title: Polygons and adhesion plaques and the disassembly and assembly of myofibrils in cardiac myocytes.
abstract: Successive stages in the disassembly of myofibrils and the subsequent assembly of new myofibrils have been studied in cultures of dissociated chick cardiac myocytes. The myofibrils in trypsinized and dispersed myocytes are sequentially disassembled during the first 3 d of culture. They split longitudinally and then assemble into transitory polygons. Multiples of single sarcomeres, the cardiac polygons, are analogous to the transitory polygonal configurations assumed by stress fibers in spreading fibroblasts. They differ from their counterparts in fibroblasts in that they consist of muscle alpha-actinin vertices and muscle myosin heavy chain struts, rather than of the nonmuscle contractile protein isoforms of stress fiber polygons. EM sections reveal the vertices and struts in cardiac polygons to be typical Z and A bands. Most cardiac polygons are eliminated by day 5 of culture. Concurrent with the disassembly and elimination of the original myofibrils new myofibrils are rapidly assembled elsewhere in the same myocyte. Without exception both distal tips of each nascent myofibril terminate in adhesion plaques. The morphology and composition of the adhesion plaques capping each end of each myofibril are similar to those of the termini of stress fibers in fibroblasts. However, whereas the adhesion complexes involving stress fibers in fibroblasts consist of vinculin/nonmuscle alpha-actinin/beta- and gamma-actins, the analogous structures in myocytes involving myofibrils consist of vinculin/muscle alpha-actinin/alpha-actin. The addition of 1.7-2.0 microns sarcomeres to the distal tips of an elongating myofibril, irrespective of whether the myofibril consists of 1, 10, or several hundred tandem sarcomeres, occurs while the myofibril appears to remain linked to its respective adhesion plaques. The adhesion plaques in vitro are the equivalent of the in vivo intercalated discs, both in terms of their molecular composition and with respect to their functioning as initiating sites for the assembly of new sarcomeres. How 1.7-2.0 microns nascent sarcomeres can be added distally during elongation while the tips of the myofibrils remain inserted into submembranous adhesion plaques is unknown.
authors: Department of Anatomy, School of Medicine, University of Pennsylvania, Philadelphia 19104.
authors: Z X
authors: ZX
authors: Lin
authors: S
authors: S
authors: Holtzer
authors: T
authors: T
authors: Schultheiss
authors: J
authors: J
authors: Murray
authors: T
authors: T
authors: Masaki
authors: D A
authors: DA
authors: Fischman
authors: H
authors: H
authors: Holtzer
mesh_terms: D000185:Actinin / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D002448:Cell Adhesion; D002454:Cell Differentiation; D002478:Cells, Cultured; D002642:Chick Embryo; D003598:Cytoskeletal Proteins; D003599:Cytoskeleton / Q000648:ultrastructure*; D003893:Desmin / Q000378:metabolism; D051180:Desmoplakins; D005455:Fluorescent Antibody Technique; D007633:Keratins / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D009024:Morphogenesis; D009124:Muscle Proteins / Q000378:metabolism; D009206:Myocardium / Q000166:cytology*; D009210:Myofibrils / Q000648:ultrastructure*; D009218:Myosins / Q000378:metabolism; D016596:Vinculin
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D003893:Desmin; D051180:Desmoplakins; D008562:Membrane Glycoproteins; D009124:Muscle Proteins; D000185:Actinin; D016596:Vinculin; D007633:Keratins; D009218:Myosins