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dc.contributor.author
Chanson, Marc
dc.contributor.author
Kotsias, Basilio Aristides
dc.contributor.author
Peracchia, Camillo
dc.contributor.author
O’Grady, Scott M.
dc.date.available
2020-05-22T20:36:23Z
dc.date.issued
2007-05
dc.identifier.citation
Chanson, Marc; Kotsias, Basilio Aristides; Peracchia, Camillo; O’Grady, Scott M.; Interactions of connexins with other membrane channels and transporters; Pergamon-Elsevier Science Ltd; Progress In Biophysics And Molecular Biology; 94; 1-2; 5-2007; 233-244
dc.identifier.issn
0079-6107
dc.identifier.uri
http://hdl.handle.net/11336/105827
dc.description.abstract
Cell-to-cell communication through gap junctions exists in most animal cells and is essential for many important biological processes including rapid transmission of electric signals to coordinate contraction of cardiac and smooth muscle, the intercellular propagation of Ca2+ waves and synchronization of physiological processes between adjacent cells within a tissue. Recent studies have shown that connexins (Cx) can have either direct or indirect interactions with other plasma membrane ion channels or membrane transport proteins with important functional consequences. For example, in tissues most severely affected by cystic fibrosis (CF), activation of the CF Transmembrane Conductance Regulator (CFTR) has been shown to influence connexin function. Moreover, a direct interaction between Cx45.6 and the Major Intrinsic Protein/AQP0 in lens appears to influence the process of cell differentiation whereas interactions between aquaporin 4 (AQP4) and Cx43 in mouse astrocytes may coordinate the intercellular movement of ions and water between astrocytes. In this review, we discuss evidence supporting interactions between Cx and membrane channels/transporters including CFTR, aquaporins, ionotropic glutamate receptors, and between pannexin1, another class of putative gapjunction- forming proteins, and Kvb3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. within a tissue. Recent studies have shown that connexins (Cx) can have either direct or indirect interactions with other plasma membrane ion channels or membrane transport proteins with important functional consequences. For example, in tissues most severely affected by cystic fibrosis (CF), activation of the CF Transmembrane Conductance Regulator (CFTR) has been shown to influence connexin function. Moreover, a direct interaction between Cx45.6 and the Major Intrinsic Protein/AQP0 in lens appears to influence the process of cell differentiation whereas interactions between aquaporin 4 (AQP4) and Cx43 in mouse astrocytes may coordinate the intercellular movement of ions and water between astrocytes. In this review, we discuss evidence supporting interactions between Cx and membrane channels/transporters including CFTR, aquaporins, ionotropic glutamate receptors, and between pannexin1, another class of putative gapjunction- forming proteins, and Kvb3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. within a tissue. Recent studies have shown that connexins (Cx) can have either direct or indirect interactions with other plasma membrane ion channels or membrane transport proteins with important functional consequences. For example, in tissues most severely affected by cystic fibrosis (CF), activation of the CF Transmembrane Conductance Regulator (CFTR) has been shown to influence connexin function. Moreover, a direct interaction between Cx45.6 and the Major Intrinsic Protein/AQP0 in lens appears to influence the process of cell differentiation whereas interactions between aquaporin 4 (AQP4) and Cx43 in mouse astrocytes may coordinate the intercellular movement of ions and water between astrocytes. In this review, we discuss evidence supporting interactions between Cx and membrane channels/transporters including CFTR, aquaporins, ionotropic glutamate receptors, and between pannexin1, another class of putative gapjunction- forming proteins, and Kvb3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. within a tissue. Recent studies have shown that connexins (Cx) can have either direct or indirect interactions with other plasma membrane ion channels or membrane transport proteins with important functional consequences. For example, in tissues most severely affected by cystic fibrosis (CF), activation of the CF Transmembrane Conductance Regulator (CFTR) has been shown to influence connexin function. Moreover, a direct interaction between Cx45.6 and the Major Intrinsic Protein/AQP0 in lens appears to influence the process of cell differentiation whereas interactions between aquaporin 4 (AQP4) and Cx43 in mouse astrocytes may coordinate the intercellular movement of ions and water between astrocytes. In this review, we discuss evidence supporting interactions between Cx and membrane channels/transporters including CFTR, aquaporins, ionotropic glutamate receptors, and between pannexin1, another class of putative gapjunction- forming proteins, and Kvb3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. 2+ waves and synchronization of physiological processes between adjacent cells within a tissue. Recent studies have shown that connexins (Cx) can have either direct or indirect interactions with other plasma membrane ion channels or membrane transport proteins with important functional consequences. For example, in tissues most severely affected by cystic fibrosis (CF), activation of the CF Transmembrane Conductance Regulator (CFTR) has been shown to influence connexin function. Moreover, a direct interaction between Cx45.6 and the Major Intrinsic Protein/AQP0 in lens appears to influence the process of cell differentiation whereas interactions between aquaporin 4 (AQP4) and Cx43 in mouse astrocytes may coordinate the intercellular movement of ions and water between astrocytes. In this review, we discuss evidence supporting interactions between Cx and membrane channels/transporters including CFTR, aquaporins, ionotropic glutamate receptors, and between pannexin1, another class of putative gapjunction- forming proteins, and Kvb3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis. b3, a regulatory b-subunit of voltage gated potassium channels. Although the precise molecular nature of these interactions has yet to be defined, their consequences may be critical for normal tissue homeostasis.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Pergamon-Elsevier Science Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CFTR
dc.subject
Conexinas
dc.subject.classification
Biofísica
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Interactions of connexins with other membrane channels and transporters
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-05-11T18:22:10Z
dc.journal.volume
94
dc.journal.number
1-2
dc.journal.pagination
233-244
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Chanson, Marc. Geneva University Hospitals; Suiza
dc.description.fil
Fil: Kotsias, Basilio Aristides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
dc.description.fil
Fil: Peracchia, Camillo. University of Rochester; Estados Unidos
dc.description.fil
Fil: O’Grady, Scott M.. University of Minnesota; Estados Unidos
dc.journal.title
Progress In Biophysics And Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0079610707000053
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.pbiomolbio.2007.03.002
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