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1

Adams, Marvin E., Heather A. Mueller та Stanley C. Froehner. "In vivo requirement of the α-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4". Journal of Cell Biology 155, № 1 (2001): 113–22. http://dx.doi.org/10.1083/jcb.200106158.

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α-Syntrophin is a scaffolding adapter protein expressed primarily on the sarcolemma of skeletal muscle. The COOH-terminal half of α-syntrophin binds to dystrophin and related proteins, leaving the PSD-95, discs-large, ZO-1 (PDZ) domain free to recruit other proteins to the dystrophin complex. We investigated the function of the PDZ domain of α-syntrophin in vivo by generating transgenic mouse lines expressing full-length α-syntrophin or a mutated α-syntrophin lacking the PDZ domain (ΔPDZ). The ΔPDZ α-syntrophin displaced endogenous α- and β1-syntrophin from the sarcolemma and resulted in sarco
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2

Williams, McRae W., and Robert J. Bloch. "Extensive but Coordinated Reorganization of the Membrane Skeleton in Myofibers of Dystrophic (mdx) Mice." Journal of Cell Biology 144, no. 6 (1999): 1259–70. http://dx.doi.org/10.1083/jcb.144.6.1259.

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We used immunofluorescence techniques and confocal imaging to study the organization of the membrane skeleton of skeletal muscle fibers of mdx mice, which lack dystrophin. β-Spectrin is normally found at the sarcolemma in costameres, a rectilinear array of longitudinal strands and elements overlying Z and M lines. However, in the skeletal muscle of mdx mice, β-spectrin tends to be absent from the sarcolemma over M lines and the longitudinal strands may be disrupted or missing. Other proteins of the membrane and associated cytoskeleton, including syntrophin, β-dystroglycan, vinculin, and Na,K-A
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3

Rybakova, Inna N., Jitandrakumar R. Patel, and James M. Ervasti. "The Dystrophin Complex Forms a Mechanically Strong Link between the Sarcolemma and Costameric Actin." Journal of Cell Biology 150, no. 5 (2000): 1209–14. http://dx.doi.org/10.1083/jcb.150.5.1209.

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The absence of dystrophin complex leads to disorganization of the force-transmitting costameric cytoskeleton and disruption of sarcolemmal membrane integrity in skeletal muscle. However, it has not been determined whether the dystrophin complex can form a mechanically strong bond with any costameric protein. We performed confocal immunofluorescence analysis of isolated sarcolemma that were mechanically peeled from skeletal fibers of mouse hindlimb muscle. A population of γ-actin filaments was stably associated with sarcolemma isolated from normal muscle and displayed a costameric pattern that
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4

Fraysse, Bodvaël, Thierry Rouaud, Marie Millour, Josiane Fontaine-Pérus, Marie-France Gardahaut, and Dmitri O. Levitsky. "Expression of the Na+/Ca2+exchanger in skeletal muscle." American Journal of Physiology-Cell Physiology 280, no. 1 (2001): C146—C154. http://dx.doi.org/10.1152/ajpcell.2001.280.1.c146.

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The expression of the Na+/Ca2+ exchanger was studied in differentiating muscle fibers in rats. NCX1 and NCX3 isoform (Na+/Ca2+ exchanger isoform) expression was found to be developmentally regulated. NCX1 mRNA and protein levels peaked shortly after birth. Conversely, NCX3 isoform expression was very low in muscles of newborn rats but increased dramatically during the first 2 wk of postnatal life. Immunocytochemical analysis showed that NCX1 was uniformly distributed along the sarcolemmal membrane of undifferentiated rat muscle fibers but formed clusters in T-tubular membranes and sarcolemma o
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5

Porter, GA, GM Dmytrenko, JC Winkelmann, and RJ Bloch. "Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle." Journal of Cell Biology 117, no. 5 (1992): 997–1005. http://dx.doi.org/10.1083/jcb.117.5.997.

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Duchenne's muscular dystrophy (DMD) is caused by the absence or drastic decrease of the structural protein, dystrophin, and is characterized by sarcolemmal lesions in skeletal muscle due to the stress of contraction. Dystrophin has been localized to the sarcolemma, but its organization there is not known. We report immunofluorescence studies which show that dystrophin is concentrated, along with the major muscle isoform of beta-spectrin, in three distinct domains at the sarcolemma: in elements overlying both I bands and M lines, and in occasional strands running along the longitudinal axis of
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6

O'Neill, Andrea, McRae W. Williams, Wendy G. Resneck, Derek J. Milner, Yassemi Capetanaki, and Robert J. Bloch. "Sarcolemmal Organization in Skeletal Muscle Lacking Desmin: Evidence for Cytokeratins Associated with the Membrane Skeleton at Costameres." Molecular Biology of the Cell 13, no. 7 (2002): 2347–59. http://dx.doi.org/10.1091/mbc.01-12-0576.

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The sarcolemma of fast-twitch muscle is organized into “costameres,” structures that are oriented transversely, over the Z and M lines of nearby myofibrils, and longitudinally, to form a rectilinear lattice. Here we examine the role of desmin, the major intermediate filament protein of muscle in organizing costameres. In control mouse muscle, desmin is enriched at the sarcolemmal domains that lie over nearby Z lines and that also contain β-spectrin. In tibialis anterior muscle from mice lacking desmin due to homologous recombination, most costameres are lost. In myofibers from desmin −/− quadr
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7

Wang, W., P. A. Hansen, B. A. Marshall, J. O. Holloszy, and M. Mueckler. "Insulin unmasks a COOH-terminal Glut4 epitope and increases glucose transport across T-tubules in skeletal muscle." Journal of Cell Biology 135, no. 2 (1996): 415–30. http://dx.doi.org/10.1083/jcb.135.2.415.

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An improved immunogold labeling procedure was used to examine the subcellular distribution of glucose transporters in Lowricryl HM20-embedded skeletal muscle from transgenic mice overexpressing either Glut1 or Glut4. In basal muscle, Glut4 was highly enriched in membranes of the transverse tubules and the terminal cisternae of the triadic junctions. Less than 10% of total muscle Glut4 was present in the vicinity of the sarcolemmal membrane. Insulin treatment increased the number of gold particles associated with the transverse tubules and the sarcolemma by three-fold. However, insulin also inc
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8

Ohlendieck, K., J. M. Ervasti, J. B. Snook, and K. P. Campbell. "Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma." Journal of Cell Biology 112, no. 1 (1991): 135–48. http://dx.doi.org/10.1083/jcb.112.1.135.

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mAbs specific for protein components of the surface membrane of rabbit skeletal muscle have been used as markers in the isolation and characterization of skeletal muscle sarcolemma membranes. Highly purified sarcolemma membranes from rabbit skeletal muscle were isolated from a crude surface membrane preparation by wheat germ agglutination. Immunoblot analysis of subcellular fractions from skeletal muscle revealed that dystrophin and its associated glycoproteins of 156 and 50 kD are greatly enriched in purified sarcolemma vesicles. The purified sarcolemma was also enriched in novel sarcolemma m
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9

Lebakken, Connie S., David P. Venzke, Ronald F. Hrstka, et al. "Sarcospan-Deficient Mice Maintain Normal Muscle Function." Molecular and Cellular Biology 20, no. 5 (2000): 1669–77. http://dx.doi.org/10.1128/mcb.20.5.1669-1677.2000.

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ABSTRACT Sarcospan is an integral membrane component of the dystrophin-glycoprotein complex (DGC) found at the sarcolemma of striated and smooth muscle. The DGC plays important roles in muscle function and viability as evidenced by defects in components of the DGC, which cause muscular dystrophy. Sarcospan is unique among the components of the complex in that it contains four transmembrane domains with intracellular N- and C-terminal domains and is a member of the tetraspan superfamily of proteins. Sarcospan is tightly linked to the sarcoglycans, and together these proteins form a subcomplex w
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10

Anderson, Judy E. "Myotube phospholipid synthesis and sarcolemmal ATPase activity in dystrophic (mdx) mouse muscle." Biochemistry and Cell Biology 69, no. 12 (1991): 835–41. http://dx.doi.org/10.1139/o91-124.

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Phospholipid incorporation of 32P by primary myotube cultures and the tissue activity of sarcolemmal Na+/K+-transporting ATPase were studied to determine whether the absence of dystrophin from dystrophic (mdx) muscle would affect membrane lipid synthesis and membrane function. The incorporation of 32P by phospholipid as a ratio with total protein was greater in cultured dystrophic cells compared with control cells. The mdx cells also incorporated more 32P than control cells into phosphatidylethanolamine, which is thought to increase prior to myoblast fusion, and less into phosphatidylserine, p
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11

Muñoz, P., M. Rosemblatt, X. Testar, et al. "The T-tubule is a cell-surface target for insulin-regulated recycling of membrane proteins in skeletal muscle." Biochemical Journal 312, no. 2 (1995): 393–400. http://dx.doi.org/10.1042/bj3120393.

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(1) In this study we have determined the distribution of various membrane proteins involved in insulin-activated glucose transport in T-tubules and in sarcolemma from rat skeletal muscle. Two independent experimental approaches were used to determine the presence of membrane proteins in T-tubules: (i) the purification of T-tubules free from sarcolemmal membranes by lectin agglutination, and (ii) T-tubule vesicle immunoadsorption. These methods confirmed that T-tubules from rat skeletal muscle were enriched with dihydropyridine receptors and tt28 protein and did not contain the sarcolemmal mark
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12

Masuda, T., N. Fujimaki, E. Ozawa, and H. Ishikawa. "Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers." Journal of Cell Biology 119, no. 3 (1992): 543–48. http://dx.doi.org/10.1083/jcb.119.3.543.

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A confocal laser microscope was used to analyze the localization pattern of dystrophin along the sarcolemma in guinea pig skeletal muscle fibers. Hind leg muscles of the normal animals were freshly dissected and frozen for cryostat sections, which were then stained with a monoclonal antidystrophin antibody. In confocal laser microscopy, immunofluorescence staining in relatively thick sections could be sharply imaged in thin optical sections. When longitudinal and transverse sections of muscle fibers were examined, the immunostaining of dystrophin was seen as linearly aligned fluorescent dots o
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13

Dickson, G., A. Azad, G. E. Morris, H. Simon, M. Noursadeghi, and F. S. Walsh. "Co-localization and molecular association of dystrophin with laminin at the surface of mouse and human myotubes." Journal of Cell Science 103, no. 4 (1992): 1223–33. http://dx.doi.org/10.1242/jcs.103.4.1223.

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In Duchenne muscular dystrophy (DMD), deficiency of the protein dystrophin results in necrosis of muscle myofibres, associated with lesions in the sarcolemma and surrounding basal lamina. Dystrophin has been proposed to be a major component of the sub-sarcolemmal cytoskeleton involved in maintaining the integrity of the myofibre plasma membrane, and is known to associate with a group of sarcolemmal glycoproteins, one of which exhibits high affinity binding to the basal lamina component laminin. However, a direct or indirect transmembrane association of dystrophin in muscle cells with the myofi
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14

Jorgensen, A. O., and L. R. Jones. "Immunoelectron microscopical localization of phospholamban in adult canine ventricular muscle." Journal of Cell Biology 104, no. 5 (1987): 1343–52. http://dx.doi.org/10.1083/jcb.104.5.1343.

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The subcellular distribution of phospholamban in adult canine ventricular myocardial cells was determined by the indirect immunogold-labeling technique. The results presented suggest that phospholamban, like the Ca2+-ATPase, is uniformly distributed in the network sarcoplasmic reticulum but absent from the junctional portion of the junctional sarcoplasmic reticulum. Unlike the Ca2+-ATPase, but like cardiac calsequestrin, phospholamban also appears to be present in the corbular sarcoplasmic reticulum. Comparison of the relative distribution of phospholamban immunolabeling in the sarcoplasmic re
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15

Schafer, DA, and FE Stockdale. "Identification of sarcolemma-associated antigens with differential distributions on fast and slow skeletal muscle fibers." Journal of Cell Biology 104, no. 4 (1987): 967–79. http://dx.doi.org/10.1083/jcb.104.4.967.

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We have identified three sarcolemma-associated antigens, including two antigens that are differentially distributed on skeletal muscle fibers of the fast, fast/slow, and slow types. Monoclonal antibodies were prepared using partially purified membranes of adult chicken skeletal muscles as immunogens and were used to characterize three antigens associated with the sarcolemma of muscle fibers. Immunofluorescence staining of cryosections of adult and embryonic chicken muscles showed that two of the three antigens differed in expression by fibers depending on developmental age and whether the fibe
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16

Walzel, Bernd, Oliver Speer, Ernie Boehm, et al. "New creatine transporter assay and identification of distinct creatine transporter isoforms in muscle." American Journal of Physiology-Endocrinology and Metabolism 283, no. 2 (2002): E390—E401. http://dx.doi.org/10.1152/ajpendo.00428.2001.

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Despite the pivotal role of creatine (Cr) and phosphocreatine (PCr) in muscle metabolism, relatively little is known about sarcolemmal creatine transport, creatine transporter (CRT) isoforms, and subcellular localization of the CRT proteins. To be able to quantify creatine transport across the sarcolemma, we have developed a new in vitro assay using rat sarcolemmal giant vesicles. The rat giant sarcolemmal vesicle assay reveals the presence of a specific high-affinity and saturable transport system for Cr in the sarcolemma (Michaelis-Menten constant 52.4 ± 9.4 μM and maximal velocity value 17.
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17

García-Pelagio, Karla P., Joaquin Muriel, Andrea O'Neill, et al. "Myopathic changes in murine skeletal muscle lacking synemin." American Journal of Physiology-Cell Physiology 308, no. 6 (2015): C448—C462. http://dx.doi.org/10.1152/ajpcell.00331.2014.

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Diseases of striated muscle linked to intermediate filament (IF) proteins are associated with defects in the organization of the contractile apparatus and its links to costameres, which connect the sarcomeres to the cell membrane. Here we study the role in skeletal muscle of synemin, a type IV IF protein, by examining mice null for synemin (synm-null). Synm-null mice have a mild skeletal muscle phenotype. Tibialis anterior (TA) muscles show a significant decrease in mean fiber diameter, a decrease in twitch and tetanic force, and an increase in susceptibility to injury caused by lengthening co
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18

Cavey, Michael J., and Harvey D. Strecker. "Ultrastructure of the caudal muscle cells in the larva of a polyclinid ascidian." Canadian Journal of Zoology 63, no. 6 (1985): 1410–19. http://dx.doi.org/10.1139/z85-211.

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Two paraxial bands of somatic striated muscle occur in the tail of the larva of the compound ascidian Aplidium ?constellatum. The mononucleate muscle cells of each band align in longitudinal rows between the epidermis and the notochord. The cross-striated myofibrils, originating and terminating at intermediate junctions on the transverse cellular boundaries, are indiscrete. They follow a spiral course through the subcortical and medullary sarcoplasm, bypassing the nucleus and the other organelles and inclusions in the center of the cell. Cisternae of the sarcoplasmic reticulum envelop the myof
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19

Lawler, John M., Mary Kunst, Jeff M. Hord та ін. "EUK-134 ameliorates nNOSμ translocation and skeletal muscle fiber atrophy during short-term mechanical unloading". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 306, № 7 (2014): R470—R482. http://dx.doi.org/10.1152/ajpregu.00371.2013.

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Reduced mechanical loading during bedrest, spaceflight, and casting, causes rapid morphological changes in skeletal muscle: fiber atrophy and reduction of slow-twitch fibers. An emerging signaling event in response to unloading is the translocation of neuronal nitric oxide synthase (nNOSμ) from the sarcolemma to the cytosol. We used EUK-134, a cell-permeable mimetic of superoxide dismutase and catalase, to test the role of redox signaling in nNOSμ translocation and muscle fiber atrophy as a result of short-term (54 h) hindlimb unloading. Fischer-344 rats were divided into ambulatory control, h
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20

Dunckley, M. G., K. E. Wells, T. A. Piper, D. J. Wells, and G. Dickson. "Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo." Journal of Cell Science 107, no. 6 (1994): 1469–75. http://dx.doi.org/10.1242/jcs.107.6.1469.

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Dystrophin has been proposed to associate with the skeletal muscle membrane by way of a glycoprotein complex that interacts with its C-terminal domains. Transfection of mdx mouse myotubes in culture or myofibres in vivo with recombinant genes encoding human dystrophin deletion mutants shows, however, that not only the C terminus of dystrophin but also its N-terminal actin-binding domain can locate independently to the muscle sarcolemma. This observation suggests that lack of sarcolemma-associated dystrophin in Duchenne muscular dystrophy (DMD) muscle may result from enhanced degradation of tru
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21

North, A. J., B. Galazkiewicz, T. J. Byers, J. R. Glenney, and J. V. Small. "Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle." Journal of Cell Biology 120, no. 5 (1993): 1159–67. http://dx.doi.org/10.1083/jcb.120.5.1159.

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The sarcolemma of the smooth muscle cell displays two alternating structural domains in the electron microscope: densely-staining plaques that correspond to the adherens junctions and intervening uncoated regions which are rich in membrane invaginations, or caveolae. The adherens junctions serve as membrane anchorage sites for the actin cytoskeleton and are typically marked by antibodies to vinculin. We show here by immunofluorescence and immunoelectron microscopy that dystrophin is specifically localized in the caveolae-rich domains of the smooth muscle sarcolemma, together with the caveolae-
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22

DRAEGER, Annette, Susan WRAY, and Eduard B. BABIYCHUK. "Domain architecture of the smooth-muscle plasma membrane: regulation by annexins." Biochemical Journal 387, no. 2 (2005): 309–14. http://dx.doi.org/10.1042/bj20041363.

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Individual signalling events are processed in distinct, spatially segregated domains of the plasma membrane. In a smooth muscle, the sarcolemma is divided into domains of focal adhesions alternating with caveolae-rich zones, both harbouring a specific subset of membrane-associated proteins. Recently, we have demonstrated that the sarcolemmal lipids are similarly segregated into domains of cholesterol-rich lipid rafts and glycerophospholipid-rich non-raft regions. In the present study, we provide a detailed structural analysis of the relationship between these proteinaceous and lipid domains. W
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23

Muñoz, P., M. Rosemblatt, X. Testar, M. Palacín, and A. Zorzano. "Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle." Biochemical Journal 307, no. 1 (1995): 273–80. http://dx.doi.org/10.1042/bj3070273.

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1. Several cell-surface domains of sarcolemma and T-tubule from skeletal-muscle fibre were isolated and characterized. 2. A protocol of subcellular fractionation was set up that involved the sequential low- and high-speed homogenization of rat skeletal muscle followed by KCl washing, Ca2+ loading and sucrose-density-gradient centrifugation. This protocol led to the separation of cell-surface membranes from membranes enriched in sarcoplasmic reticulum and intracellular GLUT4-containing vesicles. 3. Agglutination of cell-surface membranes using wheat-germ agglutinin allowed the isolation of thre
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24

Hedberg-Oldfors, Carola, Robert Meyer, Kay Nolte, et al. "Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles." Brain 143, no. 8 (2020): 2406–20. http://dx.doi.org/10.1093/brain/awaa206.

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Abstract The muscle specific isoform of the supervillin protein (SV2), encoded by the SVIL gene, is a large sarcolemmal myosin II- and F-actin-binding protein. Supervillin (SV2) binds and co-localizes with costameric dystrophin and binds nebulin, potentially attaching the sarcolemma to myofibrillar Z-lines. Despite its important role in muscle cell physiology suggested by various in vitro studies, there are so far no reports of any human disease caused by SVIL mutations. We here report four patients from two unrelated, consanguineous families with a childhood/adolescence onset of a myopathy as
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25

Iwata, Yuko, Yuki Katanosaka, Yuji Arai, Kazuo Komamura, Kunio Miyatake, and Munekazu Shigekawa. "A novel mechanism of myocyte degeneration involving the Ca2+-permeable growth factor–regulated channel." Journal of Cell Biology 161, no. 5 (2003): 957–67. http://dx.doi.org/10.1083/jcb.200301101.

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Disruption of the dystrophin–glycoprotein complex caused by genetic defects of dystrophin or sarcoglycans results in muscular dystrophy and/or cardiomyopathy in humans and animal models. However, the key early molecular events leading to myocyte degeneration remain elusive. Here, we observed that the growth factor–regulated channel (GRC), which belongs to the transient receptor potential channel family, is elevated in the sarcolemma of skeletal and/or cardiac muscle in dystrophic human patients and animal models deficient in dystrophin or δ-sarcoglycan. However, total cell GRC does not differ
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26

Halseth, Amy E., Deanna P. Bracy, and David H. Wasserman. "Functional limitations to glucose uptake in muscles comprised of different fiber types." American Journal of Physiology-Endocrinology and Metabolism 280, no. 6 (2001): E994—E999. http://dx.doi.org/10.1152/ajpendo.2001.280.6.e994.

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Skeletal muscle glucose uptake requires delivery of glucose to the sarcolemma, transport across the sarcolemma, and the irreversible phosphorylation of glucose by hexokinase (HK) inside the cell. Here, a novel method was used in the conscious rat to address the roles of these three steps in controlling the rate of glucose uptake in soleus, a muscle comprised of type I fibers, and two muscles comprised of type II fibers. Experiments were performed on conscious rats under basal conditions or during hyperinsulinemic euglycemic clamps. Rats received primed, constant infusions of 3- O-methyl-[3H]gl
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27

Cui, Chang-Hao, Taro Uyama, Kenji Miyado, et al. "Menstrual Blood-derived Cells Confer Human Dystrophin Expression in the Murine Model of Duchenne Muscular Dystrophy via Cell Fusion and Myogenic Transdifferentiation." Molecular Biology of the Cell 18, no. 5 (2007): 1586–94. http://dx.doi.org/10.1091/mbc.e06-09-0872.

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Duchenne muscular dystrophy (DMD), the most common lethal genetic disorder in children, is an X-linked recessive muscle disease characterized by the absence of dystrophin at the sarcolemma of muscle fibers. We examined a putative endometrial progenitor obtained from endometrial tissue samples to determine whether these cells repair muscular degeneration in a murine mdx model of DMD. Implanted cells conferred human dystrophin in degenerated muscle of immunodeficient mdx mice. We then examined menstrual blood–derived cells to determine whether primarily cultured nontransformed cells also repair
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28

Rezniczek, Günther A., Patryk Konieczny, Branislav Nikolic та ін. "Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with β-dystroglycan". Journal of Cell Biology 176, № 7 (2007): 965–77. http://dx.doi.org/10.1083/jcb.200604179.

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In skeletal muscle, the cytolinker plectin is prominently expressed at Z-disks and the sarcolemma. Alternative splicing of plectin transcripts gives rise to more than eight protein isoforms differing only in small N-terminal sequences (5–180 residues), four of which (plectins 1, 1b, 1d, and 1f) are found at substantial levels in muscle tissue. Using plectin isoform–specific antibodies and isoform expression constructs, we show the differential regulation of plectin isoforms during myotube differentiation and their localization to different compartments of muscle fibers, identifying plectins 1
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29

Peng, H. B., and Q. Chen. "Induction of dystrophin localization in cultured Xenopus muscle cells by latex beads." Journal of Cell Science 103, no. 2 (1992): 551–63. http://dx.doi.org/10.1242/jcs.103.2.551.

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The distribution of dystrophin in Xenopus myotomal muscle cells was examined in conventional and confocal immunofluorescence microscopy. By labeling dissociated single muscle fibers with a monoclonal or a polyclonal antibody against dystrophin, we found that dystrophin is ten times more concentrated at the myotendinous junction (MTJ) than at the extrajunctional sarcolemma. At the MTJ, dystrophin lines the membrane invaginations where myofibrils attach to the membrane. It is colocalized with talin, but is not related to the distribution of acetylcholine receptors (AChRs) which are clustered at
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30

Randazzo, Davide, Emiliana Giacomello, Stefania Lorenzini, et al. "Obscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity." Journal of Cell Biology 200, no. 4 (2013): 523–36. http://dx.doi.org/10.1083/jcb.201205118.

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Obscurin is a large myofibrillar protein that contains several interacting modules, one of which mediates binding to muscle-specific ankyrins. Interaction between obscurin and the muscle-specific ankyrin sAnk1.5 regulates the organization of the sarcoplasmic reticulum in striated muscles. Additional muscle-specific ankyrin isoforms, ankB and ankG, are localized at the subsarcolemma level, at which they contribute to the organization of dystrophin and β-dystroglycan at costameres. In this paper, we report that in mice deficient for obscurin, ankB was displaced from its localization at the M ban
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31

Duncan, C. J., and N. Shamsadeen. "Sarcolemma blebs and cell damage in mammalian skeletal muscle." Tissue and Cell 21, no. 2 (1989): 211–17. http://dx.doi.org/10.1016/0040-8166(89)90066-9.

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32

Bkaily, Ghassan, Sanaa Choufani, Sawsan Sader, et al. "Activation of sarcolemma and nuclear membranes ET-1 receptors regulates transcellular calcium levels in heart and vascular smooth muscle cells." Canadian Journal of Physiology and Pharmacology 81, no. 6 (2003): 654–62. http://dx.doi.org/10.1139/y03-020.

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The use of an ET-1 fluorescent probe in human heart and vascular smooth muscle cells showed that ET-1 receptors are present at both the sarcolemma and nuclear envelope membranes. The use of immunofluorescence studies showed that the ETA receptor was mainly present at the sarcolemma and cytosolic levels. However, the ETB receptor was present at the sarcolemma and the cytosol, as well as the nuclear envelope membranes and the nucleoplasm. In addition, ET-1 immunoreactivity was seen in the cytosol and the nucleus. Using Ca2+fluorescent probes such as Fluo-3, Indo 1, and yellow cameleon, as well a
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33

Duclos, Franck, Volker Straub, Steven A. Moore та ін. "Progressive Muscular Dystrophy in α-Sarcoglycan–deficient Mice". Journal of Cell Biology 142, № 6 (1998): 1461–71. http://dx.doi.org/10.1083/jcb.142.6.1461.

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Limb-girdle muscular dystrophy type 2D (LGMD 2D) is an autosomal recessive disorder caused by mutations in the α-sarcoglycan gene. To determine how α-sarcoglycan deficiency leads to muscle fiber degeneration, we generated and analyzed α-sarcoglycan– deficient mice. Sgca-null mice developed progressive muscular dystrophy and, in contrast to other animal models for muscular dystrophy, showed ongoing muscle necrosis with age, a hallmark of the human disease. Sgca-null mice also revealed loss of sarcolemmal integrity, elevated serum levels of muscle enzymes, increased muscle masses, and changes in
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34

Straub, Volker, Jill A. Rafael, Jeffrey S. Chamberlain, and Kevin P. Campbell. "Animal Models for Muscular Dystrophy Show Different Patterns of Sarcolemmal Disruption." Journal of Cell Biology 139, no. 2 (1997): 375–85. http://dx.doi.org/10.1083/jcb.139.2.375.

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Genetic defects in a number of components of the dystrophin–glycoprotein complex (DGC) lead to distinct forms of muscular dystrophy. However, little is known about how alterations in the DGC are manifested in the pathophysiology present in dystrophic muscle tissue. One hypothesis is that the DGC protects the sarcolemma from contraction-induced damage. Using tracer molecules, we compared sarcolemmal integrity in animal models for muscular dystrophy and in muscular dystrophy patient samples. Evans blue, a low molecular weight diazo dye, does not cross into skeletal muscle fibers in normal mice.
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35

Shear, C. R., and R. J. Bloch. "Vinculin in subsarcolemmal densities in chicken skeletal muscle: localization and relationship to intracellular and extracellular structures." Journal of Cell Biology 101, no. 1 (1985): 240–56. http://dx.doi.org/10.1083/jcb.101.1.240.

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Using immunocytochemical methods we have studied the distribution of vinculin in the anterior and posterior latissimus dorsi skeletal (ALD and PLD, respectively) muscles of the adult chicken. The ALD muscle is made up of both tonic (85%) and twitch (15%) myofibers, and the PLD muscle is made up entirely of twitch myofibers. In indirect immunofluorescence, antivinculin antibodies stained specific regions adjacent to the sarcolemma of the ALD and PLD muscles. In the central and myotendinous regions of the ALD, staining of the tonic fibers was intense all around the fiber periphery. Staining of t
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36

Iyer, Shama R., Sameer B. Shah, Christopher W. Ward, et al. "Differential YAP nuclear signaling in healthy and dystrophic skeletal muscle." American Journal of Physiology-Cell Physiology 317, no. 1 (2019): C48—C57. http://dx.doi.org/10.1152/ajpcell.00432.2018.

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Mechanical forces regulate muscle development, hypertrophy, and homeostasis. Force-transmitting structures allow mechanotransduction at the sarcolemma, cytoskeleton, and nuclear envelope. There is growing evidence that Yes-associated protein (YAP) serves as a nuclear relay of mechanical signals and can induce a range of downstream signaling cascades. Dystrophin is a sarcolemma-associated protein, and its absence underlies the pathology in Duchenne muscular dystrophy. We tested the hypothesis that the absence of dystrophin in muscle would result in reduced YAP signaling in response to loading.
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37

Lynch, Gordon S., Jill A. Rafael, Jeffrey S. Chamberlain, and John A. Faulkner. "Contraction-induced injury to single permeabilized muscle fibers from mdx, transgenic mdx, and control mice." American Journal of Physiology-Cell Physiology 279, no. 4 (2000): C1290—C1294. http://dx.doi.org/10.1152/ajpcell.2000.279.4.c1290.

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Muscle fibers of mdx mice that lack dystrophin are more susceptible to contraction-induced injury, particularly when stretched. In contrast, transgenic mdx (tg -mdx) mice, which overexpress dystrophin, show no morphological or functional signs of dystrophy. Permeabilization disrupts the sarcolemma of fibers from muscles of mdx, tg- mdx, and control mice. We tested the null hypothesis stating that, after single stretches of maximally activated single permeabilized fibers, force deficits do not differ among fibers from extensor digitorum longus muscles of mdx, tg -mdx, or control mice. Fibers we
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38

Lovering, Richard M., Andrea O'Neill, Joaquin M. Muriel, Benjamin L. Prosser, John Strong, and Robert J. Bloch. "Physiology, structure, and susceptibility to injury of skeletal muscle in mice lacking keratin 19-based and desmin-based intermediate filaments." American Journal of Physiology-Cell Physiology 300, no. 4 (2011): C803—C813. http://dx.doi.org/10.1152/ajpcell.00394.2010.

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Intermediate filaments, composed of desmin and of keratins, play important roles in linking contractile elements to each other and to the sarcolemma in striated muscle. Our previous results show that the tibialis anterior (TA) muscles of mice lacking keratin 19 (K19) lose costameres, accumulate mitochondria under the sarcolemma, and generate lower specific tension than controls. Here we compare the physiology and morphology of TA muscles of mice lacking K19 with muscles lacking desmin or both proteins [double knockout (DKO)]. K19−/− mice and DKO mice showed a threefold increase in the levels o
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Crosbie, Rachelle H., Connie S. Lebakken, Kathleen H. Holt, et al. "Membrane Targeting and Stabilization of Sarcospan Is Mediated by the Sarcoglycan Subcomplex." Journal of Cell Biology 145, no. 1 (1999): 153–65. http://dx.doi.org/10.1083/jcb.145.1.153.

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The dystrophin–glycoprotein complex (DGC) is a multisubunit complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. The proteins of the DGC are structurally organized into distinct subcomplexes, and genetic mutations in many individual components are manifested as muscular dystrophy. We recently identified a unique tetraspan-like dystrophin-associated protein, which we have named sarcospan (SPN) for its multiple sarcolemma spanning domains (Crosbie, R.H., J. Heighway, D.P. Venzke, J.C. Lee, and K.P. Campbell. 1997. J. Biol.
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40

Kahn, A. M., J. C. Allen, and H. Shelat. "Na+-Ca2+ exchange in sarcolemmal vesicles from bovine superior mesenteric artery." American Journal of Physiology-Cell Physiology 254, no. 3 (1988): C441—C449. http://dx.doi.org/10.1152/ajpcell.1988.254.3.c441.

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These studies were designed to determine whether a Na+-Ca2+ exchanger is present in sarcolemmal vesicles from bovine superior mesenteric artery and, if so, to determine whether this transport system is qualitatively similar to that found in other excitable tissues. Vesicles, preferentially enriched in sarcolemma, were prepared by a Mg2+ aggregation and differential centrifugation technique. An inwardly directed Ca2+ gradient stimulated 22Na+ efflux and an outwardly directed Ca2+ gradient stimulated 22Na+ uptake. Similarly, an inwardly directed Na+ gradient stimulated 45Ca2+ efflux, and an outw
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41

Gallant, E. M., and L. R. Lentz. "Excitation-contraction coupling in pigs heterozygous for malignant hyperthermia." American Journal of Physiology-Cell Physiology 262, no. 2 (1992): C422—C426. http://dx.doi.org/10.1152/ajpcell.1992.262.2.c422.

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A defect in the skeletal muscle sarcoplasmic reticulum (SR) calcium release channel of malignant hyperthermia-susceptible (MHS) pigs greatly enhances SR calcium release in pigs homozygous for the malignant hyperthermia (MH) gene. In pigs heterozygous at this locus, rates of calcium release from isolated SR stimulated by Ca2+, ATP, or caffeine are intermediate to those of both MHS and normal SR [Mickelson et al. Am. J. Physiol. 257 (Cell Physiol. 26): C787-C794, 1989]. In this study bundles of intact muscle cells dissected from pigs of various genotypes were used to examine the effects of the M
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42

van der Poel, Chris, Joshua N. Edwards, William A. Macdonald, and D. George Stephenson. "Mitochondrial superoxide production in skeletal muscle fibers of the rat and decreased fiber excitability." American Journal of Physiology-Cell Physiology 292, no. 4 (2007): C1353—C1360. http://dx.doi.org/10.1152/ajpcell.00469.2006.

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Mammalian skeletal muscles generate marked amounts of superoxide (O2·−) at 37°C, but it is not well understood which is the main source of O2·− production in the muscle fibers and how this interferes with muscle function. To answer these questions, O2·− production and twitch force responses were measured at 37°C in mechanically skinned muscle fibers of rat extensor digitorum longus (EDL) muscle. In mechanically skinned fibers, the sarcolemma is removed avoiding potential sources of O2·− production that are not intrinsically part of the muscle fibers, such as nerve terminals, blood cells, capil
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43

Nguyen, T. M., J. M. Ellis, D. R. Love, et al. "Localization of the DMDL gene-encoded dystrophin-related protein using a panel of nineteen monoclonal antibodies: presence at neuromuscular junctions, in the sarcolemma of dystrophic skeletal muscle, in vascular and other smooth muscles, and in proliferating brain cell lines." Journal of Cell Biology 115, no. 6 (1991): 1695–700. http://dx.doi.org/10.1083/jcb.115.6.1695.

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mAbs have been raised against different epitopes on the protein product of the DMDL gene, which is an autosomal homologue of the X-linked DMD gene for dystrophin. These antibodies provide direct evidence that DMDL protein is localized near acetylcholine receptors at neuromuscular junctions in normal and mdx mouse intercostal muscle. The primary location in tissues other than skeletal muscle is smooth muscle, especially in the vascular system, which may account for the wide tissue distribution previously demonstrated by Western blotting. The DMDL protein was undetectable in the nonjunctional sa
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CHEN, Yun-Ju, Heather J. SPENCE, Jacqueline M. CAMERON, Thomas JESS, Jane L. ILSLEY та Steven J. WINDER. "Direct interaction of β-dystroglycan with F-actin". Biochemical Journal 375, № 2 (2003): 329–37. http://dx.doi.org/10.1042/bj20030808.

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Dystroglycans are essential transmembrane adhesion receptors for laminin. α-Dystroglycan is a highly glycosylated extracellular protein that interacts with laminin in the extracellular matrix and the transmembrane region of β-dystroglycan. β-Dystroglycan, via its cytoplasmic tail, interacts with dystrophin and utrophin and also with the actin cytoskeleton. As a part of the dystrophin–glycoprotein complex of muscles, dystroglycan is also important in maintaining sarcolemmal integrity. Mutations in dystrophin that lead to Duchenne muscular dystrophy also lead to a loss of dystroglycan from the s
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45

CIECIERSKA, ANNA, TOMASZ SADKOWSKI, and TOMASZ MOTYL. "Role of satellite cells in growth and regeneration of skeletal muscles." Medycyna Weterynaryjna 75, no. 11 (2019): 6349–2019. http://dx.doi.org/10.21521/mw.6349.

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Postnatal growth and regeneration capacity of skeletal muscles is dependent mainly on adult muscle stem cells called satellite cells. Satellite cells are quiescent mononucleated cells that are normally located outside the sarcolemma within the basal lamina of the muscle fiber. Their activation, which results from injury, is manifested by mobilization, proliferation, differentiation and, ultimately, fusion into new muscle fibers. The satellite cell pool is responsible for the remarkable regenerative capacity of skeletal muscles. Moreover, these cells are capable of self-renewal and can give ris
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46

Peters, Matthew F., Hélène M. Sadoulet-Puccio, R. Mark Grady та ін. "Differential Membrane Localization and Intermolecular Associations of α-Dystrobrevin Isoforms in Skeletal Muscle". Journal of Cell Biology 142, № 5 (1998): 1269–78. http://dx.doi.org/10.1083/jcb.142.5.1269.

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α-Dystrobrevin is both a dystrophin homologue and a component of the dystrophin protein complex. Alternative splicing yields five forms, of which two predominate in skeletal muscle: full-length α-dystrobrevin-1 (84 kD), and COOH-terminal truncated α-dystrobrevin-2 (65 kD). Using isoform-specific antibodies, we find that α-dystrobrevin-2 is localized on the sarcolemma and at the neuromuscular synapse, where, like dystrophin, it is most concentrated in the depths of the postjunctional folds. α-Dystrobrevin-2 preferentially copurifies with dystrophin from muscle extracts. In contrast, α-dystrobre
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47

Hansen, O., and T. Clausen. "Quantitative determination of Na+-K+-ATPase and other sarcolemmal components in muscle cells." American Journal of Physiology-Cell Physiology 254, no. 1 (1988): C1—C7. http://dx.doi.org/10.1152/ajpcell.1988.254.1.c1.

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A recurring problem in the characterization of plasma membrane enzymes in tissues and cells is whether the samples tested are representative for the entire population of enzyme molecules present in the starting material. Measurements of [3H]-ouabain binding, enzyme activity, and maximum transport capacity all indicate that the concentration of Na+-K+ pumps in mammalian skeletal muscle is high (300-800 pmol/g wet wt). Studies on Na+-K+-ATPase activity in isolated sarcolemma, however, generally give little or no information on total cellular enzyme concentration. Due to the low and variable enzy
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48

Nakada, Satoshi, Yuri Yamashita, Shuichi Machida, Yuko Miyagoe-Suzuki, and Eri Arikawa-Hirasawa. "Perlecan Facilitates Neuronal Nitric Oxide Synthase Delocalization in Denervation-Induced Muscle Atrophy." Cells 9, no. 11 (2020): 2524. http://dx.doi.org/10.3390/cells9112524.

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Perlecan is an extracellular matrix molecule anchored to the sarcolemma by a dystrophin–glycoprotein complex. Perlecan-deficient mice are tolerant to muscle atrophy, suggesting that perlecan negatively regulates mechanical stress-dependent skeletal muscle mass. Delocalization of neuronal nitric oxide synthase (nNOS) from the sarcolemma to the cytosol triggers protein degradation, thereby initiating skeletal muscle atrophy. We hypothesized that perlecan regulates nNOS delocalization and activates protein degradation during this process. To determine the role of perlecan in nNOS-mediated mechano
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49

Gayeski, T. E., and C. R. Honig. "O2 gradients from sarcolemma to cell interior in red muscle at maximal VO2." American Journal of Physiology-Heart and Circulatory Physiology 251, no. 4 (1986): H789—H799. http://dx.doi.org/10.1152/ajpheart.1986.251.4.h789.

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The intracellular distribution of O2 in cross sections of dog gracilis muscles was determined by myoglobin (Mb) cryospectrophotometry. The volume sampled by the photometer was approximately 30 micron3 and contained 1-2 mitochondria. Measurements could be made to within 3 micron of capillaries without interference from hemoglobin. Mb saturation was uniform at all loci examined when respiration was blocked with cyanide. During twitch contraction at maximum O2 consumption, saturations within a cell cross section varied by up to 20%. The corresponding difference in partial pressure of O2 (PO2) was
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Zhou, Daixing, Jeanine A. Ursitti, and Robert J. Bloch. "Developmental Expression of Spectrins in Rat Skeletal Muscle." Molecular Biology of the Cell 9, no. 1 (1998): 47–61. http://dx.doi.org/10.1091/mbc.9.1.47.

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Skeletal muscle contains spectrin (or spectrin I) and fodrin (or spectrin II), members of the spectrin supergene family. We used isoform-specific antibodies and cDNA probes to investigate the molecular forms, developmental expression, and subcellular localization of the spectrins in skeletal muscle of the rat. We report that β-spectrin (βI) replaces β-fodrin (βII) at the sarcolemma as skeletal muscle fibers develop. As a result, adult muscle fibers contain only α-fodrin (αII) and the muscle isoform of β-spectrin (βIΣ2). By contrast, other types of cells present in skeletal muscle tissue, inclu
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