alpha-Cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform

dc.creatorLima, PRM
dc.creatorSalles, TSI
dc.creatorCosta, FF
dc.creatorSaad, STO
dc.date2003
dc.dateAUG 15
dc.date2014-11-14T23:00:16Z
dc.date2015-11-26T16:08:50Z
dc.date2014-11-14T23:00:16Z
dc.date2015-11-26T16:08:50Z
dc.date.accessioned2018-03-28T22:57:24Z
dc.date.available2018-03-28T22:57:24Z
dc.identifierJournal Of Cellular Biochemistry. Wiley-liss, v. 89, n. 6, n. 1215, n. 1221, 2003.
dc.identifier0730-2312
dc.identifierWOS:000184609400013
dc.identifier10.1002/jcb.10561
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/77172
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/77172
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/77172
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1266462
dc.descriptionThe band 3 protein is the major integral protein present in the erythrocyte membrane. Two tissue-specific isoforms area I so expressed in kidney alpha intercalated cells and in cardiomyocytes. It has been suggested that the cardiac isoform predominantly mediates the anion exchange in cardiomyocytes, but the role of the cytoplasmic domain of the band 3 (CDB3) protein in the cardiac tissue is unknown. In order to characterize novel associations of the CDB3 in the cardiac tissue, we performed the two-hybrid assay, using a bait comprising the region from leu 258 to leu 311 of the erythrocyte band 3, which must also be present in the cardiac isoform. The assay revealed two clones containing the C-terminal region of the a-cardiac actin. Immunoprecipitation of whole rat heart using an anti-actin antibody, immunoblotted with anti-human band 3, showed that actin binds to band 3 which was confirmed in the reverse assay. The confocal microscopy showed band 3 in the intercalated discs. Thus, besides the in vivo physical interaction in the Saccharomyces cerevisiae cell, we demonstrated using immunopreciptation that there is a physical association of band 3 with a-cardiac actin in cardiomyocyte, and we suggest that the binding occur 'in situ,' in the intercalated disc, a site of cell-cell contact and attachment of the sarcomere to the plasma membrane. (C) 2003 Wiley-Liss, Inc.
dc.description89
dc.description6
dc.description1215
dc.description1221
dc.languageen
dc.publisherWiley-liss
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Cellular Biochemistry
dc.relationJ. Cell. Biochem.
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectcardiac muscle
dc.subjectintercalated disc
dc.subjectthin filament
dc.subjectyeast two-hybrid screening
dc.subjectIntact Yeast-cells
dc.subjectHigh-efficiency Transformation
dc.subjectHuman Erythrocyte-membrane
dc.subjectCytoplasmic Domain
dc.subjectIdentification
dc.subjectPhosphorylation
dc.subjectCardiomyopathy
dc.subjectMutations
dc.subjectProtein
dc.subjectMuscle
dc.titlealpha-Cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución