DOCSLIB.ORG

217 a ABL Tyrosine Kinases, 193 Actin-Binding Proteins, 16–21, 24, 52, 102, 123, 125, 132, 189, 202 Actin Cytoskeleton, 13, 16

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
217 a ABL Tyrosine Kinases, 193 Actin-Binding Proteins, 16–21, 24, 52, 102, 123, 125, 132, 189, 202 Actin Cytoskeleton, 13, 16 Index A Adhesions, 1, 2, 7, 13, 14, 18, 19, 24, 29, ABL tyrosine kinases, 193 30, 57, 60, 64, 66, 90, 94, 95, 99–101, Actin-binding proteins, 16–21, 24, 52, 102, 105–112, 121–123, 125, 127–136, 153, 123, 125, 132, 189, 202 169, 177, 180, 185–196, 198, 200, 203, Actin cytoskeleton, 13, 16–19, 24, 28, 29, 44, 204, 213, 214 47, 52, 69, 72, 84, 91, 93, 94, 98, Adhesion structures, 30, 37–52, 108, 112, 123, 101–106, 108, 123, 125, 128, 130, 132, 127–129, 195 158, 169, 177, 180, 185–187, 189, 190, Adhesive functions, 7, 48, 108–110, 185, 191, 192–197, 203–205 192, 195 Actin-depolymerizing factor(ADF), 17–18. Adhesive interactions, 1–4, 10, 13, 44, See also Cofilin 57–112, 130, 185–205, 213–215 Actin dynamics, 19, 126, 193, 194 Afadin, 189 Actin filaments, 13–26, 28–30, 37, 40, Affinity, 16, 47, 48, 50, 100, 109, 134, 192 42, 44, 45, 47, 49, 50, 52, 66, 69, Alpha-actinin, 18, 47, 106, 189 71, 72, 78, 80, 87, 88, 99, 102–104, Alpha-catenin, 18, 127, 189, 194, 195, 198, 204 106, 109, 123–130, 133, 151, 154, Alpha-tubulin, 25 158, 178–181, 186, 187, 190, Alterations, 2–4, 13, 57, 74–88, 104, 105, 193–196, 203 108–112, 121, 132–135, 169, 177, 180, Actin polymerization, 13, 14, 16, 18, 185, 200–204, 213, 214 21, 24, 49, 103, 104, 123, 124, AMF. See Autocrine motility factor (AMF) 126, 127, 193 Anaplasia, 185, 205, 213 Actin-related proteins (Arp2/3), 16, 18, 19, Anchorage dependence, 2, 99–100 21, 23, 52, 103, 104, 123–125, 127, Anchorage independence, 4, 57, 111–112 193, 194 Angiogenesis, 48, 52, 90, 112, 131, 135, Activation, 19, 24, 47, 48, 50, 57, 88–93, 136, 214 96–100, 103–106, 109–112, 125–127, Anoikis, 2, 57, 99, 100, 106, 108, 111, 112 129–134, 136, 177, 190, 192–194, Anti-apoptotic signaling, 97–100, 111, 204 198–205, 214 APC. See Adenomatous polyposis coli (APC) Active cell edge, 24, 80, 125, 127, 128, protein 133, 134 Apoptosis, 2, 3, 57, 94, 97–100, 105, 106, 108, Actomyosin, 19, 49, 51, 108 111, 152, 202 ADAM proteins, 48, 50 Arginylation, 13, 14 Adenomatous polyposis coli (APC) protein, Arg kinase, 193 28, 126, 195, 198, 204 Arp2/3. See Actin-related proteins (Arp2/3) ADF. See Actin-depolymerizing factor (ADF) Asef. See Rac1-activating protein (Asef) Adherens junctions, 185–205 Assembling, 24, 52, 193 Y.A. Rovensky, Adhesive Interactions in Normal and Transformed Cells, 217 DOI 10.1007/978-1-61779-304-2, © Springer Science+Business Media, LLC 2011 218 Index ATP hydrolysis, 19 Cancer progression, 112, 198, 201, 202, 204, 205 Attachment, 2, 9, 10, 21, 24, 37, 42, 44, 57, Capping, 16–18, 21, 103, 124, 191, 2344 69, 106, 109, 122, 124, 130, 136, 145, Cas. See P130 Cas (Cas) protein 148, 151, 177, 214 Cas-associated protein, 95 Autocrine motility factor (AMF), 137 Casein kinase1, 198 Autophagy, 100 Catastrophe frequency, 50 Axin, 198, 204, 205 Catenin complex, 187–189, 194, 195, Axin/conductin, 198, 204, 205 201–204, 215 Catenins, 187, 189, 193, 195, 196, 203–204 Caveolae, 99 B Caveolin–1, 99 Bad protein, 98, 99 Cdc42, 101, 104–105, 124, 126, 129, 133, 176, Barbed ends, 17–19, 21, 23, 42, 44, 103, 104, 190, 193, 195, 196 106, 124, 129 CDH1 tumor suppressor gene, 200, 201 Basement membranes, 1, 2, 7–10, 51, 52, 112, Cell cultivation, 151 131, 135, 145, 147, 148, 153 Cell detachment, 97, 99, 100, 111 Bax protein, 98 Cell-extracellular matrix adhesion, 105, 108 BAX tumor suppressor gene, 98, 100 Cell length control, 71, 72 Bcl2 protein, 98 Cell motility, 18, 19, 49, 98, 130–132, 194, 196 BCL2 proto-oncogene, 98, 100 Cell receptors, 18, 88, 91, 110, 130, 135 Bcl 9–2 protein, 198, 205 Cell spreading, 19, 24, 37, 57–88, 107, 108, BCL-x, proto-oncogene, 98 148, 151, 154, 155, 157, 158, 167–171, Bcl-x protein, 98 173, 174, 178 Beta-catenin, 189–195, 197–205 Cell surface receptors, 7–9, 47, 57, 88–92, 94, Beta-tubulin, 25, 26 96, 111, 128, 129, 214 Blebs, 37, 42, 58, 60, 69, 80, 84, 87, 126 Cell surface relief, 57–62, 69, 72, 82–87 Bombesin, 136 Centrioles, 25 BPAG1, BP230. See Bullous pemphigoid Centripetal stretch, 49, 66, 78, 105, 106, 108, antigen1 (BPAG1, BP230) 109, 122, 178, 181 Bullous pemphigoid antigen1 (BPAG1, Centrosomal microtubules, 27 BP230), 51 Centrosome, 25, 27, 104, 126 Bundles, 14, 15, 18, 24, 28, 44, 45, 48, 51, c-ErbB1/HER1 proto-oncogene, 110 52, 66, 68, 70–72, 80, 82, 88, 102, 104, Chondroitin sulfates, 8 106, 107, 123–125, 128, 133, 151, 154, Claudins, 185, 186, 189 158, 178–181, 190, 193, 195, 196 Clustering, 47, 90, 109, 124, 192, 195 c-met proto-oncogene, 110, 136 Cobl. See Cordon-bleu (Cobl) C Cofilin, 17–19, 23, 24, 102, 103, 134. See also Cadherin isoform switching, 203 Actin-depolymerizing factor(ADF) Cadherin receptor, 129, 185, 187, 190–195 Colcemide, 28, 126 Calcium ions, 92 Colchicines, 28 Caldesmon, 19, 49, 52, 195 Collagen fibers, 9 Calmodulin, 92 Collagens, 1, 4, 8–10, 45, 48, 52, 90, 106, Calmodulin dependent protein kinases 107, 109, 112, 129, 135, 203 (CAM), 93 Collision, 121, 127, 195, 196, 200 Calpain, 48, 50 Conductin. See Axin/conductin Calpastatin, 48, 50 Conductin (Axil) tumor suppressor gene. CAM. See Calmodulin dependent protein See Axin/conductin kinases (CAM) Conformation, 19, 48, 88, 89, 91, 108, 186, cAMP. See Cyclic adenosine monophosphate 194, 199 (cAMP) Connective tissue, 2, 4, 7, 8, 10, 96, 145, 148–150 cAMP-dependent protein kinase, 93 Connexins, 186 Cancer cells, 10, 24, 51, 52, 108–112, 129, Connexon channels, 186 133–136, 154, 161, 200–205 Connexons, 186 Index 219 Contact guidance, 153 Dsh. See Dishevelled (Dsh) protein Contact inhibition, 2, 121, 127–128, 134, 185, Dynamic instability, 26–28, 50 196–200, 204–205 Dynamin, 50, 99, 131 Contact paralysis, 127, 128, 134, 194 Dynein, 27, 30, 104, 192 Contractility, 14, 19, 24, 29, 49–52, 105–107, 126, 127, 129, 133, 180, 193, 195, 203 Contraction, 19, 49, 80, 93, 107, 108, 130, E 186, 195 EB1. See End-binding protein1 (EB1) Cordon-bleu (Cobl), 16, 17 E-cadherin. See Epithelial cadherin Cortactin, 18, 21, 52, 123, 125, 193 (E-cadherin) Cortical actin, 18, 49, 126, 130, 192 EGF. See Epidermal growth factor (EGF) Curvature, 153–156, 158, 178–181 Elastin, 1, 8, 9 Cyclic adenosine monophosphate (cAMP), Elongation, 17, 21, 23, 122, 124, 152, 154, 16, 92, 93 158, 159, 179, 180 Cyclic nucleotides, 92 Embryogenesis, 2, 10, 121, 129, 151, 154, Cylindrical surface, 154, 163, 167, 179, 180 181, 185, 188 Cylindrical threads, 154, 158 EMT. See Epithelial-mesenchymal transition Cytochalasins, 84, 87 (EMT) Cytoskeleton, 2, 3, 13–30, 44, 45, 47, 52, 69, Enabled/vasodilator-stimulated 72, 84, 91, 93, 94, 98, 100–106, 108, phosphoprotein (Ena/VASP), 106 121, 123, 125, 128, 130, 132, 158, 169, Ena/VASP. See Enabled/vasodilator-stimulated 177, 180, 185–187, 189, 190, 192–197, phosphoprotein (Ena/VASP) 204, 205, 214 End-binding protein1 (EB1), 28 Cytoskeleton linkers, 30 Endocytic-exocytic transport, 131, 134 Endocytosis, 19, 50, 99, 191, 192, 202, 204 Endothelium, 2, 4, 90, 96, 109, 214 D Entactins, 9 DAG. See Diacylglycerol (DAG) Epidermal growth factor (EGF), 90, 96, 110, DAP. See Death-associated protein (DAP) 130, 132, 136 Death-associated protein (DAP), 99 Epithelial cadherin (E-cadherin), 129, 135, 187, Deletions, 105, 111, 201 188, 191–195, 198, 200–205, 214, 215 Depolymerization, 14, 16, 17, 23, 24, 26–29, Epithelial cells, 4, 7, 9, 14, 29, 30, 51, 58, 64, 49, 87, 102, 103, 126 66, 69, 71, 72, 74, 78, 80, 88, 90, 100, Dermatan sulfates, 8 122, 127–129, 131, 133, 134, 145, 154, Desmocollins, 186 158, 161, 163, 167–170, 172, 174, Desmoglein, 186 177–181, 187, 188, 191, 193, 195, 196, Desmoplakin, 187, 205 198, 200, 202, 203 Desmosomal cadherins, 186 Epithelial-mesenchymal transition (EMT), Desmosomal junctions. See Desmosomes 129, 135, 136, 198, 202–204, 214 (desmosomal junctions) Epitheliocytes. See Epithelial cells Desmosomes (desmosomal junctions), Epithelium, 29, 128 30, 185–187, 189, 202, 205 ERK. See Extracellular signal-regulated Desmuslin, 30 kinases (ERK) Detachment, 4, 40, 57, 60, 63, 97, 99, 100, ERM. See Ezrin, radixin, moezin (ERM) 111, 122, 126, 130, 170 Exocytosis, 131, 191 Diacylglycerol (DAG), 92, 94 Expression, 3, 10, 17, 24, 30, 48, 50, 91, 93, Disassembly, 17, 23, 29, 48–50, 94, 101, 104, 94, 96, 100, 105, 106, 109, 110, 125, 109, 129–132, 186, 191, 193, 203, 204 128, 129, 135, 136, 153, 180, 198, Discontinuous substrata, 154, 167–176 200–205, 214 Dishevelled (Dsh) protein, 198 Extracellular matrix, 1, 7–10, 13, 37, 57–112, Disintegrin domain, 48 121, 145, 153, 200, 213 Domain, 8–10, 16–19, 23, 45, 47, 48, 52, Extracellular signal-regulated kinases 89–93, 95, 96, 99, 100, 108, 109, 123, (ERK), 96 185, 187, 189, 191–193, 197 Ezrin, radixin, moezin (ERM), 18 220 Index F G F-actin, 13 G-actin. See Globular actin (G-actin) FAK. See Focal adhesion kinase (FAK) Gamma-catenin (g-catenin ), 187, 189 Fascin, 18, 124, 129 Gamma-tubulin (g-tubulin ), 25, 27 FGF. See Fibroblast growth factor (FGF) Gap junctions, 185, 186 Fibers, 1, 2, 9, 18, 40, 145, 147–150, 153 GAPs. See GTPase activating proteins (GAPs) Fibrillar adhesions, 37, 44, 51 GDI.
Load more

Recommended publications
  • Structural Biology of the Dystrophin-Deficient Muscle Fiber
    Dystrophin-deficient muscle fiber REVIEW ISSN- 0102-9010145 STRUCTURAL BIOLOGY OF THE DYSTROPHIN-DEFICIENT MUSCLE FIBER Maria Julia Marques Department of Anatomy, Institute of Biology, State University of Campinas (UNICAMP), Campinas, SP, Brazil. ABSTRACT The discovery of dystrophin and its gene has led to major advances in our understanding of the molecular basis of Duchenne, Becker and other muscular dystrophies related to the dystrophin-associated protein complex. The concept that dystrophin has a mechanical function in stabilizing the muscle fiber membrane has expanded in the last five years. The dystrophin-glycoprotein complex is now considered a multifunctional complex that contains molecules involved in signal transduction cascades important for cell survival. The roles of dystrophin and the dystrophin- glycoprotein complex in positioning and anchoring receptors and ion channels is also important, and much of what is known about these functions is based on studies of the neuromuscular synapse. In this review, we discuss the components and the cellular signaling molecules associated with the dystrophin-glycoprotein complex. We then focus on the molecular organization of the neuromuscular junction and its structural organization in the dystrophin-deficient muscle fibers of mdx mice, a well-established experimental model of Duchenne muscular dystrophy. Key words: Confocal microscopy, Duchenne muscular dystrophy, mdx, neuromuscular junction INTRODUCTION that can improve the quality of life of the patients, Duchenne muscular dystrophy (DMD) is an X- death usually occurs in the early twenties, as a result linked recessive, progressive muscle-wasting disease of cardiac and/or respiratory failures [24]. that affects primarily skeletal and cardiac muscle. Several other muscular dystrophies have been DMD was first reported in 1868 by Dr.
    [Show full text]
  • Typology and Profile of Spine Muscles. Structure of Myofibrils and Role of Protein Components – Review of Current Literature
    Ovidius University Annals, Series Physical Education and Sport / SCIENCE, MOVEMENT AND HEALTH Vol. XI, ISSUE 2 Supplement, 2011, Romania The JOURNAL is nationally acknowledged by C.N.C.S.I.S., being included in the B+ category publications, 2008-2011. The journal is indexed in: Ebsco, SPORTDiscus, INDEX COPERNICUS JOURNAL MASTER LIST, DOAJ DIRECTORY OF OPEN ACCES JOURNALS, Caby, Gale Cengace Learning TYPOLOGY AND PROFILE OF SPINE MUSCLES. STRUCTURE OF MYOFIBRILS AND ROLE OF PROTEIN COMPONENTS – REVIEW OF CURRENT LITERATURE STRATON ALEXANDRU1, ENE-VOICULESCU CARMEN1, GIDU DIANA1, PETRESCU ANDREI1 Abstract. Muscular profile of spine muscles has a great importance in trunk stability. It seems that muscles which support the spine show a high content of red muscle fiber with a cross section area equal or higher than white muscle fibers. It is possible that lumbar extensor muscles to have different functional capacity between sexes. Most of the myofibril structural proteins except protein actin and protein myosin have a role in maintaining the structural integrity of muscle cell. Key words: muscle, fibres, myofibrils, proteins, spine. thoracic muscle structure lying superficial and deep is Introduction composed of 74% type I fibers, lumbar muscle Proper understanding of muscle fibers profile of structure located superficially is composed of 57% muscles supporting the spine and the role of muscle type I fibers and lumbar muscle structure located deep cell structural proteins leads to better achievements in is composed of 63% type I fibers. Type I muscle fiber performance training and rehabilitation. diameter is significantly larger than that of type II fibers. Another study, conducted on 42 patients Muscle fibers typology divided into two groups - 21 patients with lumbar Skeletal muscle contains two major types of back pain and 21 patients without lumbar back pain muscle fibers: slow twitch red or type I fibers) and almost identical groups as gender, age and body mass fast twitch white or type II fibers).
    [Show full text]
  • Syncoilin Modulates Peripherin Filament Networks and Is Necessary for Large-Calibre Motor Neurons
    Research Article 2543 Syncoilin modulates peripherin filament networks and is necessary for large-calibre motor neurons W. Thomas Clarke1,*, Ben Edwards1,*, Karl J. A. McCullagh1,‡, Matthew W. Kemp1,§, Catherine Moorwood1,¶, Diane L. Sherman2, Matthew Burgess1,** and Kay E. Davies1,‡‡ 1MRC Functional Genomics Unit, Department of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford, OX1 3PT, UK 2Centre for Neuroscience Research, The University of Edinburgh, Summerhall, Edinburgh, EH9 1QH, UK *These authors contributed equally to this work ‡Present address: Regenerative Medicine Institute, National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Ireland §Present address: School of Women’s and Infants’ Health, Faculty of Medicine, Dentistry and Health Sciences, The University of Western Australia, Western Australia, WA 6009 ¶Present address: Department of Physiology and Pennsylvania Muscle Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA **Present address: Botnar Research Centre, Institute of Musculoskeletal Sciences, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford OX3 7LD, UK ‡‡Author for correspondence ([email protected]) Accepted 20 April 2010 Journal of Cell Science 123, 2543-2552 © 2010. Published by The Company of Biologists Ltd doi:10.1242/jcs.059113 Summary Syncoilin is an atypical type III intermediate filament (IF) protein, which is expressed in muscle and is associated with the dystrophin- associated protein complex. Here, we show that syncoilin is expressed in both the central and peripheral nervous systems. Isoform Sync1 is dominant in the brain, but isoform Sync2 is dominant in the spinal cord and sciatic nerve. Peripherin is a type III IF protein that has been shown to colocalise and interact with syncoilin.
    [Show full text]
  • The Toxic Effect of R350P Mutant Desmin in Striated Muscle of Man and Mouse
    Acta Neuropathol (2015) 129:297–315 DOI 10.1007/s00401-014-1363-2 ORIGINAL PAPER The toxic effect of R350P mutant desmin in striated muscle of man and mouse Christoph S. Clemen · Florian Stöckigt · Karl-Heinz Strucksberg · Frederic Chevessier · Lilli Winter · Johanna Schütz · Ralf Bauer · José-Manuel Thorweihe · Daniela Wenzel · Ursula Schlötzer-Schrehardt · Volker Rasche · Pavle Krsmanovic · Hugo A. Katus · Wolfgang Rottbauer · Steffen Just · Oliver J. Müller · Oliver Friedrich · Rainer Meyer · Harald Herrmann · Jan Wilko Schrickel · Rolf Schröder Received: 1 September 2014 / Revised: 14 October 2014 / Accepted: 30 October 2014 / Published online: 14 November 2014 © The Author(s) 2014. This article is published with open access at Springerlink.com Abstract Mutations of the human desmin gene on chro- Furthermore, we demonstrate that the missense-mutant mosome 2q35 cause autosomal dominant, autosomal reces- desmin inflicts changes of the subcellular localization and sive and sporadic forms of protein aggregation myopathies turnover of desmin itself and of direct desmin-binding part- and cardiomyopathies. We generated R349P desmin knock- ners. Our findings unveil a novel principle of pathogenesis, in mice, which harbor the ortholog of the most frequently in which not the presence of protein aggregates, but disrup- occurring human desmin missense mutation R350P. These tion of the extrasarcomeric intermediate filament network mice develop age-dependent desmin-positive protein aggre- leads to increased mechanical vulnerability of muscle fib- gation pathology, skeletal muscle weakness, dilated cardio- ers. These structural defects elicited at the myofiber level myopathy, as well as cardiac arrhythmias and conduction finally impact the entire organ and subsequently cause defects. For the first time, we report the expression level myopathy and cardiomyopathy.
    [Show full text]
  • Cytoskeletal Proteins in Neurological Disorders
    cells Review Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders Diana C. Muñoz-Lasso 1 , Carlos Romá-Mateo 2,3,4, Federico V. Pallardó 2,3,4 and Pilar Gonzalez-Cabo 2,3,4,* 1 Department of Oncogenomics, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands; [email protected] 2 Department of Physiology, Faculty of Medicine and Dentistry. University of Valencia-INCLIVA, 46010 Valencia, Spain; [email protected] (C.R.-M.); [email protected] (F.V.P.) 3 CIBER de Enfermedades Raras (CIBERER), 46010 Valencia, Spain 4 Associated Unit for Rare Diseases INCLIVA-CIPF, 46010 Valencia, Spain * Correspondence: [email protected]; Tel.: +34-963-395-036 Received: 10 December 2019; Accepted: 29 January 2020; Published: 4 February 2020 Abstract: Recent observations related to the structure of the cytoskeleton in neurons and novel cytoskeletal abnormalities involved in the pathophysiology of some neurological diseases are changing our view on the function of the cytoskeletal proteins in the nervous system. These efforts allow a better understanding of the molecular mechanisms underlying neurological diseases and allow us to see beyond our current knowledge for the development of new treatments. The neuronal cytoskeleton can be described as an organelle formed by the three-dimensional lattice of the three main families of filaments: actin filaments, microtubules, and neurofilaments. This organelle organizes well-defined structures within neurons (cell bodies and axons), which allow their proper development and function through life. Here, we will provide an overview of both the basic and novel concepts related to those cytoskeletal proteins, which are emerging as potential targets in the study of the pathophysiological mechanisms underlying neurological disorders.
    [Show full text]
  • Dystroglycan in the Nervous System
    CORE Metadata, citation and similar papers at core.ac.uk Provided by Nature Precedings Review: Dystroglycan in the Nervous System Matthias Samwald Medical University of Vienna Vienna, Austria E-Mail: matthias.samwald (at) meduniwien.ac.at Homepage: http://neuroscientific.net/curriculum Abstract Dystroglycan is part of a large complex of proteins, the dystrophin-glycoprotein complex, which has been implicated in the pathogenesis of muscular dystrophies for a long time. Besides muscular degeneration many patients manifest symptoms of neurological and cognitive dysfunction. Recent findings suggest that dystroglycan is implicated in brain development, synapse formation and plasticity, nerve-glia interactions and maintenance of the blood-brain barrier. Most research so far has focused on the functions of dystroglycan in muscle and neuromuscular junctions, while its role in the brain and interneuronal synapses has been neglected. This review will give an overview of the biochemistry of dystroglycan, its interaction with other proteins as well as its confirmed and hypothetical functions in the nervous system. Introduction In 1987 a laminin-binding membrane protein was found in brain tissue and was termed cranin (Smalheiser and Schwartz, 1987). Eight years passed until this protein proofed to be identical with dystroglycan, which was previously only thought to be associated with muscle membranes (Smalheiser and Kim, 1995). Dystroglycan gives mechanical stability to muscle fibres by linking the extracellular matrix on the extracellular surface with the actin cytoskeleton on the intracellular side. Furthermore, it is implicated in the formation of neuromuscular junctions. The function of dystroglycan and its associated proteins is impaired in a large group of hereditary diseases, the muscular dystrophies.
    [Show full text]
  • The Influence of Actn3 R577x Genotype on Performance and Muscle Adaptations to a Single Bout of Exercise
    THE INFLUENCE OF ACTN3 R577X GENOTYPE ON PERFORMANCE AND MUSCLE ADAPTATIONS TO A SINGLE BOUT OF EXERCISE by IOANNIS D. PAPADIMITRIOU Thesis submitted in fulfilment of the requirements for the degree of “DOCTOR OF PHILOSOPHY” Supervisors: Dr Nir Eynon Prof. David Bishop Dr Xu Yan 2018 The influence of ACTN3 R577X genotype on performance and muscle adaptations to a single bout of exercise Statement of Originality I, Ioannis Papadimitriou, declare that the PhD thesis by Publication entitled “The influence of ACTN3 R577X genotype on performance and muscle adaptations to a single bout of exercise” is no more than 100,000 words in length including quotes and exclusive of tables, figures, appendices, bibliography, references and footnotes. This thesis contains no material that has been submitted previously, in whole or in part, for the award of any other academic degree or diploma. Except where otherwise indicated, this thesis is my own work. Signature Date 28th August 2017 Ioannis Papadimitriou PhD research 2013-2017 2 The influence of ACTN3 R577X genotype on performance and muscle adaptations to a single bout of exercise In Loving Memory of Evangelia Taskoudi 6th Nov 1942 – 11th Sep 2016 Ioannis Papadimitriou PhD research 2013-2017 3 The influence of ACTN3 R577X genotype on performance and muscle adaptations to a single bout of exercise Acknowledgements Although my name sits alone on the spine of this thesis as its author, there are a number of people who have generously offered their time in contributing to this project over the last 4 years. I sincerely thank you all for your efforts.
    [Show full text]
  • Flavone Effects on the Proteome and Transcriptome of Colonocytes in Vitro and in Vivo and Its Relevance for Cancer Prevention and Therapy
    TECHNISCHE UNIVERSITÄT MÜNCHEN Lehrstuhl für Ernährungsphysiologie Flavone effects on the proteome and transcriptome of colonocytes in vitro and in vivo and its relevance for cancer prevention and therapy Isabel Winkelmann Vollständiger Abdruck der von der Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften genehmigten Dissertation. Vorsitzender: Univ.-Prof. Dr. D. Haller Prüfer der Dissertation: 1. Univ.-Prof. Dr. H. Daniel 2. Univ.-Prof. Dr. U. Wenzel (Justus-Liebig-Universität Giessen) 3. Prof. Dr. E.C.M. Mariman (Maastricht University, Niederlande) schriftliche Beurteilung Die Dissertation wurde am 24.08.2009 bei der Technischen Universität München eingereicht und durch die Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt am 25.11.2009 angenommen. Die Forschung ist immer auf dem Wege, nie am Ziel. (Adolf Pichler) Table of contents 1. Introduction .......................................................................................................... 1 1.1. Cancer and carcinogenesis .................................................................................. 2 1.2. Colorectal Cancer ............................................................................................... 3 1.2.1. Hereditary forms of CRC ........................................................................................ 4 1.2.2. Sporadic forms of CRC ..........................................................................................
    [Show full text]
  • The Regulation of Beta- Dystroglycan Internalization
    The Regulation of Beta- Dystroglycan Internalization Robert Piggott A thesis submitted to the University of Sheffield for the degree of Doctor of Philosophy Department of Biomedical Sciences, University of Sheffield July 2014 I TABLE OF CONTENTS CONTENTS………………………………………………………………………………II ABBREVIATIONS LIST…………………………………………………………....……VI ABSTRACT……………………………………………………………………………..VIII Chapter 1: Introduction .................................................................................. 1 1.1.1 The Dystroglycan Subunits ..................................................................... 2 1.1.2 Dystroglycan is an Essential Adhesion Protein......................................... 4 1.1.3 Dystroglycan in the Dystrophin-associated Glycoprotein Complex ............ 5 1.1.4 Dystroglycan in Other Complexes ......................................................... 10 1.1.5 Dystroglycan Complex Formation in Response to the Extracellular Matrix ................................................................................................................... 13 1.1.6 Summary: Why Dystroglycan is an Essential Protein.............................. 15 1.2.1 Duchenne Muscular Dystrophy ............................................................. 17 1.2.2 The mdx Mouse and Other Models ........................................................ 19 1.2.3 Dystroglycan Disruption and Other Muscular Dystrophies ...................... 22 1.2.4 Summary: The Loss and Restoration of β-Dystroglycan in DMD Pathology and Therapy ................................................................................................
    [Show full text]
  • Effects of 12 Weeks of Hypertrophy Resistance Exercise Training
    nutrients Article Effects of 12 Weeks of Hypertrophy Resistance Exercise Training Combined with Collagen Peptide Supplementation on the Skeletal Muscle Proteome in Recreationally Active Men Vanessa Oertzen-Hagemann 1,*, Marius Kirmse 1, Britta Eggers 2 , Kathy Pfeiffer 2, Katrin Marcus 2, Markus de Marées 1 and Petra Platen 1 1 Department of Sports Medicine and Sports Nutrition, Ruhr University Bochum, 44801 Bochum, Germany; [email protected] (M.K.); [email protected] (M.d.M.); [email protected] (P.P.) 2 Medizinisches Proteom-Center, Medical Faculty, Ruhr University Bochum, 44801 Bochum, Germany; [email protected] (B.E.); kathy.pfeiff[email protected] (K.P.); [email protected] (K.M.) * Correspondence: [email protected]; Tel.: +49-234-32-23170 Received: 10 April 2019; Accepted: 10 May 2019; Published: 14 May 2019 Abstract: Evidence has shown that protein supplementation following resistance exercise training (RET) helps to further enhance muscle mass and strength. Studies have demonstrated that collagen peptides containing mostly non-essential amino acids increase fat-free mass (FFM) and strength in sarcopenic men. The aim of this study was to investigate whether collagen peptide supplementation in combination with RET influences the protein composition of skeletal muscle. Twenty-five young men (age: 24.2 2.6 years, body mass (BM): 79.6 5.6 kg, height: 185.0 5.0 cm, fat mass (FM): ± ± ± 11.5% 3.4%) completed body composition and strength measurements and vastus lateralis biopsies ± were taken before and after a 12-week training intervention. In a double-blind, randomized design, subjects consumed either 15 g of specific collagen peptides (COL) or a non-caloric placebo (PLA) every day within 60 min after their training session.
    [Show full text]
  • AAV9-Mediated Gene Transfer of Desmin Ameliorates Cardiomyopathy in Desmin-Deficient Mice
    OPEN Gene Therapy (2016) 23, 673–679 © 2016 Macmillan Publishers Limited, part of Springer Nature. All rights reserved 0969-7128/16 www.nature.com/gt ORIGINAL ARTICLE AAV9-mediated gene transfer of desmin ameliorates cardiomyopathy in desmin-deficient mice MB Heckmann1,2, R Bauer1, A Jungmann1, L Winter3, K Rapti1,2, K-H Strucksberg3, CS Clemen4,ZLi5, R Schröder3, HA Katus1,2 and OJ Müller1,2 Mutations of the human desmin (DES) gene cause autosomal dominant and recessive myopathies affecting skeletal and cardiac muscle tissue. Desmin knockout mice (DES-KO), which develop progressive myopathy and cardiomyopathy, mirror rare human recessive desminopathies in which mutations on both DES alleles lead to a complete ablation of desmin protein expression. Here, we investigated whether an adeno-associated virus-mediated gene transfer of wild-type desmin cDNA (AAV-DES) attenuates cardiomyopathy in these mice. Our approach leads to a partial reconstitution of desmin protein expression and the de novo formation of the extrasarcomeric desmin–syncoilin network in cardiomyocytes of treated animals. This finding was accompanied by reduced fibrosis and heart weights and improved systolic left-ventricular function when compared with control vector-treated DES-KO mice. Since the re-expression of desmin protein in cardiomyocytes of DES-KO mice restores the extrasarcomeric desmin– syncoilin cytoskeleton, attenuates the degree of cardiac hypertrophy and fibrosis, and improves contractile function, AAV-mediated desmin gene transfer may be a novel and promising therapeutic approach for patients with cardiomyopathy due to the complete lack of desmin protein expression. Gene Therapy (2016) 23, 673–679; doi:10.1038/gt.2016.40 INTRODUCTION mutations, which lead to a complete ablation of desmin protein Desmin is a type III intermediate filament (IF) protein, which expression.5,6 In contrast to autosomal dominant desminopathies, is abundantly expressed in smooth and striated muscle cells.
    [Show full text]
  • Autocrine IFN Signaling Inducing Profibrotic Fibroblast Responses By
    Downloaded from http://www.jimmunol.org/ by guest on September 23, 2021 Inducing is online at: average * The Journal of Immunology , 11 of which you can access for free at: 2013; 191:2956-2966; Prepublished online 16 from submission to initial decision 4 weeks from acceptance to publication August 2013; doi: 10.4049/jimmunol.1300376 http://www.jimmunol.org/content/191/6/2956 A Synthetic TLR3 Ligand Mitigates Profibrotic Fibroblast Responses by Autocrine IFN Signaling Feng Fang, Kohtaro Ooka, Xiaoyong Sun, Ruchi Shah, Swati Bhattacharyya, Jun Wei and John Varga J Immunol cites 49 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2013/08/20/jimmunol.130037 6.DC1 This article http://www.jimmunol.org/content/191/6/2956.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* Why • • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2013 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 23, 2021. The Journal of Immunology A Synthetic TLR3 Ligand Mitigates Profibrotic Fibroblast Responses by Inducing Autocrine IFN Signaling Feng Fang,* Kohtaro Ooka,* Xiaoyong Sun,† Ruchi Shah,* Swati Bhattacharyya,* Jun Wei,* and John Varga* Activation of TLR3 by exogenous microbial ligands or endogenous injury-associated ligands leads to production of type I IFN.
    [Show full text]