Administració i la Junta General d’Accionistes l’empresa reforça aspectes com la unitat i el compromís, que son tan necessaris en moments de canvi generacional. Per una altra banda, el marc familiar ha de vetllar pel manteniment dels valors propis de la família que el predecessor ha inculcat al llarg dels anys, i que han servit de guia tant a l’empresa com a la família. El marc familiar el defineixen eines com el Protocol Familiar, que regula i gestiona les relacions entre la família, l’empresa i els propietaris de la organització. El òrgan encarregat de controlar el compliment d’allò pactat en el Protocol i d’encarregar-se del bon funcionament del marc familiar es el Consell de Família.

Published
2011

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