THE PLASMA MEMBRANE, THE TRANSVERSE TUBULAR SYSTEM, AND THE SARCOPLASMIC RETICULUM

Muscle ◽  
1972 ◽  
pp. 33-46
Author(s):  
DAVID S. SMITH
Keyword(s):  
Plasma Membrane ◽  
Sarcoplasmic Reticulum ◽  
Transverse Tubular System ◽  
Tubular System

Ultrastructural localization of dystropin in human muscle by using gold immunolabelling

1990 ◽  
Vol 240 (1297) ◽  
pp. 197-210 ◽  
Keyword(s):  
Plasma Membrane ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Human Muscle ◽  
Muscle Fibres ◽  
Mouse Muscle ◽  
Transverse Tubular System ◽  
Cytoplasmic Face ◽  
Tubular System ◽  
Gold Probe

Immunolabelling with a 5 nm gold probe was used to localize dystrophin at the ultrastructural level in human muscle. The primary antibody was monoclonal, raised against a segment (amino acids 1181-1388) from the rod domain of dystrophin. The antibody (Dy4/6D3) is specific for dystrophin and shows no immunoreactivity with any protein from mdx mouse muscle or from patients with a gene deletion spanning part of the molecule recognized by the antibody (Nicholson et al . 1989 a ; England et al . 1990). Using this antibody, labelling was almost entirely confined to a narrow 75 nm rim at the periphery of the muscle fibres. Histograms of the distance from the gold probe to the cytoplasmic face of the plasma membrane and of the distance between gold probes (nearest neighbour in a plane parallel with the plasma membrane) displayed modes at approximately 15 nm and 120 nm, respectively. The distribution of the probe was the same in longitudinal and transverse sections of the muscle. These observations suggest that the rod portion of the dystrophin mole­cule is normally arranged close to the cytoplasmic face of the plasma membrane and that the molecules form an interconnecting network. Labelling was not associated with the transverse tubular system.

scholarly journals Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers.

1983 ◽  
Vol 97 (4) ◽  
pp. 1081-1088 ◽  
Author(s):  
J V Pardo ◽  
J D Siliciano ◽  
S W Craig
Keyword(s):  
Plasma Membrane ◽  
Cardiac Muscle ◽  
Cardiac Tissue ◽  
Immunofluorescent Staining ◽  
Cardiac Muscle Cell ◽  
Transverse Tubular System ◽  
Published Evidence ◽  
Tubular System ◽  
Cardiac Muscle Fibers ◽  
Ultrastructural Findings

Immunofluorescent staining of bovine and avian cardiac tissue with affinity-purified antibody to chicken gizzard vinculin reveals two new sites of vinculin reactivity. First, vinculin is organized at the sarcolemma in a striking array of rib-like bands, or costameres. The costameres encircle the cardiac muscle cell perpendicular to the long axis of the fiber and overlie the I bands of the immediately subjacent sarcomeres. The second new site of vinculin reactivity is found in bovine cardiocytes at tubular invaginations of the plasma membrane. The frequency and location of these invaginations correspond to the known frequency and distribution of the transverse tubular system in bovine atrial, ventricular, and Purkinje fibers. We do not detect tubular invaginations that stain with antivinculin in avian cardiocytes and, in fact, a transverse tubular system has not been found in avian cardiac fibers. Apparent lateral Z-line attachments to the sarcolemma and its invaginations have been observed in cardiac muscle by electron microscopy in the same regions where we find vinculin. On the basis of these previous ultrastructural findings and our published evidence for a physical connection between costameres and the underlying myofibrils in skeletal muscle, we interpret the immunofluorescence data of this study to mean that, in cardiac muscle, vinculin is a component of an extensive system of lateral attachment of myofibrils to the plasma membrane and its invaginations.

The Ultrastructure of the White Striated Myotomal Muscle of the Cod, Gadus morhua

1967 ◽  
Vol 24 (12) ◽  
pp. 2549-2553 ◽  
Author(s):  
C. M. Bishop ◽  
P. H. Odense
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Cross Section ◽  
Actin Filaments ◽  
Gadus Morhua ◽  
Striated Muscle ◽  
Fish Muscle ◽  
Transverse Tubular System ◽  
Tubular System ◽  
Myotomal Muscle

The structure of the white skeletal muscle of the cod (Gadus morhua) is described. The peripheral fibrils are ribbon-like and rectangular in cross section with the long axis normal to the sarcolemma. The inner fibrils are mainly polygonal in cross section. Most of the mitochondria and nuclei are peripheral to the fibrils and next to the sarcolemma. The arrangement of the contractile proteins is typical for striated muscle, and the sarcoplasmic reticulum and transverse tubular system are similar to those in other white skeletal fish muscle. A distinct N-band is apparent with indications of branching and reorientation of the actin filaments. Mitochondria are often closely associated with the Z line.

The Fibrillar Flight Muscles of Giant Water-Bugs: An Electron-Microscope Study

1967 ◽  
Vol 2 (3) ◽  
pp. 435-444
Author(s):  
DOREEN E. ASHHURST
Keyword(s):  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Flight Muscle ◽  
Muscle Fibres ◽  
Transverse Tubular System ◽  
Tropical Water ◽  
Tubular System ◽  
Flight Muscles ◽  
And Function ◽  
Water Bugs

The fibrillar flight muscles of several species of tropical water-bugs of the family Belostomatidae have been examined in the electron microscope. The myofibrils are very similar to those of the other fibrillar flight muscles which have been studied. The membrane systems, however, display features which appear to be peculiar to this family. The sarcoplasmic reticulum can be divided into three parts: a series of interconnecting vesicles surrounding the Z-lines, randomly scattered small vesicles around the myofibrils, and flattened cisternae which lie along the transverse tubular system, and form the dyads. These three components of the sarcoplasmic reticulum do not appear to be interconnected. The cisternae of the dyads contain an electrondense substance. The narrow tubules of the transverse tubular system or T-system penetrate deep into the fibre from the cell membrane. They follow a course roughly perpendicular to the myofibrils at the level of the M-lines. The dyads are scattered along their length, and may not be near a myofibril. Another system of very large vesicles is found in the muscle fibres, interspersed among the mitochondria. These vesicles usually appear to be empty; their nature and function are not at present known. Numerous mitochondria are present among the myofibrils. The peculiarities of the water-bug fibrillar flight muscle are discussed in relation to the flight muscles of other insects and the physiological properties of fibrillar flight muscle.

scholarly journals CORRELATED MORPHOLOGICAL AND PHYSIOLOGICAL STUDIES ON ISOLATED SINGLE MUSCLE FIBERS

1968 ◽  
Vol 38 (1) ◽  
pp. 115-129 ◽  
Author(s):  
Philip W. Brandt ◽  
John P. Reuben ◽  
Harry Grundfest
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Current Flow ◽  
Muscle Fibers ◽  
Single Muscle ◽  
Unit Membrane ◽  
Membrane Phase ◽  
Transverse Tubular System ◽  
Contraction Coupling ◽  
Cytoplasmic Material ◽  
Tubular System

Living muscle fibers of crayfish become dark during efflux of Cl-. This change in appearance is correlated with occurrence of vacuolation in the fixed fibers. The vacuoles begin at and are mainly confined to the terminals of the transverse tubular system (TTS) which are in diadic contact with the sarcoplasmic reticulum (SR). In electron micrographs swellings more than 1 µ in diameter may be seen connected to the sarcolemma or sarcolemmal invaginations by relatively unswollen tubules about 300–500 A wide. Darkening of the living fibers can be reversed by causing an influx of Cl-. Vacuoles are then absent in the fixed preparations. These findings accord with the conclusion that the membrane of the TTS is anion permselective. Localization of the selectivity to the membrane of the terminals of the TTS strengthens the hypothesis that a channeling of current flow is responsible for initiation of excitation-contraction coupling. During the swelling, and upon its reversal, the area of the membrane of the terminals must change reversibly by about two to four orders of magnitude. The absence of changes in the dimensions of the unit membrane indicates that the expansion of the membrane and its subsequent shrinkage involve reversible incorporation of cytoplasmic material into the membrane phase.

scholarly journals CHANGES IN THE SARCOPLASMIC RETICULUM AND TRANSVERSE TUBULAR SYSTEM OF FAST AND SLOW SKELETAL MUSCLES OF THE MOUSE DURING POSTNATAL DEVELOPMENT

1971 ◽  
Vol 51 (2) ◽  
pp. 369-383 ◽  
Author(s):  
A. R. Luff ◽  
H. L. Atwood
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Postnatal Development ◽  
Surface Area ◽  
Fiber Surface ◽  
Fiber Volume ◽  
Transverse Tubular System ◽  
Tubular System ◽  
Slow Twitch Muscle ◽  
T Tubules ◽  
Relative Change

The sarcoplasmic reticulum (SR) and transverse tubular system (TTS) of a fast-twitch muscle (extensor digitorum longus-EDL) and a slow-twitch muscle (soleus-SOL) of the mouse were examined during postnatal development. Muscles of animals newborn to 60 days old were fixed in glutaraldehyde and osmium tetroxide and examined with an electron microscope. At birth the few T tubules were often oriented longitudinally, but at the age of 10 days most of them had a transverse orientation. In the EDL, the estimated volume of the TTS increased from 0.08% at birth to 0.4% in the adult; corresponding values for the SOL were 0.04% at birth and 0.22% in the adult. A similar relative change was observed in surface area of the TTS during development. Calculated on the basis of a 30 µm diameter fiber, the surface area of the TTS in the EDL increased from 0.60 cm2 TTS/cm2 fiber surface in the newborn to 3.1 cm2/cm2 in the adult, compared with 0.15 cm2/cm2 at birth to 1.80 cm2/cm2 in the adult for the SOL. The SR in the newborn muscles occurred as a loose network of tubules that developed rapidly within the subsequent 20 days, especially at the I band level. The volume of the SR increased in the EDL from 1.1% of fiber volume at birth to 5.5% in the adult. In the SOL the change was from 1.7% to 2.9%. The SOL approached the adult values more rapidly than the EDL, although the EDL had more SR and T tubules. Fibers of both EDL and SOL muscles showed variation in Z line thickness, mitochondrial content, and diameter, but over-all differences between the two muscles in amount of SR and TTS were significant. It is considered that the differing amounts of SR and TTS are closely related to the differing speeds of contraction that have been demonstrated for these two muscles.

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