Human Oral Mucosa: Development, Structure and Function
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Ultrastructure and Immunocytochemistry of the Apodemes in the Chelae of the Blue Crab, Callinectes Sapidus
ULTRASTRUCTURE AND IMMUNOCYTOCHEMISTRY OF THE APODEMES IN THE CHELAE OF THE BLUE CRAB, CALLINECTES SAPIDUS Anne E. Leaser A Thesis Submitted to the University of North Carolina Wilmington in Partial Fulfillment of the Requirements for the Degree of Master of Science Department of Biology and Marine Biology University of North Carolina Wilmington 2010 Approved by Advisory Committee ________Thomas H. Shafer________ _________Robert D. Roer_________ _______Richard M. Dillaman______ Chair Accepted by ______________________________ Dean, Graduate School This thesis has been prepared in a style and format consistent with the journal The Journal of Structural Biology ii TABLE OF CONTENTS ABSTRACT...............................................................................................................................v ACKNOWLEDGMENTS .................................................................................................... viiii LIST OF TABLES................................................................................................................. viii LIST OF FIGURES ..................................................................................................................ix CHAPTER 1: ULTRASTRUCTURE AND IMMUNOCYTOCHEMISTRY OF THE APODEMES AND ASSOCIATED TISSUE IN THE CHELAE OF THE BLUE CRAB.......1 1. Introduction............................................................................................................................1 2. Materials and methods ...........................................................................................................4 -
Inherited Connective Tissue Disorders of Collagens: Lessons from Targeted Mutagenesis
13 Inherited Connective Tissue Disorders of Collagens: Lessons from Targeted Mutagenesis Christelle Bonod-Bidaud and Florence Ruggiero Institut de Génomique Fonctionnelle de Lyon, ENS de Lyon, UMR CNRS 5242, University Lyon 1, France 1. Introduction The extracellular matrix (ECM) is the cell structural environment in tissues and organs. The ECM is a dynamic structure that it is constantly remodelled. It contributes to tissue integrity and mechanical properties. It is also essential for maintaining tissue homeostasis, morphogenesis and differentiation, which it does, through specific interactions with cells. The ECM is composed of a mixture of water and macromolecules classified into four main categories: collagens, proteoglycans, elastic proteins, and non-collagenous glycoproteins (also called adhesive glycoproteins). The nature, concentration and ratio of the different ECM components are all important factors in the regulation of the assembly of complex tissue-specific networks tuned to meet mechanical and biological requirements of tissues. Collagens form a superfamily of 28 trimeric proteins, distinguishable from the other ECM components by their particular abundance in tissues (collagens represent up to 80-90% of total proteins in skin, tendon and bones) and their capacity to self-assemble into supramolecular organized structures (the best known being the banded fibers). The collagen superfamily is highly complex and shows a remarkable diversity in structure, tissue distribution and function (Ricard-Blum and Ruggiero, 2005). The importance -
Copyrighted Material
Part 1 General Dermatology GENERAL DERMATOLOGY COPYRIGHTED MATERIAL Handbook of Dermatology: A Practical Manual, Second Edition. Margaret W. Mann and Daniel L. Popkin. © 2020 John Wiley & Sons Ltd. Published 2020 by John Wiley & Sons Ltd. 0004285348.INDD 1 7/31/2019 6:12:02 PM 0004285348.INDD 2 7/31/2019 6:12:02 PM COMMON WORK-UPS, SIGNS, AND MANAGEMENT Dermatologic Differential Algorithm Courtesy of Dr. Neel Patel 1. Is it a rash or growth? AND MANAGEMENT 2. If it is a rash, is it mainly epidermal, dermal, subcutaneous, or a combination? 3. If the rash is epidermal or a combination, try to define the SIGNS, COMMON WORK-UPS, characteristics of the rash. Is it mainly papulosquamous? Papulopustular? Blistering? After defining the characteristics, then think about causes of that type of rash: CITES MVA PITA: Congenital, Infections, Tumor, Endocrinologic, Solar related, Metabolic, Vascular, Allergic, Psychiatric, Latrogenic, Trauma, Autoimmune. When generating the differential, take the history and location of the rash into account. 4. If the rash is dermal or subcutaneous, then think of cells and substances that infiltrate and associated diseases (histiocytes, lymphocytes, mast cells, neutrophils, metastatic tumors, mucin, amyloid, immunoglobulin, etc.). 5. If the lesion is a growth, is it benign or malignant in appearance? Think of cells in the skin and their associated diseases (keratinocytes, fibroblasts, neurons, adipocytes, melanocytes, histiocytes, pericytes, endothelial cells, smooth muscle cells, follicular cells, sebocytes, eccrine -
Nomina Histologica Veterinaria, First Edition
NOMINA HISTOLOGICA VETERINARIA Submitted by the International Committee on Veterinary Histological Nomenclature (ICVHN) to the World Association of Veterinary Anatomists Published on the website of the World Association of Veterinary Anatomists www.wava-amav.org 2017 CONTENTS Introduction i Principles of term construction in N.H.V. iii Cytologia – Cytology 1 Textus epithelialis – Epithelial tissue 10 Textus connectivus – Connective tissue 13 Sanguis et Lympha – Blood and Lymph 17 Textus muscularis – Muscle tissue 19 Textus nervosus – Nerve tissue 20 Splanchnologia – Viscera 23 Systema digestorium – Digestive system 24 Systema respiratorium – Respiratory system 32 Systema urinarium – Urinary system 35 Organa genitalia masculina – Male genital system 38 Organa genitalia feminina – Female genital system 42 Systema endocrinum – Endocrine system 45 Systema cardiovasculare et lymphaticum [Angiologia] – Cardiovascular and lymphatic system 47 Systema nervosum – Nervous system 52 Receptores sensorii et Organa sensuum – Sensory receptors and Sense organs 58 Integumentum – Integument 64 INTRODUCTION The preparations leading to the publication of the present first edition of the Nomina Histologica Veterinaria has a long history spanning more than 50 years. Under the auspices of the World Association of Veterinary Anatomists (W.A.V.A.), the International Committee on Veterinary Anatomical Nomenclature (I.C.V.A.N.) appointed in Giessen, 1965, a Subcommittee on Histology and Embryology which started a working relation with the Subcommittee on Histology of the former International Anatomical Nomenclature Committee. In Mexico City, 1971, this Subcommittee presented a document entitled Nomina Histologica Veterinaria: A Working Draft as a basis for the continued work of the newly-appointed Subcommittee on Histological Nomenclature. This resulted in the editing of the Nomina Histologica Veterinaria: A Working Draft II (Toulouse, 1974), followed by preparations for publication of a Nomina Histologica Veterinaria. -
Lysyl Hydroxylases. Studies on Recombinant Lysyl Hydroxylases and Mouse Lines Lacking Lysyl Hydroxylase 1 Or Lysyl Hydroxylase 3
D920etukansi.kesken.fm Page 1 Friday, March 30, 2007 9:33 AM D 920 OULU 2007 D 920 UNIVERSITY OF OULU P.O. Box 7500 FI-90014 UNIVERSITY OF OULU FINLAND ACTA UNIVERSITATIS OULUENSIS ACTA UNIVERSITATIS OULUENSIS ACTA D SERIES EDITORS Kati Takaluoma MEDICA KatiTakaluoma ASCIENTIAE RERUM NATURALIUM Professor Mikko Siponen LYSYL HYDROXYLASES BHUMANIORA Professor Harri Mantila STUDIES ON RECOMBINANT LYSYL HYDROXYLASES AND MOUSE LINES LACKING CTECHNICA LYSYL HYDROXYLASE 1 OR LYSYL HYDROXYLASE 3 Professor Juha Kostamovaara DMEDICA Professor Olli Vuolteenaho ESCIENTIAE RERUM SOCIALIUM Senior Assistant Timo Latomaa FSCRIPTA ACADEMICA Communications Officer Elna Stjerna GOECONOMICA Senior Lecturer Seppo Eriksson EDITOR IN CHIEF Professor Olli Vuolteenaho EDITORIAL SECRETARY Publications Editor Kirsti Nurkkala FACULTY OF MEDICINE, DEPARTMENT OF MEDICAL BIOCHEMISTRY AND MOLECULAR BIOLOGY, BIOCENTER OULU, ISBN 978-951-42-8427-4 (Paperback) UNIVERSITY OF OULU ISBN 978-951-42-8428-1 (PDF) ISSN 0355-3221 (Print) ISSN 1796-2234 (Online) ACTA UNIVERSITATIS OULUENSIS D Medica 920 KATI TAKALUOMA LYSYL HYDROXYLASES Studies on recombinant lysyl hydroxylases and mouse lines lacking lysyl hydroxylase 1 or lysyl hydroxylase 3 Academic dissertation to be presented, with the assent of the Faculty of Medicine of the University of Oulu, for public defence in the Auditorium of the Medipolis Research Center (Kiviharjuntie 11), on May 25th, 2007, at 13 p.m. OULUN YLIOPISTO, OULU 2007 Copyright © 2007 Acta Univ. Oul. D 920, 2007 Supervised by Docent Johanna Myllyharju Reviewed by Doctor Susanne Grässel Professor Nicholai Miosge ISBN 978-951-42-8427-4 (Paperback) ISBN 978-951-42-8428-1 (PDF) http://herkules.oulu.fi/isbn9789514284281/ ISSN 0355-3221 (Printed) ISSN 1796-2234 (Online) http://herkules.oulu.fi/issn03553221/ Cover design Raimo Ahonen OULU UNIVERSITY PRESS OULU 2007 Takaluoma, Kati, Lysyl hydroxylases. -
Collagen VI), Multiplexin (E.G
Essays in Biochemistry (2019) 63 297–312 https://doi.org/10.1042/EBC20180071 Review Article Basement membrane collagens and disease mechanisms Anna Gatseva1, Yuan Yan Sin1, Gaia Brezzo1,2 and Tom Van Agtmael1 1Institute of Cardiovascular and Medical Sciences, University of Glasgow, University Avenue, Glasgow G12 8QQ, United Kingdom; 2Centre for Discovery Brain Sciences, Medical Downloaded from https://portlandpress.com/essaysbiochem/article-pdf/63/3/297/844117/ebc-2018-0071c.pdf by University of Glasgow user on 14 October 2019 School, University of Edinburgh, Edinburgh EH16 4SB, United Kingdom Correspondence: Tom Van Agtmael ([email protected]) Basement membranes (BMs) are specialised extracellular matrix (ECM) structures and col- lagens are a key component required for BM function. While collagen IV is the major BM collagen, collagens VI, VII, XV, XVII and XVIII are also present. Mutations in these collagens cause rare multi-systemic diseases but these collagens have also been associated with major common diseases including stroke. Developing treatments for these conditions will require a collective effort to increase our fundamental understanding of the biology of these collagens and the mechanisms by which mutations therein cause disease. Novel insights into pathomolecular disease mechanisms and cellular responses to these mutations has been exploited to develop proof-of-concept treatment strategies in animal models. Com- bined, these studies have also highlighted the complexity of the disease mechanisms and the need to obtain a more complete understanding of these mechanisms. The identification of pathomolecular mechanisms of collagen mutations shared between different disorders represent an attractive prospect for treatments that may be effective across phenotypically distinct disorders. -
Recombinant Human Collagen XV Α1/COL15A1, Immobilized at 0.5 Μg/Ml, Is Able to Significantly Enhance Neurite Outgrowth
Recombinant Human Collagen XV α1/COL15A1 Catalog Number: 9854-CL DESCRIPTION Source Human embryonic kidney cell, HEK293derived Human COL15A1 Hemagglutinin Tag (Asn1133Ser1381) (YPYDVPDYA) Accession # P39059 Nterminal Sequence Tyr Analysis Structure / Form Noncovalentlylinked homotrimer Predicted Molecular 29 kDa Mass SPECIFICATIONS SDSPAGE 2636 kDa, reducing conditions Activity Measured by its ability to enhance neurite outgrowth of E16E18 rat embryonic cortical neurons. Recombinant Human Collagen XV α1/COL15A1, immobilized at 0.5 μg/mL, is able to significantly enhance neurite outgrowth. Endotoxin Level <0.10 EU per 1 μg of the protein by the LAL method. Purity >95%, by SDSPAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. Formulation Lyophilized from a 0.2 μm filtered solution in PBS. See Certificate of Analysis for details. PREPARATION AND STORAGE Reconstitution Reconstitute at 500 μg/mL in PBS. Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw cycles. l 12 months from date of receipt, 20 to 70 °C as supplied. l 1 month, 2 to 8 °C under sterile conditions after reconstitution. l 3 months, 20 to 70 °C under sterile conditions after reconstitution. BACKGROUND Recombinant human Collagen XV α1/COL15A1 is the Cterminal endostatinlike domain (amino acids 11331381) of human Collagen XV. Collagen XV is one of the two members of a vertebrate collagen family termed multiplexins. The other member of this family is Collagen XVIII. This family is characterized by a collagen triple helix region that is interrupted by several noncollagenous stretches, as well as a Cterminal nontriple helical NC1 domain (1, 2). -
Architectural Delineation and Molecular Identification Of
© 2017. Published by The Company of Biologists Ltd | Biology Open (2017) 6, 1383-1390 doi:10.1242/bio.026336 RESEARCH ARTICLE Architectural delineation and molecular identification of extracellular matrix in ascidian embryos and larvae Jiankai Wei1, Guilin Wang1, Xiang Li1, Ping Ren1, Haiyan Yu1 and Bo Dong1,2,3,* ABSTRACT date, 28 types of collagens and >40 distinct α-chains have been The extracellular matrix (ECM) not only provides essential physical identified in vertebrates (Ricard-Blum, 2011). Collagens play scaffolding for cellular constituents but also initiates crucial structural roles and contribute to mechanical properties, biochemical and biomechanical cues that are required for tissue organization and pattern shaping of tissues. Proteoglycans are morphogenesis. In this study, we utilized wheat germ agglutinin characterized by a core protein that is covalently linked to (WGA) staining to characterize the ECM architecture in ascidian glycosaminoglycans (GAGs), which are long, negatively charged embryos and larvae. The results showed three distinct populations of and linear chains of disaccharide repeats. The primary biological ECM presenting in Ciona embryogenesis: the outer layer localized at function of proteoglycans derives from the biochemical and the surface of embryo, an inner layer of notochord sheath and the hydrodynamic characteristics of the GAGs, which bind water to apical ECM secreted by the notochord. To further elucidate the provide hydration and compressive resistance (Mouw et al., 2014). precise structure of Ciona -
Prolyl Hydroxylases, Cloning and Characterization of Novel Human
D957etukansi.kesken.fm Page 1 Thursday, November 15, 2007 11:23 AM D 957 OULU 2007 D 957 UNIVERSITY OF OULU P.O. Box 7500 FI-90014 UNIVERSITY OF OULU FINLAND ACTA UNIVERSITATIS OULUENSIS ACTA UNIVERSITATIS OULUENSIS ACTA D SERIES EDITORS Päivi Fonsén MEDICA PäiviFonsén ASCIENTIAE RERUM NATURALIUM Professor Mikko Siponen PROLYL HYDROXYLASES BHUMANIORA Professor Harri Mantila CLONING AND CHARACTERIZATION OF NOVEL HUMAN AND PLANT PROLYL 4-HYDROXYLASES, CTECHNICA AND THREE HUMAN PROLYL 3-HYDROXYLASES Professor Juha Kostamovaara DMEDICA Professor Olli Vuolteenaho ESCIENTIAE RERUM SOCIALIUM Senior Assistant Timo Latomaa FSCRIPTA ACADEMICA Communications Officer Elna Stjerna GOECONOMICA Senior Lecturer Seppo Eriksson EDITOR IN CHIEF Professor Olli Vuolteenaho EDITORIAL SECRETARY Publications Editor Kirsti Nurkkala FACULTY OF MEDICINE, DEPARTMENT OF MEDICAL BIOCHEMISTRY AND MOLECULAR BIOLOGY, BIOCENTER OULU, ISBN 978-951-42-8672-8 (Paperback) COLLAGEN RESEARCH UNIT, ISBN 978-951-42-8673-5 (PDF) UNIVERSITY OF OULU ISSN 0355-3221 (Print) ISSN 1796-2234 (Online) ACTA UNIVERSITATIS OULUENSIS D Medica 957 PÄIVI FONSÉN PROLYL HYDROXYLASES Cloning and characterization of novel human and plant prolyl 4-hydroxylases, and three human prolyl 3-hydroxylases Academic dissertation to be presented, with the assent of the Faculty of Medicine of the University of Oulu, for public defence in Auditorium F101 of the Department of Physiology (Aapistie 7), on December 21st, 2007, at 10 a.m. OULUN YLIOPISTO, OULU 2007 Copyright © 2007 Acta Univ. Oul. D 957, 2007 Supervised by Professor Johanna Myllyharju Docent Peppi Karppinen Reviewed by Professor Joachim Fandrey Professor Dörthe Katschinski ISBN 978-951-42-8672-8 (Paperback) ISBN 978-951-42-8673-5 (PDF) http://herkules.oulu.fi/isbn9789514286735/ ISSN 0355-3221 (Printed) ISSN 1796-2234 (Online) http://herkules.oulu.fi/issn03553221/ Cover design Raimo Ahonen OULU UNIVERSITY PRESS OULU 2007 Fonsén, Päivi, Prolyl hydroxylases. -
A Noninvasive Mucinous Cystic Neoplasm
Li et al. Diagnostic Pathology 2012, 7:89 http://www.diagnosticpathology.org/content/7/1/89 CASE REPORT Open Access A noninvasive mucinous cystic neoplasm with intermediate-grade dysplasia of the pancreas and extensive squamous metaplasia: a case report with clinicopathological correlation Peifeng Li1,2†, Yingmei Wang1†, Qingqing Zhang3, Yixiong Liu1, Yang Lv1 and Zhe Wang1* Abstract: Squamous metaplasia presenting in noninvasive mucinous cystic neoplasm (MCN) of the pancreas is extremely rare. We described a case of 39-year-old Chinese female with a 5-year history of a slow growing mass in the left upper abdomen and an 18-month history of surgical incision exudation. The patient underwent cystojejunostomy, laparotomy and distal pancreatectomy consecutively because of the initial diagnosis of “pancreatic cyst”. The histological section showed columnar mucin-producing epithelium formed small papillary projections and extensively visible squamous metaplasia. Therefore the diagnosis of “noninvasive MCN with intermediate-grade dysplasia of the pancreas and extensive squamous metaplasia” was made finally. The squamous component of the pancreas may be derived from pluripotent stem cells, and may be in association with cystojejunostomy. Virtual slides: The virtual slide(s) for this article can be found here http://www.diagnosticpathology.diagnomx.eu/ vs/1322364365718540 Keywords: Mucinous cystic neoplasm, Squamous metaplasia, Pancreas, Immunohistochemistry Background extensive squamous metaplasia. In addition, we discuss the Mucinous cystic neoplasm (MCN) is a rare exocrine pathogenesis of squamous metaplasia and its clinicopatho- pancreatic tumor that can be classified into four histo- logical correlation. pathological types [1]: noninvasive MCN with low-grade, intermediate-grade or high-grade dysplasia and invasive Case presentation MCN. -
Hydrolyzed Collagen—Sources and Applications
molecules Review Hydrolyzed Collagen—Sources and Applications Arely León-López 1, Alejandro Morales-Peñaloza 2,Víctor Manuel Martínez-Juárez 1, Apolonio Vargas-Torres 1, Dimitrios I. Zeugolis 3,4 and Gabriel Aguirre-Álvarez 1,* 1 Instituto de Ciencias Agropecuarias, Universidad Autónoma del Estado de Hidalgo, Av. Universidad km 1. Ex Hacienda de Aquetzalpa. Tulancingo, Hidalgo 43600, Mexico; [email protected] (A.L.-L.); [email protected] (V.M.M.-J.); [email protected] (A.V.-T.) 2 Universidad Autónoma del Estado de Hidalgo, Escuela Superior de Apan, Carretera Apan-Calpulalpan s/n, Colonia, Chimalpa Tlalayote, Apan, Hidalgo 43920 Mexico; [email protected] 3 Regenerative, Modular & Developmental Engineering Laboratory (REMODEL), National University of Ireland Galway (NUI Galway), H91 TK33 Galway, Ireland; [email protected] 4 Science Foundation Ireland (SFI) Centre for Research in Medical Devices (CÚRAM) National University of Ireland Galway (NUI Galway), H91 TK33 Galway, Ireland * Correspondence: [email protected]; Tel.: +52-775-145-9265 Academic Editors: Manuela Pintado, Ezequiel Coscueta and María Emilia Brassesco Received: 7 October 2019; Accepted: 5 November 2019; Published: 7 November 2019 Abstract: Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. -
Hücre Biyolojisi
HÜCRE BİYOLOJİSİ Makrotransfer Ders: 7 Dr. Öğretim Üyesi Banu EREN • MAKRO TRANSFER: • Su, yağlar, mineral madde iyonlarının hücre zarında değişiklik olmaksızın osmoz, difüzyon gibi olaylar ile hücreye girişine mikrotransfer denir. • İri moleküllü proteinler, karbonhidratlar, nükleik asitler, büyük partiküller, bakteriler ve başkaları aynı yolla hücreye girip çıkamazlar. • Büyük moleküllerin taşınıması için hücre zarı tarafından özel yöntemler geliştirilmiştir. 2 • Sitozis; genel olarak plazma zarından makro moleküllerin geçişine denir. Kütle transportu olarakta tanımlayabiliriz. • Endositozis hücre içine doğru geçişlere, • Ekzositozis ise hücreler arası boşluğa veya dışarıya doğru olan çıkışlara denir. 3 • Endositoz alınan maddelerin katı yada sıvı oluşuna göre ikiye ayrılır. • Pinositoz ve Fagositoz. • Her iki olayda da gelen madde hücre zarında ki reseptörlere bağlanarak hücre içine alınır. 4 • Pinositoz: Moleküller ve kolloidal eriyiklerin, proteinler, karbonhidratlar, yağlar gibi küçük damlacıklar halinde alınmasıdır. • Böyle bir madde kütlesi reseptör aracılığı ile hücre zarına bağlanınca zar bu kısımda çukurlaşmaya başlar. • Gelen madde reseptör ile birlikte bu çukura yerleşir. • Zarın çukurlaşması gittikçe artar ve sonuda bu kısım içindeki maddeler ile birlikte hücre zarından koparak ufak bir kese halinde (pinositoz vesikülü) sitoplazma ya geçer. 5 • Şekillenen pinositoz keseciklerinin çapına göre pinositoz ikiye ayrılır. • 1-)Mikro pinositoz (=kesecikler 0,1mikron dan daha küçük ise) • 2-)Makro pinositoz (=kesecikler 0,1 ile 1 mikron arasında ise) • Makro pinositoz da kesecikler vakuol düzeyindedir. Işık mikroskobunda görülebilir. • Mikropinositoz dan farklı olarak gelen maddeyi kavramak üzere yalancı ayaklar meydana gelebilir. 6 • Pinositoz vezikülleri çabuk gelişir. • Hücre içinde veziküller 3 şekilde sonuca ulaşır; 7 1)Veziküller değişmeden hücreyi geçerler= • Hücrede oluşan pinosotetik veziküller (pinosomlar) hücrelerin diğer tarafından tekrar hücreyi terk ederler. •Buna sitopompis =transsitozis denir.