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• W2056570135 abstract "In 1967, Revel and Karnovsky 1 Revel J.P. Karnovsky M.J. Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J Cell Biol. 1967; 33: C7-C12 Crossref PubMed Scopus (1037) Google Scholar first described an aggregate of membrane associated particles that, while looking like they blocked the extracellular space, allowed the tracer lanthanum hydroxide to pass through small gaps between the aggregates and named this cluster of particles the “gap junction.” In the heart, they described these structures to be primarily at the long ends of the cells, identified as the intercalated disk (ID). Further studies by Page and his colleague 2 Manjunath C.K. Page E. Cell biology and protein composition of cardiac gap junctions. Am J Physiol. 1985; 248: H783-H791 PubMed Google Scholar noted the presence of a “fuzzy coat” under the gap junctions, giving rise to the speculation that the extracellular aggregates crossed the myocyte membrane and anchored within the cell. From these early studies grew a new field of research on what these aggregates were made of and how they worked. In cardiac studies, the primary component of cardiac gap junctions was identified as a 43-kD protein, 3 Beyer E.C. Paul D.L. Goodenough D.A. Connexin43: a protein from rat heart homologous to a gap junction protein from liver. J Cell Biol. 1987; 105: 2621-2629 Crossref PubMed Scopus (915) Google Scholar subsequently named Connexin43 (Cx43). Studies showed that unlike liver cells, where the hepatocyte connexin, connexin 32, was localized all over the cells, 4 Goodenough D.A. Paul D.L. Jesaitis L. Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions. J Cell Biol. 1988; 107: 1817-1824 Crossref PubMed Scopus (144) Google Scholar in the myocytes of the heart, connexins were preferentially localized to the ends of cells at the IDs such that images showing longitudinal sections of myocytes gave a straight line of staining that was evident at myocyte ends (Figure 1A). Transverse images show that Cx43 does not cover the entire ends of the myocytes; rather it is positioned in a ring around the edges of the ID (Figure 1B). This pattern has been shown in the hearts of mice, 5 Gutstein D.E. et al. Conduction slowing and sudden arrhythmic death in mice with cardiac-restricted inactivation of connexin43. Circ Res. 2001; 88: 333-339 Crossref PubMed Scopus (585) Google Scholar dogs, 6 Peters N.S. et al. Disturbed connexin43 gap junction distribution correlates with the location of reentrant circuits in the epicardial border zone of healing canine infarcts that cause ventricular tachycardia. Circulation. 1997; 95: 988-996 Crossref PubMed Scopus (503) Google Scholar and humans, 7 Smith J.H. et al. Altered patterns of gap junction distribution in ischemic heart disease: an immunohistochemical study of human myocardium using laser scanning confocal microscopy. Am J Pathol. 1991; 139: 801-821 PubMed Google Scholar indicating that this highly organized pattern is conserved across species. Understanding of the function of gap junctions as conduits for electrical current led to hypotheses that the localization of Cx43 in the heart was important for the normal anisotropic conduction of the heart." @default.
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• W2056570135 date "2012-08-01" @default.
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• W2056570135 title "The molecular mechanisms of gap junction remodeling" @default.
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