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Article: Selective defects in channel permeability associated with Cx32 mutations causing X-linked Charcot-Marie-Tooth disease

TitleSelective defects in channel permeability associated with Cx32 mutations causing X-linked Charcot-Marie-Tooth disease
Authors
KeywordsConnexin
Dye coupling
Gap junction
Genetic disease
Human
PNS
Issue Date2006
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ynbdi
Citation
Neurobiology Of Disease, 2006, v. 21 n. 3, p. 607-617 How to Cite?
AbstractThe X-linked form of Charcot-Marie-Tooth disease (CMTX) is caused by mutations in connexin32 (Cx32), a gap junction protein expressed by Schwann cells where it forms reflexive channels that allow the passage of ions and signaling molecules across the myelin sheath. Although most mutations result in loss of function, several studies have reported that some retain the ability to form homotypic intercellular channels. To gain insight into the molecular defect of three functional CMTX variants, S26L, Δ111-116 and R220stop, we have used several fluorescent tracers of different size and ionic charge to compare their permeation properties to those of wild-type Cx32. Although all mutations allowed the passage of the dye with the smallest molecular mass, they exhibited a clear reduction in the permeability of either one or all of the probes with respect to wild-type channels, as assessed by the percentage of injections showing dye coupling. These data reveal that a lower size cutoff distinguishes these functional CMTX variants from wild-type channels and suggest that this defect may be of pathophysiological relevance. © 2005 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/132693
ISSN
2015 Impact Factor: 4.856
2015 SCImago Journal Rankings: 2.875
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorBicego, Men_HK
dc.contributor.authorMorassutto, Sen_HK
dc.contributor.authorHernandez, VHen_HK
dc.contributor.authorMorgutti, Men_HK
dc.contributor.authorMammano, Fen_HK
dc.contributor.authorD'Andrea, Pen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.date.accessioned2011-03-28T09:28:18Z-
dc.date.available2011-03-28T09:28:18Z-
dc.date.issued2006en_HK
dc.identifier.citationNeurobiology Of Disease, 2006, v. 21 n. 3, p. 607-617en_HK
dc.identifier.issn0969-9961en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132693-
dc.description.abstractThe X-linked form of Charcot-Marie-Tooth disease (CMTX) is caused by mutations in connexin32 (Cx32), a gap junction protein expressed by Schwann cells where it forms reflexive channels that allow the passage of ions and signaling molecules across the myelin sheath. Although most mutations result in loss of function, several studies have reported that some retain the ability to form homotypic intercellular channels. To gain insight into the molecular defect of three functional CMTX variants, S26L, Δ111-116 and R220stop, we have used several fluorescent tracers of different size and ionic charge to compare their permeation properties to those of wild-type Cx32. Although all mutations allowed the passage of the dye with the smallest molecular mass, they exhibited a clear reduction in the permeability of either one or all of the probes with respect to wild-type channels, as assessed by the percentage of injections showing dye coupling. These data reveal that a lower size cutoff distinguishes these functional CMTX variants from wild-type channels and suggest that this defect may be of pathophysiological relevance. © 2005 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ynbdien_HK
dc.relation.ispartofNeurobiology of Diseaseen_HK
dc.subjectConnexinen_HK
dc.subjectDye couplingen_HK
dc.subjectGap junctionen_HK
dc.subjectGenetic diseaseen_HK
dc.subjectHumanen_HK
dc.subjectPNSen_HK
dc.titleSelective defects in channel permeability associated with Cx32 mutations causing X-linked Charcot-Marie-Tooth diseaseen_HK
dc.typeArticleen_HK
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_HK
dc.identifier.authorityBruzzone, R=rp01442en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.nbd.2005.09.005en_HK
dc.identifier.pmid16442804-
dc.identifier.scopuseid_2-s2.0-33244478285en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33244478285&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume21en_HK
dc.identifier.issue3en_HK
dc.identifier.spage607en_HK
dc.identifier.epage617en_HK
dc.identifier.isiWOS:000235899100016-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBicego, M=7004711890en_HK
dc.identifier.scopusauthoridMorassutto, S=12645523300en_HK
dc.identifier.scopusauthoridHernandez, VH=12645138300en_HK
dc.identifier.scopusauthoridMorgutti, M=8905989600en_HK
dc.identifier.scopusauthoridMammano, F=7006987421en_HK
dc.identifier.scopusauthoridD'Andrea, P=7005979859en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK

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