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Development and Maintenance of Epidermal Stem Cells in Skin Adnexa
International Journal of Molecular Sciences Review Development and Maintenance of Epidermal Stem Cells in Skin Adnexa Jaroslav Mokry * and Rishikaysh Pisal Medical Faculty, Charles University, 500 03 Hradec Kralove, Czech Republic; [email protected] * Correspondence: [email protected] Received: 30 October 2020; Accepted: 18 December 2020; Published: 20 December 2020 Abstract: The skin surface is modified by numerous appendages. These structures arise from epithelial stem cells (SCs) through the induction of epidermal placodes as a result of local signalling interplay with mesenchymal cells based on the Wnt–(Dkk4)–Eda–Shh cascade. Slight modifications of the cascade, with the participation of antagonistic signalling, decide whether multipotent epidermal SCs develop in interfollicular epidermis, scales, hair/feather follicles, nails or skin glands. This review describes the roles of epidermal SCs in the development of skin adnexa and interfollicular epidermis, as well as their maintenance. Each skin structure arises from distinct pools of epidermal SCs that are harboured in specific but different niches that control SC behaviour. Such relationships explain differences in marker and gene expression patterns between particular SC subsets. The activity of well-compartmentalized epidermal SCs is orchestrated with that of other skin cells not only along the hair cycle but also in the course of skin regeneration following injury. This review highlights several membrane markers, cytoplasmic proteins and transcription factors associated with epidermal SCs. Keywords: stem cell; epidermal placode; skin adnexa; signalling; hair pigmentation; markers; keratins 1. Epidermal Stem Cells as Units of Development 1.1. Development of the Epidermis and Placode Formation The embryonic skin at very early stages of development is covered by a surface ectoderm that is a precursor to the epidermis and its multiple derivatives. -
FLRT Proteins Are Endogenous Latrophilin Ligands and Regulate Excitatory Synapse Development
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Neuron Report FLRT Proteins Are Endogenous Latrophilin Ligands and Regulate Excitatory Synapse Development Matthew L. O’Sullivan,1,5 Joris de Wit,1,5 Jeffrey N. Savas,2 Davide Comoletti,3 Stefanie Otto-Hitt,1,6 John R. Yates III,2 and Anirvan Ghosh1,4,* 1Neurobiology Section, Division of Biology, University of California San Diego, La Jolla, CA 92093, USA 2Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA 3Child Health Institute of New Jersey and Department of Neuroscience and Cell Biology, UMDNJ/Robert Wood Johnson Medical School, New Brunswick, NJ 08901, USA 4CNS Discovery, F. Hoffmann-La Roche, 4070 Basel, Switzerland 5These authors contributed equally to this work 6Present address: Department of Natural Sciences, Carroll College, Helena, MT 59625, USA *Correspondence: [email protected] DOI 10.1016/j.neuron.2012.01.018 SUMMARY much effort has been expended investigating the mechanisms of a-latrotoxin action (Su¨ dhof, 2001), nothing is known about Latrophilins (LPHNs) are a small family of G protein- the endogenous function of latrophilins in vertebrates. Further coupled receptors known to mediate the massive evidence for the importance of latrophilins in the proper synaptic exocytosis caused by the black widow functioning of neural circuits comes from recent human spider venom a-latrotoxin, but their endogenous genetics studies that have linked LPHN3 mutations to attention ligands and function remain unclear. Mutations in deficit hyperactivity disorder (ADHD), a common and highly LPHN3 are strongly associated with attention deficit heritable developmental psychiatric disorder (Arcos-Burgos et al., 2010; Domene´ et al., 2011; Jain et al., 2011; Ribase´ s hyperactivity disorder, suggesting a role for latrophi- et al., 2011). -
Edinburgh Research Explorer
Edinburgh Research Explorer International Union of Basic and Clinical Pharmacology. LXXXVIII. G protein-coupled receptor list Citation for published version: Davenport, AP, Alexander, SPH, Sharman, JL, Pawson, AJ, Benson, HE, Monaghan, AE, Liew, WC, Mpamhanga, CP, Bonner, TI, Neubig, RR, Pin, JP, Spedding, M & Harmar, AJ 2013, 'International Union of Basic and Clinical Pharmacology. LXXXVIII. G protein-coupled receptor list: recommendations for new pairings with cognate ligands', Pharmacological reviews, vol. 65, no. 3, pp. 967-86. https://doi.org/10.1124/pr.112.007179 Digital Object Identifier (DOI): 10.1124/pr.112.007179 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Pharmacological reviews Publisher Rights Statement: U.S. Government work not protected by U.S. copyright General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 02. Oct. 2021 1521-0081/65/3/967–986$25.00 http://dx.doi.org/10.1124/pr.112.007179 PHARMACOLOGICAL REVIEWS Pharmacol Rev 65:967–986, July 2013 U.S. -
1 ICR-Geneset Gene List
ICR-geneset Gene List. IMAGE ID UniGene Locus Name Cluster 20115 Hs.62185 SLC9A6 solute carrier family 9 (sodium/hydrogen exchanger), isoform 6 21738 21899 Hs.78353 SRPK2 SFRS protein kinase 2 21908 Hs.79133 CDH8 cadherin 8, type 2 22040 Hs.151738 MMP9 matrix metalloproteinase 9 (gelatinase B, 92kD gelatinase, 92kD type IV collagenase) 22411 Hs.183 FY Duffy blood group 22731 Hs.1787 PHRET1 PH domain containing protein in retina 1 22859 Hs.356487 ESTs 22883 Hs.150926 FPGT fucose-1-phosphate guanylyltransferase 22918 Hs.346868 EBNA1BP2 EBNA1 binding protein 2 23012 Hs.158205 BLZF1 basic leucine zipper nuclear factor 1 (JEM-1) 23073 Hs.284244 FGF2 fibroblast growth factor 2 (basic) 23173 Hs.151051 MAPK10 mitogen-activated protein kinase 10 23185 Hs.289114 TNC tenascin C (hexabrachion) 23282 Hs.8024 IK IK cytokine, down-regulator of HLA II 23353 23431 Hs.50421 RB1CC1 RB1-inducible coiled-coil 1 23514 23548 Hs.71848 Human clone 23548 mRNA sequence 23629 Hs.135587 Human clone 23629 mRNA sequence 23658 Hs.265855 SETMAR SET domain and mariner transposase fusion gene 23676 Hs.100841 Homo sapiens clone 23676 mRNA sequence 23772 Hs.78788 LZTR1 leucine-zipper-like transcriptional regulator, 1 23776 Hs.75438 QDPR quinoid dihydropteridine reductase 23804 Hs.343586 ZFP36 zinc finger protein 36, C3H type, homolog (mouse) 23831 Hs.155247 ALDOC aldolase C, fructose-bisphosphate 23878 Hs.99902 OPCML opioid binding protein/cell adhesion molecule-like 23903 Hs.12526 Homo sapiens clone 23903 mRNA sequence 23932 Hs.368063 Human clone 23932 mRNA sequence 24004 -
The Intrinsically Disordered Proteins of Myelin in Health and Disease
cells Review Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease Arne Raasakka 1 and Petri Kursula 1,2,* 1 Department of Biomedicine, University of Bergen, Jonas Lies vei 91, NO-5009 Bergen, Norway; [email protected] 2 Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Aapistie 7A, FI-90220 Oulu, Finland * Correspondence: [email protected] Received: 30 January 2020; Accepted: 16 February 2020; Published: 18 February 2020 Abstract: Myelin ensheathes selected axonal segments within the nervous system, resulting primarily in nerve impulse acceleration, as well as mechanical and trophic support for neurons. In the central and peripheral nervous systems, various proteins that contribute to the formation and stability of myelin are present, which also harbor pathophysiological roles in myelin disease. Many myelin proteins have common attributes, including small size, hydrophobic segments, multifunctionality, longevity, and regions of intrinsic disorder. With recent advances in protein biophysical characterization and bioinformatics, it has become evident that intrinsically disordered proteins (IDPs) are abundant in myelin, and their flexible nature enables multifunctionality. Here, we review known myelin IDPs, their conservation, molecular characteristics and functions, and their disease relevance, along with open questions and speculations. We place emphasis on classifying the molecular details of IDPs in myelin, and we correlate these with their various functions, including susceptibility to post-translational modifications, function in protein–protein and protein–membrane interactions, as well as their role as extended entropic chains. We discuss how myelin pathology can relate to IDPs and which molecular factors are potentially involved. Keywords: myelin; intrinsically disordered protein; multiple sclerosis; peripheral neuropathies; myelination; protein folding; protein–membrane interaction; protein–protein interaction 1. -
Ɑ6ß1 Andɑ7ß1 Integrins Are Required in Schwann Cells to Sort
The Journal of Neuroscience, November 13, 2013 • 33(46):17995–18007 • 17995 Cellular/Molecular ␣61 and ␣71 Integrins Are Required in Schwann Cells to Sort Axons Marta Pellegatta,1,2 Ade`le De Arcangelis,3 Alessandra D’Urso,1 Alessandro Nodari,1 Desire´e Zambroni,1 Monica Ghidinelli,1,2 Vittoria Matafora,1 Courtney Williamson,2 Elisabeth Georges-Labouesse,3† Jordan Kreidberg,4 Ulrike Mayer,5 Karen K. McKee,6 Peter D. Yurchenco,6 Angelo Quattrini,1 Lawrence Wrabetz,1,2 and Maria Laura Feltri1,2 1San Raffaele Scientific Institute, Milano 20132, Italy, 2Hunter James Kelly Research Institute, University at Buffalo, State University of New York, New York 14203, 3Development and Stem Cells Program, Institut de Ge´ne´tique et de Biologie Mole´culaire et Cellulaire, Centre National de la Recherche Scientifique, Unite´ Mixte de Recherche 7104, Institut National de la Sante´ et de la Recherche Me´dicale U964, Universite´ de Strasbourg, Illkirch 67404, France, 4Department of Medicine, Children’s Hospital Boston and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts 02115, 5Biomedical Research Centre, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom, and 6Robert Wood Johnson Medical School, Piscataway, New Jersey, New Jersey 08854 During development, Schwann cells extend lamellipodia-like processes to segregate large- and small-caliber axons during the process of radial sorting. Radial sorting is a prerequisite for myelination and is arrested in human neuropathies because of laminin deficiency. Experiments in mice using targeted mutagenesis have confirmed that laminins 211, 411, and receptors containing the 1 integrin subunit are required for radial sorting; however, which of the 11 ␣ integrins that can pair with 1 forms the functional receptor is unknown. -
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Published OnlineFirst December 17, 2015; DOI: 10.1158/0008-5472.CAN-15-0884 Cancer Tumor and Stem Cell Biology Research Eva1 Maintains the Stem-like Character of Glioblastoma-Initiating Cells by Activating the Noncanonical NF-kB Signaling Pathway Naoki Ohtsu1, Yuka Nakatani2, Daisuke Yamashita3, Shiro Ohue3, Takanori Ohnishi3,and Toru Kondo1,2 Abstract Glioblastoma (GBM)–initiating cells (GIC) are a tumorigenic as Eva1 overexpression enhanced these properties. Eva1 deficien- subpopulation that are resistant to radio- and chemotherapies cy was also associated with decreased expression of stemness- and are the source of disease recurrence. Therefore, the identifi- related genes, indicating a requirement for Eva1 in maintaining cation and characterization of GIC-specific factors is critical GIC pluripotency. We further demonstrate that Eva1 induced GIC toward the generation of effective GBM therapeutics. In this study, proliferation through the activation of the RelB-dependent non- we investigated the role of epithelial V-like antigen 1 (Eva1, also canonical NF-kB pathway by recruiting TRAF2 to the cytoplasmic known as myelin protein zero-like 2) in stemness and GBM tail. Taken together, our findings highlight Eva1 as a novel tumorigenesis. Eva1 was prominently expressed in GICs in vitro regulator of GIC function and also provide new mechanistic and in stem cell marker (Sox2, CD15, CD49f)-expressing cells insight into the role of noncanonical NF-kB activation in GIC, derived from human GBM tissues. Eva1 knockdown in GICs thus offering multiple potential therapeutic targets for preclinical reduced their self-renewal and tumor-forming capabilities, where- investigation in GBM. Cancer Res; 76(1); 171–81. Ó2015 AACR. -
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PROBING THE INTERACTION OF ASPERGILLUS FUMIGATUS CONIDIA AND HUMAN AIRWAY EPITHELIAL CELLS BY TRANSCRIPTIONAL PROFILING IN BOTH SPECIES by POL GOMEZ B.Sc., The University of British Columbia, 2002 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF MASTER OF SCIENCE in THE FACULTY OF GRADUATE STUDIES (Experimental Medicine) THE UNIVERSITY OF BRITISH COLUMBIA (Vancouver) January 2010 © Pol Gomez, 2010 ABSTRACT The cells of the airway epithelium play critical roles in host defense to inhaled irritants, and in asthma pathogenesis. These cells are constantly exposed to environmental factors, including the conidia of the ubiquitous mould Aspergillus fumigatus, which are small enough to reach the alveoli. A. fumigatus is associated with a spectrum of diseases ranging from asthma and allergic bronchopulmonary aspergillosis to aspergilloma and invasive aspergillosis. Airway epithelial cells have been shown to internalize A. fumigatus conidia in vitro, but the implications of this process for pathogenesis remain unclear. We have developed a cell culture model for this interaction using the human bronchial epithelium cell line 16HBE and a transgenic A. fumigatus strain expressing green fluorescent protein (GFP). Immunofluorescent staining and nystatin protection assays indicated that cells internalized upwards of 50% of bound conidia. Using fluorescence-activated cell sorting (FACS), cells directly interacting with conidia and cells not associated with any conidia were sorted into separate samples, with an overall accuracy of 75%. Genome-wide transcriptional profiling using microarrays revealed significant responses of 16HBE cells and conidia to each other. Significant changes in gene expression were identified between cells and conidia incubated alone versus together, as well as between GFP positive and negative sorted cells. -
How Does Protein Zero Assemble Compact Myelin?
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 13 May 2020 doi:10.20944/preprints202005.0222.v1 Peer-reviewed version available at Cells 2020, 9, 1832; doi:10.3390/cells9081832 Perspective How Does Protein Zero Assemble Compact Myelin? Arne Raasakka 1,* and Petri Kursula 1,2 1 Department of Biomedicine, University of Bergen, Jonas Lies vei 91, NO-5009 Bergen, Norway 2 Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Aapistie 7A, FI-90220 Oulu, Finland; [email protected] * Correspondence: [email protected] Abstract: Myelin protein zero (P0), a type I transmembrane protein, is the most abundant protein in peripheral nervous system (PNS) myelin – the lipid-rich, periodic structure that concentrically encloses long axonal segments. Schwann cells, the myelinating glia of the PNS, express P0 throughout their development until the formation of mature myelin. In the intramyelinic compartment, the immunoglobulin-like domain of P0 bridges apposing membranes together via homophilic adhesion, forming a dense, macroscopic ultrastructure known as the intraperiod line. The C-terminal tail of P0 adheres apposing membranes together in the narrow cytoplasmic compartment of compact myelin, much like myelin basic protein (MBP). In mouse models, the absence of P0, unlike that of MBP or P2, severely disturbs the formation of myelin. Therefore, P0 is the executive molecule of PNS myelin maturation. How and when is P0 trafficked and modified to enable myelin compaction, and how disease mutations that give rise to incurable peripheral neuropathies alter the function of P0, are currently open questions. The potential mechanisms of P0 function in myelination are discussed, providing a foundation for the understanding of mature myelin development and how it derails in peripheral neuropathies. -
Hypomesus Transpacificus
Aquatic Toxicology 105 (2011) 369–377 Contents lists available at ScienceDirect Aquatic Toxicology jou rnal homepage: www.elsevier.com/locate/aquatox Sublethal responses to ammonia exposure in the endangered delta smelt; Hypomesus transpacificus (Fam. Osmeridae) ∗ 1 2 Richard E. Connon , Linda A. Deanovic, Erika B. Fritsch, Leandro S. D’Abronzo , Inge Werner Aquatic Toxicology Laboratory, Department of Anatomy, Physiology and Cell Biology, School of Veterinary Medicine, University of California, Davis, California 95616, United States a r t i c l e i n f o a b s t r a c t Article history: The delta smelt (Hypomesus transpacificus) is an endangered pelagic fish species endemic to the Received 9 May 2011 Sacramento-San Joaquin Estuary in Northern California, which acts as an indicator of ecosystem health Received in revised form 29 June 2011 in its habitat range. Interrogative tools are required to successfully monitor effects of contaminants upon Accepted 2 July 2011 the delta smelt, and to research potential causes of population decline in this species. We used microarray technology to investigate genome-wide effects in fish exposed to ammonia; one of multiple contami- Keywords: nants arising from wastewater treatment plants and agricultural runoff. A 4-day exposure of 57-day Hypomesus transpacificus + old juveniles resulted in a total ammonium (NH4 –N) median lethal concentration (LC50) of 13 mg/L, Delta smelt Microarray and a corresponding un-ionized ammonia (NH3) LC50 of 147 g/L. Using the previously designed delta + Biomarker smelt microarray we assessed altered gene transcription in juveniles exposed to 10 mg/L NH4 –N from Ammonia this 4-day exposure. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
Structural and Biochemical Changes Underlying a Keratoderma-Like Phenotype in Mice Lacking Suprabasal AP1 Transcription Factor Function
Citation: Cell Death and Disease (2015) 6, e1647; doi:10.1038/cddis.2015.21 OPEN & 2015 Macmillan Publishers Limited All rights reserved 2041-4889/15 www.nature.com/cddis Structural and biochemical changes underlying a keratoderma-like phenotype in mice lacking suprabasal AP1 transcription factor function EA Rorke*,1, G Adhikary2, CA Young2, RH Rice3, PM Elias4, D Crumrine4, J Meyer4, M Blumenberg5 and RL Eckert2,6,7,8 Epidermal keratinocyte differentiation on the body surface is a carefully choreographed process that leads to assembly of a barrier that is essential for life. Perturbation of keratinocyte differentiation leads to disease. Activator protein 1 (AP1) transcription factors are key controllers of this process. We have shown that inhibiting AP1 transcription factor activity in the suprabasal murine epidermis, by expression of dominant-negative c-jun (TAM67), produces a phenotype type that resembles human keratoderma. However, little is understood regarding the structural and molecular changes that drive this phenotype. In the present study we show that TAM67-positive epidermis displays altered cornified envelope, filaggrin-type keratohyalin granule, keratin filament, desmosome formation and lamellar body secretion leading to reduced barrier integrity. To understand the molecular changes underlying this process, we performed proteomic and RNA array analysis. Proteomic study of the corneocyte cross-linked proteome reveals a reduction in incorporation of cutaneous keratins, filaggrin, filaggrin2, late cornified envelope precursor proteins, hair keratins and hair keratin-associated proteins. This is coupled with increased incorporation of desmosome linker, small proline-rich, S100, transglutaminase and inflammation-associated proteins. Incorporation of most cutaneous keratins (Krt1, Krt5 and Krt10) is reduced, but incorporation of hyperproliferation-associated epidermal keratins (Krt6a, Krt6b and Krt16) is increased.