Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/77172
Type: Artigo de periódico
Title: alpha-Cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform
Author: Lima, PRM
Salles, TSI
Costa, FF
Saad, STO
Abstract: The 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.
Subject: cardiac muscle
intercalated disc
thin filament
yeast two-hybrid screening
Country: EUA
Editor: Wiley-liss
Rights: fechado
Identifier DOI: 10.1002/jcb.10561
Date Issue: 2003
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

Files in This Item:
File Description SizeFormat 
WOS000184609400013.pdf218.91 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.