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Relevant bibliographies by topics / Muscle cell sarcolemma

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Academic literature on the topic 'Muscle cell sarcolemma'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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Journal articles on the topic "Muscle cell sarcolemma"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Muscle cell sarcolemma"

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Piper, Tony Andrew. "A study of the transfer of recombinant dystrophin genes into skeletal muscle cells." Thesis, Royal Holloway, University of London, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.286683.

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Nichol, James A. "The mechanical properties of sarcolemmal vesicles from rabbit muscle : the effects of internal calcium and membrane active molecules." Thesis, University of Glasgow, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266185.

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Zhang, Jing. "Sarcoplasmic reticulum ATPase and sarcolemmal calcium(2+)-ATPase messenger RNA expression during in vitro skeletal muscle cell differentiation." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ32292.pdf.

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Zhang, Jing. "Sarcoplasmic reticulum ATPase and sarcolemmal calcium(2+)-ATPase messenger RNA expression during in vitro skeletal muscle cell differentiation." 1997. http://hdl.handle.net/1993/1381.

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Three genes coding sarcoplasmic reticulum Ca$\sp{2+}$-ATPases (SERCA) and at least four genes coding sarcolemmal Ca$\sp{2+}$-ATPase (PMCA) have been isolated and characterized. The objective of this work was to study the mRNA expression for Ca$\sp{2+}$-ATPase isoforms during in vitro differentiation of skeletal muscle cell lines. To analyze the mRNA expression pattern of the SERCA and PMCA isoforms, three skeletal muscle cell lines (L6, C2C12, Sol8) were used as models. The mRNAs of these Ca$\sp{2+}$-ATPase gene were detected by a semi-quantitatively RT-PCR technique. It is generally regarded

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Books on the topic "Muscle cell sarcolemma"

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1948-, Mrak Robert E., ed. Muscle membranes in diseases of muscle. CRC Press, 1985.

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Book chapters on the topic "Muscle cell sarcolemma"

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Aickin, C. Claire. "Chloride Transport across the Sarcolemma of Vertebrate Smooth and Skeletal Muscle." In Chloride Channels and Carriers in Nerve, Muscle, and Glial Cells. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4757-9685-8_7.

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Lunze, K., J. Stålhand, and S. Leonhardt. "Modeling of Stretch-Activated Sarcolemmal Channels in Smooth Muscle Cells." In IFMBE Proceedings. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03882-2_197.

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Hanna, Michael G., and Enrico Bugiardini. "Structure and function of muscle." In Oxford Textbook of Medicine, edited by Christopher Kennard. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0608.

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The motor unit—the final common pathway for all voluntary muscle activity—is composed of an anterior horn cell, its peripheral axon, the axon terminal branches, the associated neuromuscular junctions, and the muscle fibres innervated. The muscle cells are multinucleate units with unique structures adapted for response to metabolic, nervous, and autocrine signals. Meanwhile, there are also different types of motor units: type 1—rich in mitochondria and specialized for oxidative metabolism of fat; type 2—larger fibres with abundant glycogen that generate energy by glycosis and are critical for short-lived muscle contraction. Knowledge of the underlying molecular cell biology, neurophysiology, and biochemical energetics of muscle provides a useful basis for understanding the symptoms, signs, and pathogenesis of clinical disorders affecting the muscles. Mutations in sarcolemmal proteins, such as dystrophin, cause diseases with widespread effects on skeletal muscle function, the heart, and survival.

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Conference papers on the topic "Muscle cell sarcolemma"

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García-Pelagio, Karla P., Robert J. Bloch, Alicia Ortega, and Hugo González-Serratos. "Elastic Properties of the Sarcolemma-Costamere Complex of Muscle Cells in Normal Mice." In MEDICAL PHYSICS: Ninth Mexican Symposium on Medical Physics. AIP, 2006. http://dx.doi.org/10.1063/1.2356399.

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