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Open AccessJournal ArticleDOI

THE ULTRASTRUCTURE OF THE CAT MYOCARDIUM: I. Ventricular Papillary Muscle

Don W. Fawcett, +1 more
- 01 Jul 1969 - 
- Vol. 42, Iss: 1, pp 1-45
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TLDR
In papillary muscles worked in vitro without added substrate, there is a marked depletion of both glycogen and lipid, and no morphological evidence for preferential use of glycogen was found.
Abstract
The ultrastructure of cat papillary muscle was studied with respect to the organization of the contractile material, the structure of the organelles, and the cell junctions. The morphological changes during prolonged work in vitro and some effects of fixation were assessed. The myofilaments are associated in a single coherent bundle extending throughout the fiber cross-section. The absence of discrete "myofibrils" in well preserved cardiac muscle is emphasized. The abundant mitochondria confined in clefts among the myofilaments often have slender prolongations, possibly related to changes in their number or their distribution as energy sources within the contractile mass. The large T tubules that penetrate ventricular cardiac muscle fibers at successive I bands are arranged in rows and are lined with a layer of protein-polysaccharide. Longitudinal connections between T tubules are common. The simple plexiform sarcoplasmic reticulum is continuous across the Z lines, and no circumferential "Z tubules" were identified. Specialized contacts between the reticulum and the sarcolemma are established on the T tubules and the cell periphery via subsarcolemmal saccules or cisterns. At cell junctions, a 20 A gap can be demonstrated between the apposed membranes in those areas commonly interpreted as sites of membrane fusion. In papillary muscles worked in vitro without added substrate, there is a marked depletion of both glycogen and lipid. No morphological evidence for preferential use of glycogen was found.

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Book ChapterDOI

Structure and function of intercellular junctions.

TL;DR: This chapter reviews the morphological information on intercellular junctions derived from thin-sectioning, negative staining and freeze-cleave techniques, as well as from x-ray diffraction and biochemical investigations, and correlates the structural parameters with known or proposed physiological functions.
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Junctophilins: a novel family of junctional membrane complex proteins.

TL;DR: The junctophilins (JPs), a novel conserved family of proteins that are components of the junctional complexes, are identified and suggest that JPs are important components of junctional membrane complexes.
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Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues.

TL;DR: A topological model of connexins with unique cytoplasmic domains but conserved transmembrane and extracellular regions is supported, supported by direct evidence that connexin43 is a cardiac gap junction protein and raised rabbit antisera directed against synthetic oligopeptides corresponding to two unique regions of its sequence.
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Sarcoplasmic reticulum and excitation-contraction coupling in mammalian smooth muscles

TL;DR: The presence of both thick and thin myofilaments and of rough SR in smooth muscles supports the dual, contractile and morphogenetic, function of smooth muscle.
References
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Journal ArticleDOI

A simplified lead citrate stain for use in electron microscopy.

TL;DR: This communication reports the use of a commercially available lead citratO to eliminate the lead citrate stain in electron microscopy.
Journal ArticleDOI

Junctional complexes in various epithelia

TL;DR: The tight junction is impervious to concentrated protein solutions and appears to function as a diffusion barrier or "seal," and the desmosome and probably also the zonula adhaerens may represent intercellular attachment devices.
Journal ArticleDOI

Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle.

TL;DR: The results obtained show that the filaments are structurally polarized, and in muscle are arranged so that all of them attached on one side of a given Z-line point in one direction, whilst those on the other are oppositely oriented.
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