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  1. Article ; Online: Pediatric cataracts of different etiologies contain insoluble, calcified particles.

    Minogue, Peter J / Rodriguez, Sarah H / Berthoud, Viviana M / Beyer, Eric C

    Frontiers in ophthalmology

    2023  Volume 3

    Abstract: Our recent studies in mice suggest that a crucial event for the development of cataracts is the formation of calcium-containing deposits. To examine the generality of pathologic mineralization as a novel mechanism of cataract formation, we analyzed lens ... ...

    Abstract Our recent studies in mice suggest that a crucial event for the development of cataracts is the formation of calcium-containing deposits. To examine the generality of pathologic mineralization as a novel mechanism of cataract formation, we analyzed lens material from different human cataract surgeries. Human lens material was obtained from routine cataract surgeries performed on three patients with dense, white cataracts: a 10-month-old with congenital cataracts, a 9-year-old with a uveitic cataract, and a 17-year-old with a traumatic cataract. The aspirated material from the cataract surgeries contained insoluble material that could be isolated by centrifugation. Many particles within the insoluble fraction stained with Alizarin red, a dye that stains insoluble calcified material. The appearance of these human insoluble, Alizarin red-stained particles was similar to some of those detected in homogenates from cataractous mouse lenses. These results support the hypothesis that pathologic mineralization may have a mechanistic role in the formation of cataracts of different etiologies.
    Language English
    Publishing date 2023-07-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 3123828-2
    ISSN 2674-0826 ; 2674-0826
    ISSN (online) 2674-0826
    ISSN 2674-0826
    DOI 10.3389/fopht.2023.1213359
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Editorial: Ion channels, pumps, and transporters in lens physiology and disease.

    Beyer, Eric C / Berthoud, Viviana M / Lim, Julie C / Donaldson, Paul J

    Frontiers in physiology

    2022  Volume 13, Page(s) 1071215

    Language English
    Publishing date 2022-11-03
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.1071215
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  3. Article: Loss of fiber cell communication may contribute to the development of cataracts of many different etiologies.

    Beyer, Eric C / Mathias, Richard T / Berthoud, Viviana M

    Frontiers in physiology

    2022  Volume 13, Page(s) 989524

    Abstract: The lens is an avascular organ that is supported by an internal circulation of water and solutes. This circulation is driven by ion pumps, channels and transporters in epithelial cells and by ion channels in fiber cells and is maintained by fiber-fiber ... ...

    Abstract The lens is an avascular organ that is supported by an internal circulation of water and solutes. This circulation is driven by ion pumps, channels and transporters in epithelial cells and by ion channels in fiber cells and is maintained by fiber-fiber and fiber-epithelial cell communication. Gap junctional intercellular channels formed of connexin46 and connexin50 are critical components of this circulation as demonstrated by studies of connexin null mice and connexin mutant mice. Moreover, connexin mutants are one of the most common causes of autosomal dominant congenital cataracts. However, alterations of the lens circulation and coupling between lens fiber cells are much more prevalent, beyond the connexin mutant lenses. Intercellular coupling and levels of connexins are decreased with aging. Gap junction-mediated intercellular communication decreases in mice expressing mutant forms of several different lens proteins and in some mouse models of lens protein damage. These observations suggest that disruption of ionic homeostasis due to reduction of the lens circulation is a common component of the development of many different types of cataracts. The decrease in the lens circulation often reflects low levels of lens fiber cell connexins and/or functional gap junction channels.
    Language English
    Publishing date 2022-09-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.989524
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Levels and Modifications of Both Lens Fiber Cell Connexins Are Affected in Connexin Mutant Mice.

    Jara, Oscar / Minogue, Peter J / Berthoud, Viviana M / Beyer, Eric C

    Cells

    2022  Volume 11, Issue 18

    Abstract: In the lens, cell homeostasis and transparency are supported by intercellular communication facilitated by the channels formed of connexin46 (Cx46) and connexin50 (Cx50). Mutations of these connexins are linked to inherited cataracts. We studied the ... ...

    Abstract In the lens, cell homeostasis and transparency are supported by intercellular communication facilitated by the channels formed of connexin46 (Cx46) and connexin50 (Cx50). Mutations of these connexins are linked to inherited cataracts. We studied the levels and the variations in electrophoretic mobilities of the immunoreactive Cx46 and Cx50 bands between 1 and 21 days after birth in the lenses of wild-type mice and homozygous animals from two different mouse models of connexin-linked cataracts (Cx46fs380 and Cx50D47A). In Cx50D47A mice, the expression of the mutant Cx50 reduced the normal phosphorylation of the co-expressed wild-type Cx46. In both models, levels of the mutant connexin and the co-expressed wild-type connexin decayed more rapidly than in wild-type mice but with different time courses. In the Cx46fs380 mice, modeling suggested that Cx50 degradation could be explained by the mixing of mutant Cx46 with wild-type Cx50. However, in Cx50D47A mice, similar modeling suggested that mixing alone could not explain the decrease in Cx46 levels. These data highlight the complex influences between two connexin proteins expressed in the same cell, some of which occur through direct mixing, while others occur indirectly, as in Cx50D47A mice, where the expression of the mutant connexin causes endoplasmic reticulum stress and impaired differentiation.
    MeSH term(s) Animals ; Cataract/genetics ; Cataract/metabolism ; Connexins/genetics ; Connexins/metabolism ; Epithelial Cells/metabolism ; Gap Junctions/metabolism ; Lens, Crystalline/metabolism ; Mice
    Chemical Substances Connexins ; connexin 50
    Language English
    Publishing date 2022-09-07
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells11182786
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  5. Article ; Online: Remembrances of Dr. Michael V.L. Bennett by Iberoamerican Colleagues and Friends.

    Abudara, Verónica / Araneda, Ricardo C / Barrio, Luis / Berthoud, Viviana M / Contreras, Jorge E / Eugenín, Eliseo / Lerma, Juan / Orellana, Juan A / Palacios-Prado, Nicolás / Pérez-Armendariz, Elia Martha / Retamal, Mauricio A / Sáez, Juan C

    Neuroscience

    2024  

    Language English
    Publishing date 2024-01-23
    Publishing country United States
    Document type Journal Article
    ZDB-ID 196739-3
    ISSN 1873-7544 ; 0306-4522
    ISSN (online) 1873-7544
    ISSN 0306-4522
    DOI 10.1016/j.neuroscience.2024.01.011
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    In stock of ZB MED Cologne/Königswinter

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  6. Article ; Online: Pediatric cataracts of different etiologies contain insoluble, calcified particles

    Peter J. Minogue / Sarah H. Rodriguez / Viviana M. Berthoud / Eric C. Beyer

    Frontiers in Ophthalmology, Vol

    2023  Volume 3

    Abstract: Our recent studies in mice suggest that a crucial event for the development of cataracts is the formation of calcium-containing deposits. To examine the generality of pathologic mineralization as a novel mechanism of cataract formation, we analyzed lens ... ...

    Abstract Our recent studies in mice suggest that a crucial event for the development of cataracts is the formation of calcium-containing deposits. To examine the generality of pathologic mineralization as a novel mechanism of cataract formation, we analyzed lens material from different human cataract surgeries. Human lens material was obtained from routine cataract surgeries performed on three patients with dense, white cataracts: a 10-month-old with congenital cataracts, a 9-year-old with a uveitic cataract, and a 17-year-old with a traumatic cataract. The aspirated material from the cataract surgeries contained insoluble material that could be isolated by centrifugation. Many particles within the insoluble fraction stained with Alizarin red, a dye that stains insoluble calcified material. The appearance of these human insoluble, Alizarin red-stained particles was similar to some of those detected in homogenates from cataractous mouse lenses. These results support the hypothesis that pathologic mineralization may have a mechanistic role in the formation of cataracts of different etiologies.
    Keywords cataract ; calcium precipitation ; biomineralization ; lens ; pediatric ; Medicine ; R
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: A crystallin mutant cataract with mineral deposits.

    Minogue, Peter J / Gao, Junyuan / Mathias, Richard T / Williams, James C / Bledsoe, Sharon B / Sommer, Andre J / Beyer, Eric C / Berthoud, Viviana M

    The Journal of biological chemistry

    2023  Volume 299, Issue 8, Page(s) 104935

    Abstract: Connexin mutant mice develop cataracts containing calcium precipitates. To test whether pathologic mineralization is a general mechanism contributing to the disease, we characterized the lenses from a nonconnexin mutant mouse cataract model. By ... ...

    Abstract Connexin mutant mice develop cataracts containing calcium precipitates. To test whether pathologic mineralization is a general mechanism contributing to the disease, we characterized the lenses from a nonconnexin mutant mouse cataract model. By cosegregation of the phenotype with a satellite marker and genomic sequencing, we identified the mutant as a 5-bp duplication in the γC-crystallin gene (Crygc
    MeSH term(s) Animals ; Mice ; Calcium/metabolism ; Cataract/genetics ; Cataract/physiopathology ; Connexins/genetics ; Connexins/metabolism ; Crystallins/genetics ; Crystallins/metabolism ; Lens, Crystalline/pathology ; Minerals/metabolism ; X-Ray Microtomography ; Disease Models, Animal
    Chemical Substances alizarin (60MEW57T9G) ; Calcium (SY7Q814VUP) ; Connexins ; Crystallins ; Minerals
    Language English
    Publishing date 2023-06-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.104935
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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  8. Article: Gap junction structure: unraveled, but not fully revealed.

    Beyer, Eric C / Berthoud, Viviana M

    F1000Research

    2017  Volume 6, Page(s) 568

    Abstract: Gap junction channels facilitate the intercellular exchange of ions and small molecules, a process that is critical for the function of many different kinds of cells and tissues. Recent crystal structures of channels formed by one connexin isoform ( ... ...

    Abstract Gap junction channels facilitate the intercellular exchange of ions and small molecules, a process that is critical for the function of many different kinds of cells and tissues. Recent crystal structures of channels formed by one connexin isoform (connexin26) have been determined, and they have been subjected to molecular modeling. These studies have provided high-resolution models to gain insights into the mechanisms of channel conductance, molecular permeability, and gating. The models share similarities, but there are some differences in the conclusions reached by these studies. Many unanswered questions remain to allow an atomic-level understanding of intercellular communication mediated by connexin26. Because some domains of the connexin polypeptides are highly conserved (like the transmembrane regions), it is likely that some features of the connexin26 structure will apply to other members of the family of gap junction proteins. However, determination of high-resolution structures and modeling of other connexin channels will be required to account for the diverse biophysical properties and regulation conferred by the differences in their sequences.
    Language English
    Publishing date 2017
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2699932-8
    ISSN 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.10490.1
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  9. Article ; Online: Focus on lens connexins.

    Berthoud, Viviana M / Ngezahayo, Anaclet

    BMC cell biology

    2017  Volume 18, Issue Suppl 1, Page(s) 6

    Abstract: The lens is an avascular organ composed of an anterior epithelial cell layer and fiber cells that form the bulk of the organ. The lens expresses connexin43 (Cx43), connexin46 (Cx46) and connexin50 (Cx50). Epithelial Cx50 has critical roles in cell ... ...

    Abstract The lens is an avascular organ composed of an anterior epithelial cell layer and fiber cells that form the bulk of the organ. The lens expresses connexin43 (Cx43), connexin46 (Cx46) and connexin50 (Cx50). Epithelial Cx50 has critical roles in cell proliferation and differentiation, likely involving growth factor-dependent signaling pathways. Both Cx46 and Cx50 are crucial for lens transparency; mutations in their genes have been linked to congenital and age-related cataracts. Congenital cataract-associated connexin mutants can affect protein trafficking, stability and/or function, and the functional effects may differ between gap junction channels and hemichannels. Dominantly inherited cataracts may result from effects of the connexin mutant on its wild type isotype, the other co-expressed wild type connexin and/or its interaction with other cellular components.
    MeSH term(s) Animals ; Cataract/genetics ; Cataract/metabolism ; Cataract/pathology ; Connexins/chemistry ; Connexins/genetics ; Connexins/metabolism ; Humans ; Intercellular Signaling Peptides and Proteins/metabolism ; Lens, Crystalline/metabolism ; Mutation/genetics ; Signal Transduction
    Chemical Substances Connexins ; Intercellular Signaling Peptides and Proteins
    Language English
    Publishing date 2017-01-17
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1471-2121
    ISSN (online) 1471-2121
    DOI 10.1186/s12860-016-0116-6
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  10. Article: Gap junction gene and protein families: Connexins, innexins, and pannexins.

    Beyer, Eric C / Berthoud, Viviana M

    Biochimica et biophysica acta. Biomembranes

    2017  Volume 1860, Issue 1, Page(s) 5–8

    Abstract: Gap junction channels facilitate the intercellular exchange of ions and small molecules. While this process is critical to all multicellular organisms, the proteins that form gap junction channels are not conserved. Vertebrate gap junctions are formed by ...

    Abstract Gap junction channels facilitate the intercellular exchange of ions and small molecules. While this process is critical to all multicellular organisms, the proteins that form gap junction channels are not conserved. Vertebrate gap junctions are formed by connexins, while invertebrate gap junctions are formed by innexins. Interestingly, vertebrates and lower chordates contain innexin homologs, the pannexins, which also form channels, but rarely (if ever) make intercellular channels. While the connexin and the innexin/pannexin polypeptides do not share significant sequence similarity, all three of these protein families share a similar membrane topology and some similarities in quaternary structure. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.
    MeSH term(s) Animals ; Connexins/genetics ; Connexins/metabolism ; Gap Junctions/genetics ; Gap Junctions/metabolism ; Humans ; Ion Transport/physiology
    Chemical Substances Connexins
    Language English
    Publishing date 2017-05-27
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2736 ; 0006-3002 ; 0005-2728 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0005-2736 ; 0006-3002 ; 0005-2728 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2017.05.016
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