Progress in brain research, volume 214

Advisory Editors Stephen G Waxman Bridget Marie Flaherty Professor of Neurology Neurobiology, and Pharmacology; Director, Center for Neuroscience & Regeneration/Neurorehabilitation Research Yale University School of Medicine New Haven, Connecticut USA Donald G Stein Asa G Candler Professor Department of Emergency Medicine Emory University Atlanta, Georgia USA Dick F Swaab Professor of Neurobiology Medical Faculty, University of Amsterdam; Leader Research team Neuropsychiatric Disorders Netherlands Institute for Neuroscience Amsterdam The Netherlands Howard L Fields Professor of Neurology Endowed Chair in Pharmacology of Addiction Director, Wheeler Center for the Neurobiology of Addiction University of California San Francisco, California USA Elsevier Radarweg 29, PO Box 211, 1000 AE Amsterdam, Netherlands The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, UK 225 Wyman Street, Waltham, MA 02451, USA First edition 2014 Copyright # 2014 Elsevier B.V All rights reserved No part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or any information storage and retrieval system, without permission in writing from the publisher Details on how to seek permission, further information about the Publisher’s permissions policies and our arrangements with organizations such as the Copyright Clearance Center and the Copyright Licensing Agency, can be found at our website: www.elsevier.com/permissions This book and the individual contributions contained in it are protected under copyright by the Publisher (other than as may be noted herein) Notices Knowledge and best practice in this field are constantly changing As new research and experience broaden our understanding, changes in research methods, professional practices, or medical treatment may become necessary Practitioners and researchers must always rely on their own experience and knowledge in evaluating and using any information, methods, compounds, or experiments described herein In using such information or methods they should be mindful of their own safety and the safety of others, including parties for whom they have a professional responsibility To the fullest extent of the law, neither the Publisher nor the authors, contributors, or editors, assume any liability for any injury and/or damage to persons or property as a matter of products liability, negligence or otherwise, or from any use or operation of any methods, products, instructions, or ideas contained in the material herein ISBN: 978-0-444-63486-3 ISSN: 0079-6123 For information on all Elsevier publications visit our website at store.elsevier.com Contributors Hayder Amin Istituto Italiano di Tecnologia, NetS3 Laboratory, Neuroscience and Brain Technologies Dpt., Genova, Italy Pavle Andjus Center for Laser Microscopy, Institute for Physiology and Biochemistry, Faculty of Biology, University of Belgrade, Belgrade, Serbia Eleonora Aronica Department of (Neuro)Pathology, Academic Medical Center and Swammerdam Institute for Life Sciences, Center for Neuroscience, University of Amsterdam, Amsterdam, and SEIN—Stichting Epilepsie Instellingen Nederland, Heemstede, The Netherlands Ke´vin Baranger Aix Marseille Universite´, CNRS, UMR 7259, NICN, 13344, and Neurology and Neuropsychology Department, AP-HM, Marseille, France Martin Bastmeyer Institute of Zoologie, Karlsruhe, and Institute of Functional Interfaces (IFG), Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany Luca Berdondini Istituto Italiano di Tecnologia, NetS3 Laboratory, Neuroscience and Brain Technologies Dpt., Genova, Italy Vladimir Berezin Laboratory of Neural Plasticity, Department of Neuroscience and Pharmacology, University of Copenhagen, Symbion, Fruebjergvej 3, Box 39, Copenhagen Ø, Denmark Katarzyna Bieganska Cellular Neurophysiology, Hannover Medical School, Hannover, Germany Judit Bigas Iproteos S.L., Barcelona, Spain Elodie Chabrol UCL Institute of Neurology, University College London, Queen Square, London, UK Kae-Jiun Chang Program in Developmental Biology, and Department of Neuroscience, Baylor College of Medicine, One Baylor Plaza, Houston, TX, USA Lorenzo A Cingolani Department of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy v vi Contributors Stefanie Dedeurwaerdere Department of Translational Neuroscience, University of Antwerp, Wilrijk, Belgium Alexander Dityatev Molecular Neuroplasticity Group, German Center for Neurodegenerative Diseases (DZNE), Magdeburg, Germany; Medical Faculty, Otto-von-Guericke University, Magdeburg, Germany; Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany; Laboratory for Brain Extracellular Matrix Research, University of Nizhny Novgorod, Nizhny Novgorod, Russia; Department of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genova, Italy Veronica Estrada Molecular Neurobiology Laboratory, Department of Neurology, Heinrich-HeineUniversity Medical Center Duăsseldorf, Duăsseldorf, Germany Andreas Faissner Department of Cell Morphology and Molecular Neurobiology, Ruhr-University Bochum, Bochum, Germany James W Fawcett John van Geest Centre for Brain Repair, University of Cambridge, Forvie Site, Robinson Way, Cambridge, UK Charles ffrench-Constant MRC Centre for Regenerative Medicine, The University of Edinburgh, Edinburgh, UK Mikhail Filippov Molecular Neuroplasticity Group, German Center for Neurodegenerative Diseases (DZNE), Magdeburg, Germany Renato Frischknecht Department for Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, and Center for Behavioral Brain Sciences (CBBS) Magdeburg, Germany Denis Grandgirard Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, Switzerland Anne Heikkinen Oulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland Natasˇa Jovanov Milosˇevic´ Croatian Institute for Brain Research, and Department of Medical Biology, University of Zagreb School of Medicine, Zagreb, Croatia Milosˇ Judasˇ Croatian Institute for Brain Research, University of Zagreb School of Medicine, Zagreb, Croatia Contributors Leszek Kaczmarek Department of Molecular and Cellular Neurobiology, Nencki Institute, Warsaw, Poland Meghan E Kerrisk Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA Michel Khrestchatisky Aix Marseille Universite´, CNRS, UMR 7259, NICN, 13344, Marseille, France Anthony J Koleske Department of Molecular Biophysics and Biochemistry; Department of Neurobiology; Interdepartmental Neuroscience Program, and Program in Cellular Neuroscience, Neurodegeneration, and Repair, Yale University, New Haven, CT, USA Svetlana Korotchenko Laboratory for Brain Extracellular Matrix Research, University of Nizhny Novgorod, Nizhny Novgorod, Russia; Department of Neuroscience and Brain Technologies; Istituto Italiano di Tecnologia, Genova, Italy Ivica Kostovic Croatian Institute for Brain Research, University of Zagreb School of Medicine, Zagreb, Croatia Jessica C.F Kwok John van Geest Centre for Brain Repair, University of Cambridge, Forvie Site, Robinson Way, Cambridge, UK Tomasz Lebitko Department of Molecular and Cellular Neurobiology, Nencki Institute, Warsaw, Poland Stephen L Leib Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, and Biology Division, Spiez Laboratory, Swiss Federal Office for Civil Protection, Spiez, Switzerland Fabian D Liechti Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, Switzerland Katherine Long MRC Centre for Regenerative Medicine, The University of Edinburgh, Edinburgh, UK Bart R Lubbers Department of Molecular & Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, HV Amsterdam, The Netherlands vii viii Contributors Katarzyna Łukasiuk The Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland Alessandro Maccione Istituto Italiano di Tecnologia, NetS3 Laboratory, Neuroscience and Brain Technologies Dpt., Genova, Italy Markus Morawski University of Leipzig, EU-ESF Transnational Junior Research Group “MESCAMP”, Paul Flechsig Institute for Brain Research, Leipzig, Germany Mariusz Mucha University of Exeter, Exeter, UK Xavier E Ndode-Ekane Department of Neurobiology, A I Virtanen Institute for Molecular Sciences, University of Eastern Finland, Kuopio, Finland Thierry Nieus Istituto Italiano di Tecnologia, NetS3 Laboratory, Neuroscience and Brain Technologies Dpt., Genova, Italy Ghislain Opdenakker Department of Microbiology and Immunology, Laboratory of Immunobiology, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium Robert Pawlak University of Exeter, Exeter, UK Taina Pihlajaniemi Oulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland Asla Pitkaănen Department of Neurobiology, A I Virtanen Institute for Molecular Sciences, University of Eastern Finland, and Department of Neurology, Kuopio University Hospital, Kuopio, Finland Evgeni Ponimaskin Cellular Neurophysiology, Hannover Medical School, Hannover, Germany Elizabeth M Powell Department of Anatomy & Neurobiology, University of Maryland School of Medicine, Baltimore, MD, USA Lidija Radenovic Center for Laser Microscopy, Institute for Physiology and Biochemistry, Faculty of Biology, University of Belgrade, Belgrade, Serbia Matthew N Rasband Department of Neuroscience, and Program in Developmental Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX, USA Contributors Santiago Rivera Aix Marseille Universite´, CNRS, UMR 7259, NICN, 13344, Marseille, France Jesu´s Seco Iproteos S.L., Barcelona, Spain Constanze I Seidenbecher Center for Behavioral Brain Sciences (CBBS), and Department of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, Magdeburg, Germany Oleg Senkov Molecular Neuroplasticity Group, German Center for Neurodegenerative Diseases (DZNE), Magdeburg, Germany Alessandro Simi Istituto Italiano di Tecnologia, NetS3 Laboratory, Neuroscience and Brain Technologies Dpt., Genova, Italy August B Smit Department of Molecular & Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, HV Amsterdam, The Netherlands Eduardo Soriano Department of Cell Biology, University of Barcelona; Centro de Investigacio´n en Red sobre Enfermedades Neurodegenerativas (CIBERNED), ISCIII, Madrid, and Vall d’Hebron Institut de Recerca (VHIR), Barcelona, Spain Sabine Spijker Department of Molecular & Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, HV Amsterdam, The Netherlands Vera Stamenkovic Center for Laser Microscopy, Institute for Physiology and Biochemistry, Faculty of Biology, University of Belgrade, Belgrade, Serbia Michal Stawarski Laboratory of Cell Biophysics, Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, Warsaw, Poland Teresa Tarrago Iproteos S.L., and Institute for Research in Biomedicine (IRB Barcelona), Barcelona, Spain Ayse Tekinay UNAM-National Nanotechnology Research Center, Institute of Materials Science and Nanotechnology, Bilkent University, Ankara, Turkey Ursula Theocharidis Department of Cell Morphology and Molecular Neurobiology, Ruhr-University Bochum, Bochum, Germany ix x Contributors Effie Tsilibary Institute of Biosciences and Applications, NCSR “Demokritos”, Athens, Greece Athina Tzinia Institute of Biosciences and Applications, NCSR “Demokritos”, Athens, Greece Jo Van Damme Department of Microbiology and Immunology, Laboratory of Immunobiology, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium Michel C van den Oever Department of Molecular & Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, HV Amsterdam, The Netherlands Jennifer Vandooren Department of Microbiology and Immunology, Laboratory of Immunobiology, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium Lydia Vargova Charles University, 2nd Faculty of Medicine, and Institute of Experimental Medicine AS CR, v.v.i., Department of Neuroscience, Prague, Czech Republic Naiara Vazquez Department of Translational Neuroscience, University of Antwerp, Wilrijk, Belgium Matthew C Walker UCL Institute of Neurology, University College London, Queen Square, London, UK Peter S Walmod Laboratory of Neural Plasticity, Department of Neuroscience and Pharmacology, University of Copenhagen, Symbion, Fruebjergvej 3, Box 39, Copenhagen Ø, Denmark Bernhard Wehrle-Haller Department of Cell Physiology and Metabolism, Centre Me´dical Universitaire, University of Geneva, Geneva, Switzerland Hans Werner Muăller Molecular Neurobiology Laboratory, Department of Neurology, Heinrich-HeineUniversity Medical Center Duăsseldorf, Duăsseldorf, Germany Grzegorz M Wilczynski The Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland Jakub Wlodarczyk Laboratory of Cell Biophysics, Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, Warsaw, Poland Contributors Sujeong Yang John van Geest Centre for Brain Repair, University of Cambridge, Forvie Site, Robinson Way, Cambridge, UK Michisuke Yuzaki Department of Physiology, School of Medicine, Keio University, Tokyo, Japan Andre Zeug Cellular Neurophysiology, Hannover Medical School, Hannover, Germany xi Preface The organization of the extracellular matrix (ECM) is a reflection of the role and function of organs in our bodies The interaction of cells with the ECM determines their polarity, shape, and form and is providing cues for survival and proliferation The brain, in comparison with other organs, shows an extremely complex architecture, in which neurons, glial cells, and blood vessels are interacting to create and maintain a dynamic network, in which beneficial synaptic connections need to be actively maintained and other remodeled in response to changes in signaling input Similar to other organ systems, cell–cell interactions based on direct contacts via cadherins and signaling receptors, as well as cell–matrix interactions with the ECM scaffold, are controlling the organization of glial cells and neurons as well as the projections of neurites and location of synapses All these structures are embedded within an ECM scaffold formed by fiber or network-forming proteins and membrane-anchored or secreted glycosaminoglycans Despite recent advances in the ECM field, the importance of neural ECM for physiological and pathological processes is less widely recognized than that of other nervous system elements To overcome this, a European consortium “Brain Extracellular Matrix in Health and Disease (ECMNet)” was established in 2010 as a part of intergovernmental framework for European Cooperation in Science and Technology (COST) Now, ECMNet combines more than 200 young and established researchers from 20 European countries (http://www.costbm1001.eu/) Each book chapter of this volume is prepared involving ECMNet members and other leading experts from the USA and Japan The chapters cover the broad range of topics, grouped into four parts, which are devoted to normal physiological functions of neural ECM, its role in brain diseases, development of methods to image the ECM, to therapeutically target it, and to generate artificial ECM FUNCTIONS OF NEURAL ECM The neural ECM is well recognized to play a key role in neural development and the first two chapters of the book are devoted to this topic Theocharidis, Long, ffrenchConstant, and Faissner (2014) discuss available data on expression of tenascins, laminins, and proteoglycans in the ECM of the stem cell niche and argue for crucial importance of ECM for the biology of this cellular compartment Heikkinen, Pihlajaniemi, Faissner, and Yuzaki (2014) focus on how proteoglycans, tenascin, and C1q (C1qDC) family proteins regulate synapse formation, maintenance, and pruning during neural development In the adult central nervous system (CNS), multiple neural ECM molecules together with astroglial, pre-, and postsynaptic elements form tetrapartite synapses, and the ECM regulates Hebbian synaptic plasticity through the modulation of perisomatic GABAergic inhibition, intrinsic neuronal excitability, and intracellular signaling, as presented by Senkov, Andjus, Radenovic, xiii 458 CHAPTER 18 Integrin signaling Nayal, A., Webb, D.J., Brown, C.M., Schaefer, E.M., Vicente-Manzanares, M., Horwitz, A.R., 2006 Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics J Cell Biol 173, 587–589 Niewmierzycka, A., Mills, J., St-Arnaud, R., Dedhar, S., Reichardt, L.F., 2005 Integrin-linked kinase deletion from mouse cortex results in cortical lamination defects resembling cobblestone lissencephaly J Neurosci 25, 7022–7031 Nishiya, N., Kiosses, W.B., Han, J., Ginsberg, M.H., 2005 An alpha4 integrin-paxillin-ArfGAP complex restricts Rac activation to the leading edge of migrating cells Nat Cell Biol 7, 343–352 Partridge, M.A., Marcantonio, E.E., 2006 Initiation of attachment and generation of mature focal adhesions by integrin-containing filopodia in cell spreading Mol Biol Cell 17, 4237–4248 Pelham Jr., R.J., Wang, Y., 1997 Cell locomotion and focal adhesions are regulated by substrate flexibility Proc Natl Acad Sci U S A 94, 13661–13665 Pinon, P., Parssinen, J., Vazquez, P., Bachmann, M., Rahikainen, R., Jacquier, M.C., Azizi, L., Maatta, J.A., Bastmeyer, M., Hytonen, V.P., Wehrle-Haller, B., 2014 Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing J Cell Biol 205, 265–281 Ricard-Blum, S., Salza, R., 2014 Matricryptins and matrikines: biologically active fragments of the extracellular matrix Exp Dermatol 23, 457–463 Rico, B., Beggs, H.E., Schahin-Reed, D., Kimes, N., Schmidt, A., Reichardt, L.F., 2004 Control of axonal branching and synapse formation by focal adhesion kinase Nat Neurosci 7, 1059–1069 Riveline, D., Zamir, E., Balaban, N.Q., Schwarz, U.S., Ishizaki, T., Narumiya, S., Kam, Z., Geiger, B., Bershadsky, A.D., 2001 Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism J Cell Biol 153, 1175–1186 Saltel, F., Mortier, E., Hytonen, V.P., Jacquier, M.C., Zimmermann, P., Vogel, V., Liu, W., Wehrle-Haller, B., 2009 New PI(4,5)P2- and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering J Cell Biol 187, 715–731 Santiago-Medina, M., Gregus, K.A., Gomez, T.M., 2013 PAK-PIX interactions regulate adhesion dynamics and membrane protrusion to control neurite outgrowth J Cell Sci 126, 1122–1133 Sawada, Y., Sheetz, M.P., 2002 Force transduction by Triton cytoskeletons J Cell Biol 156, 609–615 Schaller, M.D., Borgman, C.A., Cobb, B.S., Vines, R.R., Reynolds, A.B., Parsons, J.T., 1992 pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions Proc Natl Acad Sci U S A 89, 5192–5196 Schaller, M.D., Otey, C.A., Hildebrand, J.D., Parsons, J.T., 1995 Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains J Cell Biol 130, 1181–1187 Schmid, R.S., Shelton, S., Stanco, A., Yokota, Y., Kreidberg, J.A., Anton, E.S., 2004 alpha3beta1 integrin modulates neuronal migration and placement during early stages of cerebral cortical development Development 131, 6023–6031 Schmidt, S., Nakchbandi, I., Ruppert, R., Kawelke, N., Hess, M.W., Pfaller, K., Jurdic, P., Fassler, R., Moser, M., 2011 Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption J Cell Biol 192, 883–897 References Shi, Y., Pontrello, C.G., DeFea, K.A., Reichardt, L.F., Ethell, I.M., 2009 Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity J Neurosci 29, 8129–8142 Sirois, J., Cote, J.F., Charest, A., Uetani, N., Bourdeau, A., Duncan, S.A., Daniels, E., Tremblay, M.L., 2006 Essential function of PTP-PEST during mouse embryonic vascularization, mesenchyme formation, neurogenesis and early liver development Mech Dev 123, 869–880 Springer, T.A., Zhu, J., Xiao, T., 2008 Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3 J Cell Biol 182, 791–800 Stevens, A., Jacobs, J.R., 2002 Integrins regulate responsiveness to slit repellent signals J Neurosci 22, 4448–4455 Su, J., Stenbjorn, R.S., Gorse, K., Su, K., Hauser, K.F., Ricard-Blum, S., Pihlajaniemi, T., Fox, M.A., 2012 Target-derived matricryptins organize cerebellar synapse formation through alpha3beta1 integrins Cell Rep 2, 223–230 Tadokoro, S., Shattil, S.J., Eto, K., Tai, V., Liddington, R.C., de Pereda, J.M., Ginsberg, M.H., Calderwood, D.A., 2003 Talin binding to integrin beta tails: a final common step in integrin activation Science 302, 103–106 Tumbarello, D.A., Brown, M.C., Turner, C.E., 2002 The paxillin LD motifs FEBS Lett 513, 114–118 Turner, C.E., Glenney Jr., J.R., Burridge, K., 1990 Paxillin: a new vinculin-binding protein present in focal adhesions J Cell Biol 111, 1059–1068 Varnum-Finney, B., Reichardt, L.F., 1994 Vinculin-deficient PC12 cell lines extend unstable lamellipodia and filopodia and have a reduced rate of neurite outgrowth J Cell Biol 127, 1071–1084 Wade, R., Vande Pol, S., 2006 Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase Biochem J 393, 565–573 Wade, R., Bohl, J., Vande Pol, S., 2002 Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase Oncogene 21, 96–107 Wang, X.B., Bozdagi, O., Nikitczuk, J.S., Zhai, Z.W., Zhou, Q., Huntley, G.W., 2008 Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately Proc Natl Acad Sci U S A 105, 19520–19525 Webb, D.J., Donais, K., Whitmore, L.A., Thomas, S.M., Turner, C.E., Parsons, J.T., Horwitz, A.F., 2004 FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly Nat Cell Biol 6, 154–161 Wegener, K.L., Partridge, A.W., Han, J., Pickford, A.R., Liddington, R.C., Ginsberg, M.H., Campbell, I.D., 2007 Structural basis of integrin activation by talin Cell 128, 171–182 Wehrle-Haller, B., 2012a Assembly and disassembly of cell matrix adhesions Curr Opin Cell Biol 24, 569–581 Wehrle-Haller, B., 2012b Structure and function of focal adhesions Curr Opin Cell Biol 24, 116–124 White, D.P., Caswell, P.T., Norman, J.C., 2007 alpha v beta3 and alpha5beta1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration J Cell Biol 177, 515–525 Wiseman, P.W., Brown, C.M., Webb, D.J., Hebert, B., Johnson, N.L., Squier, J.A., Ellisman, M.H., Horwitz, A.F., 2004 Spatial mapping of integrin interactions and dynamics during cell migration by image correlation microscopy J Cell Sci 117, 5521–5534 459 460 CHAPTER 18 Integrin signaling Ylanne, J., Huuskonen, J., O’Toole, T.E., Ginsberg, M.H., Virtanen, I., Gahmberg, C.G., 1995 Mutation of the cytoplasmic domain of the integrin beta subunit Differential effects on cell spreading, recruitment to adhesion plaques, endocytosis, and phagocytosis J Biol Chem 270, 9550–9557 Yu, C.H., Law, J.B., Suryana, M., Low, H.Y., Sheetz, M.P., 2011 Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation Proc Natl Acad Sci U S A 108, 20585–20590 Zhang, H., Webb, D.J., Asmussen, H., Horwitz, A.F., 2003 Synapse formation is regulated by the signaling adaptor GIT1 J Cell Biol 161, 131–142 Zhang, H., Berg, J.S., Li, Z., Wang, Y., Lang, P., Sousa, A.D., Bhaskar, A., Cheney, R.E., Stromblad, S., 2004 Myosin-X provides a motor-based link between integrins and the cytoskeleton Nat Cell Biol 6, 523–531 Zhang, H., Webb, D.J., Asmussen, H., Niu, S., Horwitz, A.F., 2005 A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC J Neurosci 25, 3379–3388 Zhu, J., Zhu, J., Springer, T.A., 2013 Complete integrin headpiece opening in eight steps J Cell Biol 201, 1053–1068 Index Note: Page numbers followed by b indicate boxes, f indicate figures and t indicate tables A Ab-degrading enzymes (ADEs), 366 Ab-derived diffusible ligands (ADDLs), 208–209 Acceptor photobleaching (APB) approach, 300–301 Active pixel sensor (APS), 421 AD See Alzheimer’s disease (AD) Addiction See Drug addiction ADEs See Ab-degrading enzymes (ADEs) A disintegrin and metalloproteases (ADAMs), 358 A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs), 358 cancer, 367 ischemia, 367 Agarose, 400 AIS See Axon initial segment (AIS) Alginate, 400 Alzheimer’s disease (AD) ADAM10, 366 ADEs, 366 and aging Ab aggregates, 208 ChABC treatment, 356 CSPGs, PNs and ACs, 214–216 ECS diffusion, 212–213 heparin mimetics, 357 HSPGs (see Heparan sulfate proteoglycans (HSPGs)) LMW heparin, 356–357 MMP-2, 217–218 MMP-3, 217 MMP-9, 216 neuroparin/C3, 356–357 reelin expression, 211–212 yokukansan, 356 CSPGs, 59–60, 182 HSPGs, 181–182 hyaluronic acid, CSF levels of, 61 integrins, 371 LDLRs, 118–119 LRRC15, 376 MMP/TIMP system, 314, 323–325 NEP, 366 PAI-1, 366 reelin, 69–70 tPA/plasmin, 366 Amblyopia, 184–185 AMPA-type glutamate receptor (AMPAR), 104 Anacardic acid, 361 Apolipoprotein E receptor (ApoER2), 114 Aseptic meningitis, 329 Atomic force microscopy (AFM), 289 Autism spectrum disorder (ASD), 246, 248 BTBR mouse model, 248 integrin b3, 118 MMP-9, 148, 170 Plaur gene, 247–248 reelin, 69 Autofluorescence lifetime microscopy (ALM), 290 Axonal coat (AC), 213–214 Axon initial segment (AIS), 84–85 L-type voltage-gated calcium channels, 88–90 nodes of Ranvier, 90–93, 91f PNNs, 88–90, 89f B Bacterial meningitis (BM) brain damage, pathophysiology of, 326–327 clinical and epidemiological aspects, 326 MMPIs/TACE inhibition cortical injury, 330–333 hippocampal apoptosis, 330–332 interventions, timing of, 332 negative effects on survival, 332 neurofunctional damage, 332 TNF-a activation, 329 MMPs, role of, 327–329, 328f MMP-9/TIMP-1, imbalance of, 329 Biosensors, 303–305, 304f Bipolar disorder MMP-9, 148 neuropsin, 147 PNNs, 275 reelin, 69, 275–276 schizophrenia, 273f BM See Bacterial meningitis (BM) Brain-enriched hyaluronic acid-binding (BEHAB) protein, 182 Brain tumor hyaluronan, 182 MMPs and TIMPs, 314 SPARC and BEHAB protein, 182 tenascin-C, 182 461 462 Index C Cancer ADAMTS, 367 marimastat and batimastat, 367 MMPs, 367 Neovastat, 361 plasminogen system, 368 RECK expression, 367–368 Captopril, 326 Carbon nanotubes (CNTs), 426 Cell adhesion molecule L1 (L1-CAM), 375–376 Cell adhesion molecules (CAMs), 373t coxsackievirus and CAR, 372–374 function, 371–372 ICAM-5, 375 L1-CAM, 375–376 LRRC15, 376 NCAM1, 375 Thy-1/CD90, 372 Cerebral amyloid angiopathy (CAA), 208 Chitosan, 401 Chondroitinase ABC (ChABC), 266 Alzheimer’s disease, 356 ischemic stroke, 355 learning and memory, 59 spinal cord injury, 186 synaptic plasticity, 54–59 Chondroitin sulfate proteoglycans (CSPGs), 249 astrocyte-derived ECM, 30 axonal coat, 213–214 DSD-1-PG/phosphacan, 15–16 ECS diffusion, 212–213 integrin receptors, 103, 105 laminar and connectivity development early human fetal brain, 160–162 midfetal period, 162–164, 163f learning and memory, 59–60 lecticans, 15–16 membrane-based part-time, 16 PNNs, 180–181 Alzheimer’s disease, 182, 214–216 amblyopia, 184–185 brain tumors, 182 fear memory, 183–184 OR memory, 184 somatosensory/barrel cortex, 185 spinal cord injury, 183 stroke, 183, 185–186 structural components of, 180 schizophrenia, 169–170 structure of, 180 synaptic plasticity, 54–59 versican, 15–16 Cobblestone malformations, 169 Collagens, 392–395, 399 BM-associated, 36–38 ColQ, 38 in ECM, 33–34 transmembrane, 34–36 Conditioned place preference (CPP), 265–266, 267–268, 269 Confocal reflection microscopy, 290–291 Congenital microcephaly, 165 Coxsackievirus, 372–374 C1qDC family proteins Cbln1, 40–41 C1q, 39 profiles of, 38–39 CRASH syndrome, 375–376 CSPGs See Chondroitin sulfate proteoglycans (CSPGs) D Disulfiram, 326 Drug addiction alcohol, 270–271 animal models, 267b, 267f behavioral sensitization, 267, 268 conditioned place preference paradigm, 265–266, 267–268 definition, 265 drug self-administration paradigm, 265–266, 268 integrin receptors, 118 MMP-9, 148 opioids, 265–267, 267b, 267f perineuronal nets, 357–358 psychostimulants, 268–270 synaptic plasticity, 271 tPA/plasmin system, 147 E ECM See Extracellular matrix (ECM) ECS See Extracellular space (ECS) Electroencephalographic (EEG) activity, 246 Endothelial basement membranes (EBMs), 193–194 Epilepsy autism and schizophrenia, 246–249 integrins, 370–371 LGI1, 240–241 ADAM22 and ADAM23, 241–242, 242f developmental role of, 243 Kv1.1, 241 LRR, 239–240 MMPs, 235–238 Index perineuronal nets, 357–358 PET imaging, 245 uPAR interactome components of, 230–231, 231f expression and role, 232t FPRL1, 234 integrins, 235 kininogen, 234 LRP-1, 234 PDGFR-b, 234–235 SRPX2, 233 uPA–uPAR interaction, 233 vitronectin, 233 Epileptogenesis definition, 230 18 F-FDG PET, 244 MMPs, 235–238 neuroimaging, 244 perineuronal nets, 238–239 uPAR interactome components of, 230–231, 231f expression and role, 232t FPRL1, 234 integrins, 235 kininogen, 234 LRP-1, 234 PDGFR-b, 234–235 SRPX2, 233 uPA–uPAR interaction, 233 vitronectin, 233 Erythropoietin (EPO) EAE, 366 hypoxia and ischemia, 366 Euonymus alatus, 361 Experimental autoimmune encephalomyelitis (EAE), 194–197, 366 Extracellular matrix (ECM) AFM, 289 ALM, 290 Alzheimer’s disease (see Alzheimer’s disease (AD)) ASD (see Autism spectrum disorder (ASD)) axon initial segment, 84–85 L-type voltage-gated calcium channels, 88–90 nodes of Ranvier, 90–93, 91f PNNs, 88–90, 89f CAMs (see Cell adhesion molecules (CAMs)) confocal reflection microscopy, 290–291 CSPGs (see Chondroitin sulfate proteoglycans (CSPGs)) drug addiction (see Drug addiction) ECM mimetics acellular therapies, 397 advantages, 402 agarose, 400 alginate, 400 applications of, 393f bioengineered ECM scaffolds, 398 cell-based therapies, 397 cell transplantation strategies, 397 chitosan, 401 collagen, 399 diffusion-based delivery systems, 398 fibrin, 401 fibronectin, 401–402 HA-derived materials, 399–400 hydrogels, 398, 402 in vitro cell culture experiments, 395, 399 lactide- and glycolide-derived polyesters, 403 Matrigel™, 400–401 nanostructured materials, 404 NeuroGel™, 404 PEG, 402–403 poly(2-hydroxyethyl methacrylate), 404 polycaprolactones, 403 requirements and considerations for, 394f scaffold and host tissue, interaction of, 395–396 self-assembling materials, 404–405 soluble factors, 397–398 translational potential, 405 enzymatic and acute manipulations, 57t epilepsy (see Epilepsy) fibrillar proteins and glycosaminoglycans, 392–395 FRET-based methods (see F€ orster resonance energy transfer (FRET)) FTIR, 292–293 functions of, 392–395, 393f homeostatic synaptic plasticity brevican, ADAMTS4, 85–86 GABAergic synapses, 86–87 HA-based ECM, 85–86 heparan sulfates, 86 narp, 86–87 neuronal firing, 82 ocular dominance plasticity, 87–88 perineuronal nets, 83–85, 83f set point, readjustment, 82 TNF-a signaling, 87–88 HSPGs (see Heparan sulfate proteoglycans (HSPGs)) integrins (see Integrins) in vivo imaging of, 171 463 464 Index Extracellular matrix (ECM) (Continued) labeling strategies, proteolytic remodeling DQ substrates, 297–298 fluorochrome labels, 297 HA labeling, 293–294 immunodetection, 296 in gel zymography, 298 ISZ, 298–299 IVZ, 298, 299 VVL labeling, 294–296, 294f, 295f WFA labeling, 294–296 in laminar and connectivity development early human fetal brain, 160–162, 161f midfetal period, 162–164, 163f third gestational trimester and early postnatal year, 164 learning (see Learning) MCD (see Malformations of cortical development (MCD)) memory (see Memory) MMPs (see Matrix metalloproteinases (MMPs)) mood disorders (see Mood disorders) multiphoton-excitation microscopy, 291–292 OCT, 292 schizophrenia (see Schizophrenia (SZ)) SEM, 289–290 SHIM, 291–292 stroke (see Stroke) structures, 54 superresolution imaging, 293 synaptic plasticity (see Synaptic plasticity) synaptic quadriga, 54 tetrapartite synapse, 54 Extracellular matrix metalloproteinase inducer (EMMPRIN), 361 Extracellular space (ECS), 212–213 F Fear memory, 183–184 Fibrin, 401 Fibronectin, 401–402 Focal cortical dysplasias (FCDs), 165–168, 169 Formyl peptide G protein-coupled receptor (FPRL1), 234 F€ orster resonance energy transfer (FRET), 299–300 fluorescence lifetime approaches, 300 FRET-based biosensors, 303–305, 304f GDNF, 301 HB-GAM, 301 intensity-based FRET approaches, 300–301 Fourier transform infrared microspectroscopy (FTIR), 292–293 Fragile X mutation protein (FRMP), 246–247 Fragile X syndrome (FXS), 170, 246–247 G Gangliogliomas (GGs), 165–168, 166t Glial cell line-derived neurotrophic factor (GDNF), 301 Glioblastoma ADAMTS inhibitors, 367 captopril and disulfiram, 360 cathepsin B inhibitors, 368 integrins, 368–369 Glycans, 293–296, 294f, 295f Glycosaminoglycans (GAGs), 392–395 G protein-coupled receptor (GPCR), 234 H HA See Hyaluronic acid (HA) HA-binding proteins (HABPs), 293–294 Heparan sulfate proteoglycans (HSPGs), 16–17, 248 agrin, 112–113 Alzheimer’s disease, 181–182 astrocyte-derived ECM, 31 Ab/ADDLs AMPA and NMDA receptors, 210–211 amyloid plaques, 209 in vivo and in vitro studies, 209 synapses, glypicans and syndecans, 210 synaptic plasticity, learning and memory, 66–68 syndecan receptors, 110–112 Heparan sulfates (HSs) Alzheimer’s disease, 356–357 homeostatic plasticity, 86 synaptic plasticity, learning and memory, 66–68 Heparin-binding growth-associated molecule (HB-GAM), 301 Hepatocyte growth factor (HGF), 247–248 Histone deacetylase (HDAC) inhibitors, 360 Homeostatic plasticity brevican, ADAMTS4, 85–86 GABAergic synapses, 86–87 HA-based ECM, 85–86 heparan sulfates, 86 narp, 86–87 neuronal firing, 82 ocular dominance plasticity, 87–88 perineuronal nets, 83–85, 83f set point, readjustment, 82 TNF-a signaling, 87–88 HSPGs See Heparan sulfate proteoglycans (HSPGs) Hyaluronan- and proteoglycan-binding link protein (HAPLN), 61–62 Index Hyaluronan synthase (HAS3), 239 Hyaluronic acid (HA), 293–294 CSF levels, in AD patients, 61 epileptic seizures, 61 hyaluronan synthetases, 60 laminar and connectivity development early human fetal brain, 160–162 midfetal period, 162–164, 163f memory, 60 reversal learning process, 60–61 Hypoxia, 366 I ICAM-5 See Intercellular adhesion molecule-5 (ICAM-5) In situ zymography (ISZ), 298–299 Integrins addiction, 118 Alzheimer’s disease, 371 ASDs, 118 CSPGs, 103, 105 epilepsy, 370–371 glioblastoma, 368–369 injury and stroke, 369–370 intellectual disability, 117–118 kinase signaling, 108–109 laminins, 105 in learning and memory, 108 LTP, 105–106 and MMPs, 109–110 multiple sclerosis and neuroinflammation, 369 RGD receptors, 103–104 Sema7A, 104 SPARC, 104 structure, 102–103 in synaptic plasticity glutamate release, probability of, 105–106 integrin a subunits, 107–108 integrin b1 receptors, 106–107 integrin b3 receptors, 107 TLCN–b1 integrin interaction, 104–105 Integrin signaling a- and b-subunit, 445–448, 446f cell–matrix adhesions beads, 449–451 FAK, 448–449 long-term potentiation, 444, 452–453 paxillin recruitment (see Paxillin) tension-mediated intracellular signaling, 449–451 functions, 444 Intercellular adhesion molecule-5 (ICAM-5), 270, 375 In vivo zymography (IVZ), 298, 299 K Kallikreins, 359 Kininogen, 234 L Learning CSPGs, 59–60 genetic manipulations, effects of, 55t HSPGs, 66–68 hyaluronic acid, 60–61 integrin receptors, 108 MMP-9, 141–143 neuropsin, 145 neurotrypsin, 146–147 plasminogen-activating system, 358–359 reelin, 68, 69 tenascin-C, 64–65 tenascin-R, 63 tenascin-X, 66 TIMPs and MMPs, 314–315 tPA/plasmin system, 143–144 Leucine-rich, glioma-inactivated (LGI1) gene LRR, 239–240 and TLE ADAM22 and ADAM23, 241–242, 242f developmental role of, 243 epilepsy, 240–241, 241f Kv1.1, 241 Leucine-rich repeat containing 15 (LRRC15), 376 Leucine-rich repeats (LRR), 239–240 Leucine-rich repeat transmembrane neuronal (LRRTM4) protein, 210 Lipoprotein receptor-related protein (LRP1), 209 Lipoprotein receptors (LPRs) ApoER2, 114 low-density LRP, 115–116, 118–119 reelin, 113–114 VLDLR, 111f, 114, 115f Lissencephaly, 160–162, 169 Long-term depression (LTD) ChABC treatment, 54–58 TN-C, 64 TN-R, 63 Long-term potentiation (LTP) ChABC treatment, 54–59 HB-GAM receptor, 66–67 hyaluronic acid, 60 integrins, 105–106, 107–108, 444, 452–453 465 466 Index Long-term potentiation (LTP) (Continued) MMP-9, 141–143 MMP/TIMP system, 314–315 TN-C, 64 TN-R, 63 Low-density lipoprotein receptor (LDLR) Alzheimer’s disease, 118–119 synaptic transmission, 115–116 Low-density lipoprotein receptor-related protein (LRP-1), 234 Low-density lipoprotein-related protein (LRP), 115–116 LPRs See Lipoprotein receptors (LPRs) L1 syndrome, 375–376 LTP See Long-term potentiation (LTP) L-type voltage-dependent calcium channels (LVDCCs), 116–117 Luteolin, 360 M Magnolia obovata, 361 Major depressive disorder (MDD), 275–276 Malformations of cortical development (MCD), 166t cobblestone malformations, 169 congenital microcephaly, 165 FCD type II, 165–168 GG and TSC, 165–168 lissencephaly, 169 megalencephalies, 165 PMG, 168 seizures, 168 Marimastat, 367 Matrigel™, 400–401 Matrix metalloproteinase-9 (MMP-9), 236–237, 238, 246–247 Alzheimer’s disease, 216 anacardic acid, 361 arthritis patients, synovial fluid analysis, 197 aseptic meningitis, 329 autism spectrum disorders, 148, 170 bacterial meningitis, 327–329 bipolar disorder and schizophrenia, 148 captopril and disulfiram, 360 depression, 148 drug addiction, 148 FMRP, 246–247 gelatin in-gel zymography technique, 201 inflammatory proteinase, 194–197 LTP and learning, 141–143, 142f Magnolia obovata and Euonymus alatus, 361 MMP-2/TIMP-1, production of, 194–197, 196t monomers and multimers, 193–194, 199, 200f, 202 MS autoimmunity, REGA model of, 193–194, 197, 198f neuroinflammation, 199–200 NGAL, 199 PBM, 193–194 regulation in leukocyte types, 194–197, 196t seizures, 168 siRNA gene silencing, 360 spines, evaluation of, 142f substrates and binding partners, 202 and tPA, 265–266, 267f zymographic analysis, 193–194 Matrix metalloproteinases (MMPs) activators and inhibitors of, 363t Alzheimer’s disease, 217–218 cancer treatment, 367 ECM degradation, 358 EMMPRIN, 361 expression and activation, regulation of, 137 FN-439, 269 integrin receptors, 109–110 marine organisms, 361 MMP-9 (see Matrix metalloproteinase-9 (MMP-9)) psychostimulant-induced locomotor sensitization, 269 structural and functional features of, 315–316 and TIMP Alzheimer’s disease, 314, 323–325 aseptic meningitis, 329 bacterial meningitis (see Bacterial meningitis (BM)) BBB and brain hemorrhage, 314 brain tumors, 314 CNS development and pathophysiology, 318–320 CNS expression, 315, 316t in EAE and MS, 320–323, 362–366 expression and activation, regulation of, 317 HTLV-1 infection, 314 learning, and memory, 314–315 MMP-3, 314 physiological tissue remodeling, 314 seizures and LTP, 314–315 targeted proteinases, 318, 319t timp and synapsin genes, 317–318 zinc-dependent proteases, 137 MCD See Malformations of cortical development (MCD) MEAs See Multielectrode arrays (MEAs) Membrane-associated collagens with interrupted triple helices (MACITs) collagens, 34 Index Memory CSPGs, 59–60 genetic manipulations, effects of, 55t HSPGs, 66–68 hyaluronic acid, 60 integrin receptors, 108 link proteins, 61–62 MMP-9, 141–143 neuropsin, 145 neurotrypsin, 146–147 reelin, 68, 69 tenascin-C, 64–65 tenascin-R, 63 tenascin-X, 66 TIMPs and MMPs, 314–315 Mero-CBD sensor, 305 Microcontact printing (mCP), 423–426, 424f, 425f Microfluidics, 423–426, 424f MMP-9 See Matrix metalloproteinase-9 (MMP-9) MMP inhibitors (MMPIs) in Alzheimer’s disease, 324–325 bacterial meningitis, 330–333, 331t BBB permeability, 336–337 compounds, 361 in EAE and MS, 322 structural classes of, 333–336, 334t MMPs See Matrix metalloproteinases (MMPs) Mood disorders and PNNs, 275 and reelin, 275–276 MS See Multiple sclerosis (MS) Multielectrode arrays (MEAs) active pixel sensor, 421 development of, 417–418 EPON SU-8 microstructures, 424f in vitro electrophysiology, 418f NeuroBIT project, 434f patterned grid networks, 435–436, 435f physical clustering microstructures, 434 primary neural cell cultures, 419–421, 420f, 422f substrate functionalization first-order statistical parameters, 433t PDL, 431–432, 432f PEI, 431–432, 432f 3D culturing system, 429–430, 430f Multiple sclerosis (MS) integrins, 369 MMP-9, 193–194, 197, 198f MMP/TIMP system, 320–323, 362–366 Myelin-associated glycoprotein (MAG), 320–321 Myelin basic protein (MBP), 320–321 N Nanodropping system, 424f, 427f Neoepitopes, 296 Neovastat, 361 Neprilysin (NEP), 366 Network topology, neural networks EPON SU-8, 423–426, 424f microcontact printing, 423–426, 424f, 425f microfluidic structures, 423, 424f nanodropping adhesion-promoting microspots, 424f, 427f surface functionalization and nanomaterials, 423–427, 425f, 427f Neural cell adhesion molecule (NCAM1), 375 Neural networks in vitro cell culture techniques, 417–418 network topology EPON SU-8, 423–426, 424f microcontact printing, 423–426, 424f, 425f microfluidic structures, 423, 424f nanodropping adhesion-promoting microspots, 424f, 427f surface functionalization and nanomaterials, 423–427, 425f, 427f Neural stem cells (NSCs) regulation asymmetrical division, 4–5 CSPG, 15–16 ECM receptors, 17–18 environmental asymmetry (see Stem cell niches) HSPGs, 16–17 neurogenesis, tenascin proteins, 6–8, 13–14 Neuroelectronics micro-/nanostructured substrates, neurons, 417–419 primary neuronal cultures, 419–421, 420f, 422f 3D neuronal cultures hydrogel/alginate scaffolds, 428–429, 428f matrix-like sponges, 428–429, 428f multilayered polyimide membrane approach, 430f nanofiber scaffolds, 428–429, 428f primary hippocampal cultures, 430f spheroids/organoids, 429 types of, 418–419, 418f NeuroGel™, 404 Neuronal activity-regulated pentraxin (Narp), 83f, 86–87 Neuronal pentraxin (NP1), 86–87 Neuropsin activity, regulation of, 136 bipolar disorder, 147 467 468 Index Neuropsin (Continued) inhibitors of, 136 kallikrein-related protease, 136, 144 schizophrenia, 147 in synaptic plasticity and behavior, 144–145 Neurotrypsin agrin, 137, 138f cognitive brain functions, 148 synaptic plasticity, learning and memory, 146–147 zymogen activation site, 136–137, 138f Neutrophil gelatinase B-associated lipocalin (NGAL), 199 NSCs See Neural stem cells (NSCs) regulation Nucleus accumbens (NAc), 265–266, 268, 269 O Object recognition (OR) memory, 184 Oligodendrocyte precursor cells (OPCs), 183 Opioids, 265–267, 267b, 267f Optical coherence tomography, 292 P Parenchymal basement membrane (PBM), 193–194 Parvalbumin-positive interneurons (PV-INs), 83f, 84, 86–87 Paxillin, 444 cell spreading and FAK recruitment, 449–451 GIT/PIX/PAK module, 451–452 LIM domains, 451 phosphorylation-dependent regulation, 451–452 stress-mediated recruitment, 449–451 talin–integrin-binding affinity, 449–451 PEI See Polyethylenimine (PEI) Perineuronal nets (PNNs) addiction, 357–358 Alzheimer’s disease, 182, 214–216 amblyopia, 184–185 axon initial segment, 88–90, 89f components of, 139 epilepsy, 357–358 fear memory, 183–184 functions of, 139 homeostatic plasticity, 83–85, 83f and mood disorders, 275 opiates, 266, 267f OR memory, 184 and schizophrenia, 272–274, 273f, 357–358 somatosensory/barrel cortex, 185 spinal cord injury, 183 stroke, 183, 185–186 structural components of, 180 synaptic plasticity and behavior, 139–140 VVL labeling, 294–296, 294f WFA labeling, 294–296 Perisylvian polymicrogyria (PMG), 168 Plasminogen activator inhibitors (PAIs), 358–359 Platelet-derived growth factor receptor-b (PDGFR-b), 234–235 PNNs See Perineuronal nets (PNNs) Polycaprolactones, 403 Poly-D-lysine (PDL), 429–430, 430f, 431–432, 432f Polyethylene glycol (PEG), 402–403 Polyethylenimine (PEI), 429–430, 430f, 431–432, 432f Proteoglycans (PGs), 179–180 astrocyte-derived ECM CSPGs, 30 HSPGs, 31 RGCs, 30 in vitro cell-culture insert system, 32–33 in vitro model, 31–32, 32f long-term potentiation (LTP), 32–33 Proteolytic beacons (PBs), 298, 299 Psychostimulants, 268–270 R Radial glial cells cortical expansion, molecular determinants, asymmetrical division, 4–5 subventricular zone, ventricular zone, symmetrical divisions, Reelin Alzheimer’s disease, 211–212 autism, 247 LPR receptors, 113–114 and mood disorders, 275–276 in neuronal migration, 160–162 and schizophrenia, 274 synaptic plasticity, learning and memory, 68–70 Rehabilitation amblyopia, 184–185 fear memory, 183–184 OR memory, 184 somatosensory/barrel cortex, 185 spinal cord injury, 183 stroke, 185–186 Retinal ganglion cell neurons (RGCs), 30 Reversion-inducing cysteine-rich protein with Kazal motifs (RECK), 360–361, 367–368 S Scanning electron microscopy (SEM), 289–290 Schizophrenia (SZ) ADAMTSL3, 169–170 CSPGs, 169–170, 249 Index MMP-9, 148 neuropsin, 147 perineuronal nets, 272–274, 273f, 357–358 reelin, 69, 169–170, 274 tPA/plasmin system, 147 Second-harmonic imaging microscopy (SHIM), 291–292 Secreted protein acidic and rich in cysteine (SPARC), 104, 182 Seizures hyaluronic acid, 61 integrins, 370–371 MMP-9, 168 MMP/TIMP system, 314–315 tPA/plasmin system, 147 Semaphorin 7A (Sema7A), 104 Serine proteases, 136–137 Spinal cord injury, 183, 186 Stem cell niches in adult CNS, 5–6 environmental asymmetry, laminin proteins, 14–15 Stochastic optical reconstruction microscopy (STORM), 293 Stroke CSPGs astrocytes, microglia, and OPCs, 183 ChABC treatment, 355 CS-E, 355 functional recovery, 185–186 glial scar formation, 183 phosphacan, 183 integrins, 369–370 NGAL–MMP-9 complex form, 199 tPA/plasmin system, 147 Subplate remnant (SPr), 164 Superresolution imaging, 293 Sushi-repeat protein X-linked (SRPX2), 233 Synaptic plasticity CSPGs, 54–59, 139–140 genetic manipulations, effects of, 55t homeostatic plasticity (see Homeostatic plasticity) HSPGs, 66–68 integrin receptors glutamate release, probability of, 105–106 integrin a subunits, 107–108 integrin b1 receptors, 106–107 integrin b3 receptors, 107 link proteins, 61–62 MMP-9, 141–143 neuropsin, 144–145 neurotrypsin, 146–147 plasminogen-activating system, 358–359 reelin, 68–70 tenascin-C, 64–66 tenascin-R, 63–64 tenascin-X, 66 tPA/plasmin system, 144 Synaptogenesis collagens, 33–38 C1qDC family proteins, 38–41 proteoglycans, 30–33 Syndecans, 110–112 SZ See Schizophrenia (SZ) T Temporal lobe epilepsy (TLE) ADAM22 and ADAM23, 241–242, 242f developmental role of, 243 epilepsy, 240–241, 241f Kv1.1, 241 Tenascin-C (TN-C), 32–33, 83–84 brain tumor, 182 learning and memory, 64–65 in mature stem cell niches, 8, 9f in NSCs, 13–14 N-terminus links, 6–8 in oligodendrocyte progenitors, 11–13 in radial glia and astrocyte progenitors Bergmann glia cells, 11, 12f delayed EGFR expression, 8–11 embryonic stem cell niche, 8–11, 10f Sam68 expression, 8–11 transcription factor Pax6, 8–11 spliced FNIII domains, 6–8 structure, 6–8, 7f synaptic plasticity, 65–66 Tenascin-R (TN-R), 83–84, 238–239 laminar and connectivity development early human fetal brain, 160–162 midfetal period, 162–164 learning, 63 memory, 63 synaptic plasticity, 63–64 Tenascin-X (TN-X), 66 Tetraspanin (TSPAN7), 116 Tetraspanins, 116 Time-correlated single-photon counting (TCSPC), 300 TIMP See Tissue inhibitors of metalloproteinase (TIMP) Tissue inhibitors of metalloproteinase (TIMP), 235–236, 237, 359 Alzheimer’s disease, 314, 323–325 aseptic meningitis, 329 bacterial meningitis (see Bacterial meningitis (BM)) 469 470 Index Tissue inhibitors of metalloproteinase (TIMP) (Continued) BBB and brain hemorrhage, 314 brain tumors, 314 CNS development and pathophysiology, 318–320 CNS expression, 315, 316t in EAE and MS, 320–323, 362–366 expression and activation, regulation of, 317 HTLV-1 infection, 314 learning, and memory, 314–315 MMP-3, 314 physiological tissue remodeling, 314 seizures and LTP, 314–315 targeted proteinases, 318, 319t timp and synapsin genes, 317–318 Tissue plasminogen activator (tPA) activity, regulation of, 136, 143 alcohol, 270–271 Alzheimer’s disease, 366 learning, 143–144 mental and thromboembolic disorders, 147 mRNA expression, 136 opiates, 265–266, 267f psychostimulants, 268 synaptic plasticity, 144 thrombolysis, 136 TN-C See Tenascin-C (TN-C) TN-R See Tenascin-R (TN-R) Trichostatin A, 269–270 Tuberous sclerosis complex (TSC), 165–168, 166t U Urokinase-type plasminogen activator receptor (uPAR) components of, 230–231, 231f expression and role of, 232t extracellular ligands of kininogen, 234 SRPX2, 233 uPA–uPAR interaction, 233 vitronectin, 233 lateral partners of FPRL1, 234 integrins, 235 LRP-1, 234 PDGFR-b, 234–235 TLE, 247–248 V Ventral tegmental area (VTA), 265 Very low-density lipoprotein receptor (VLDLR), 111f, 114, 115f, 234 Vicia villosa lectin (VVL), 294–296, 294f, 295f Vitronectin, 233 Volume transmission (VT), 212 Z Zymography, 298–299 Other volumes in PROGRESS IN BRAIN RESEARCH Volume 167: Stress Hormones and Post Traumatic Stress Disorder: Basic Studies and Clinical Perspectives, by E.R de Kloet, M.S Oitzl and E Vermetten (Eds.) – 2008, ISBN 978-0-444-53140-7 Volume 168: Models of Brain and Mind: Physical, Computational and Psychological Approaches, by R Banerjee and B.K Chakrabarti (Eds.) – 2008, ISBN 978-0-444-53050-9 Volume 169: Essence of Memory, by W.S Sossin, J.-C Lacaille, V.F Castellucci and S Belleville (Eds.) – 2008, ISBN 978-0-444-53164-3 Volume 170: Advances in Vasopressin and Oxytocin – From Genes to Behaviour to Disease, by I.D Neumann and R Landgraf (Eds.) – 2008, ISBN 978-0-444-53201-5 Volume 171: Using Eye Movements as an Experimental Probe of Brain Function—A Symposium in Honor of Jean Buăttner-Ennever, by Christopher Kennard and R John Leigh (Eds.) – 2008, ISBN 978-0-444-53163-6 Volume 172: Serotonin–Dopamine Interaction: Experimental Evidence and Therapeutic Relevance, by Giuseppe Di Giovanni, Vincenzo Di Matteo and Ennio Esposito (Eds.) – 2008, ISBN 978-0-444-53235-0 Volume 173: Glaucoma: An Open Window to Neurodegeneration and Neuroprotection, by Carlo Nucci, Neville N Osborne, Giacinto Bagetta and Luciano Cerulli (Eds.) – 2008, ISBN 978-0-444-53256-5 Volume 174: Mind and Motion: The Bidirectional Link Between Thought and Action, by Markus Raab, Joseph G Johnson and Hauke R Heekeren (Eds.) – 2009, 978-0-444-53356-2 Volume 175: Neurotherapy: Progress in Restorative Neuroscience and Neurology — Proceedings of the 25th International Summer School of Brain Research, held at the Royal Netherlands Academy of Arts and Sciences, Amsterdam, The Netherlands, August 25–28, 2008, by J Verhaagen, E.M Hol, I Huitinga, J Wijnholds, A.A Bergen, G.J Boer and D.F Swaab (Eds.) –2009, ISBN 978-0-12-374511-8 Volume 176: Attention, by Narayanan Srinivasan (Ed.) – 2009, ISBN 978-0-444-53426-2 Volume 177: Coma Science: Clinical and Ethical Implications, by Steven Laureys, Nicholas D Schiff and Adrian M Owen (Eds.) – 2009, 978-0-444-53432-3 Volume 178: Cultural Neuroscience: Cultural Influences On Brain Function, by Joan Y Chiao (Ed.) – 2009, 978-0-444-53361-6 Volume 179: Genetic models of schizophrenia, by Akira Sawa (Ed.) – 2009, 978-0-444-53430-9 Volume 180: Nanoneuroscience and Nanoneuropharmacology, by Hari Shanker Sharma (Ed.) – 2009, 978-0-444-53431-6 Volume 181: Neuroendocrinology: The Normal Neuroendocrine System, by Luciano Martini, George P Chrousos, Fernand Labrie, Karel Pacak and Donald W Pfaff (Eds.) – 2010, 978-0-444-53617-4 Volume 182: Neuroendocrinology: Pathological Situations and Diseases, by Luciano Martini, George P Chrousos, Fernand Labrie, Karel Pacak and Donald W Pfaff (Eds.) – 2010, 978-0-444-53616-7 Volume 183: Recent Advances in Parkinson’s Disease: Basic Research, by Anders Bj€orklund and M Angela Cenci (Eds.) – 2010,978-0-444-53614-3 Volume 184: Recent Advances in Parkinson’s Disease: Translational and Clinical Research, by Anders Bj€orklund and M Angela Cenci (Eds.) – 2010, 978-0-444-53750-8 Volume 185: Human Sleep and Cognition Part I: Basic Research, by Gerard A Kerkhof and Hans P.A Van Dongen (Eds.) – 2010, 978-0-444-53702-7 Volume 186: Sex Differences in the Human Brain, their Underpinnings and Implications, by Ivanka Savic (Ed.) – 2010, 978-0-444-53630-3 Volume 187: Breathe, Walk and Chew: The Neural Challenge: Part I, by Jean-Pierre Gossard, Re´jean Dubuc and Arlette Kolta (Eds.) – 2010, 978-0-444-53613-6 Volume 188: Breathe, Walk and Chew; The Neural Challenge: Part II, by Jean-Pierre Gossard, Re´jean Dubuc and Arlette Kolta (Eds.) – 2011, 978-0-444-53825-3 Volume 189: Gene Expression to Neurobiology and Behaviour: Human Brain Development and Developmental Disorders, by Oliver Braddick, Janette Atkinson and Giorgio M Innocenti (Eds.) – 2011, 978-0-444-53884-0 471 472 Other volumes in PROGRESS IN BRAIN RESEARCH Volume 190: Human Sleep and Cognition Part II: Clinical and Applied Research, by Hans P.A Van Dongen and Gerard A Kerkhof (Eds.) – 2011, 978-0-444-53817-8 Volume 191: Enhancing Performance for Action and perception: Multisensory Integration, Neuroplasticity and Neuroprosthetics: Part I, by Andrea M Green, C Elaine Chapman, John F Kalaska and Franco Lepore (Eds.) – 2011, 978-0-444-53752-2 Volume 192: Enhancing Performance for Action and Perception: Multisensory Integration, Neuroplasticity and Neuroprosthetics: Part II, by Andrea M Green, C Elaine Chapman, John F Kalaska and Franco Lepore (Eds.) – 2011, 978-0-444-53355-5 Volume 193: Slow Brain Oscillations of Sleep, Resting State and Vigilance, by Eus J.W Van Someren, Ysbrand D Van Der Werf, Pieter R Roelfsema, Huibert D Mansvelder and Fernando H Lopes da Silva (Eds.) – 2011, 978-0-444-53839-0 Volume 194: Brain Machine Interfaces: Implications For Science, Clinical Practice And Society, by Jens Schouenborg, Martin Garwicz and Nils Danielsen (Eds.) – 2011, 978-0-444-53815-4 Volume 195: Evolution of the Primate Brain: From Neuron to Behavior, by Michel A Hofman and Dean Falk (Eds.) – 2012, 978-0-444-53860-4 Volume 196: Optogenetics: Tools for Controlling and Monitoring Neuronal Activity, by Thomas Kn€opfel and Edward S Boyden (Eds.) – 2012, 978-0-444-59426-6 Volume 197: Down Syndrome: From Understanding the Neurobiology to Therapy, by Mara Dierssen and Rafael De La Torre (Eds.) – 2012, 978-0-444-54299-1 Volume 198: Orexin/Hypocretin System, by Anantha Shekhar (Ed.) – 2012, 978-0-444-59489-1 Volume 199: The Neurobiology of Circadian Timing, by Andries Kalsbeek, Martha Merrow, Till Roenneberg and Russell G Foster (Eds.) – 2012, 978-0-444-59427-3 Volume 200: Functional Neural Transplantation III: Primary and stem cell therapies for brain repair, Part I, by Stephen B Dunnett and Anders Bj€orklund (Eds.) – 2012, 978-0-444-59575-1 Volume 201: Functional Neural Transplantation III: Primary and stem cell therapies for brain repair, Part II, by Stephen B Dunnett and Anders Bj€orklund (Eds.) – 2012, 978-0-444-59544-7 Volume 202: Decision Making: Neural and Behavioural Approaches, by V.S Chandrasekhar Pammi and Narayanan Srinivasan (Eds.) – 2013, 978-0-444-62604-2 Volume 203: The Fine Arts, Neurology, and Neuroscience: Neuro-Historical Dimensions, by Stanley Finger, Dahlia W Zaidel, Franc¸ois Boller and Julien Bogousslavsky (Eds.) – 2013, 978-0-444-62730-8 Volume 204: The Fine Arts, Neurology, and Neuroscience: New Discoveries and Changing Landscapes, by Stanley Finger, Dahlia W Zaidel, Franc¸ois Boller and Julien Bogousslavsky (Eds.) – 2013, 978-0-444-63287-6 Volume 205: Literature, Neurology, and Neuroscience: Historical and Literary Connections, by Anne Stiles, Stanley Finger and Franc¸ois Boller (Eds.) – 2013, 978-0-444-63273-9 Volume 206: Literature, Neurology, and Neuroscience: Neurological and Psychiatric Disorders, by Stanley Finger, Franc¸ois Boller and Anne Stiles (Eds.) – 2013, 978-0-444-63364-4 Volume 207: Changing Brains: Applying Brain Plasticity to Advance and Recover Human Ability, by Michael M Merzenich, Mor Nahum and Thomas M Van Vleet (Eds.) – 2013, 978-0-444-63327-9 Volume 208: Odor Memory and Perception, by Edi Barkai and Donald A Wilson (Eds.) – 2014, 978-0-444-63350-7 Volume 209: The Central Nervous System Control of Respiration, by Gert Holstege, Caroline M Beers and Hari H Subramanian (Eds.) – 2014, 978-0-444-63274-6 Volume 210: Cerebellar Learning, Narender Ramnani (Ed.) – 2014, 978-0-444-63356-9 Volume 211: Dopamine, by Marco Diana, Gaetano Di Chiara and Pierfranco Spano (Eds.) – 2014, 978-0-444-63425-2 Volume 212: Breathing, Emotion and Evolution, by Gert Holstege, Caroline M Beers and Hari H Subramanian (Eds.) – 2014, 978-0-444-63488-7 Volume 213: Genetics of Epilepsy, by Ortrud K Steinlein (Ed.) – 2014, 978-0-444-63326-2 ... development in healthy and diseased human brain Prog Brain Res 214, 159–178 Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., Vargova, L., 2014 ECM in brain aging and dementia Prog Brain Res 214, ... Glial progenitors, Integrins, Laminin, Neural stem cell niche, Phosphacan, Proteoglycans, Radial glial cells, Subventricular zone, Tenascin Progress in Brain Research, Volume 214, ISSN 0079-6123,... compared to the functioning of the extracellular matrix in the brain, which although scarce plays a key role in initiation, maintenance, and plasticity of intercellular interactions in the nervous system