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Studies on the Proteome of Human Hair - Identifcation of Histones and Deamidated Keratins Received: 15 August 2017 Sunil S
www.nature.com/scientificreports OPEN Studies on the Proteome of Human Hair - Identifcation of Histones and Deamidated Keratins Received: 15 August 2017 Sunil S. Adav 1, Roopa S. Subbaiaih2, Swat Kim Kerk 2, Amelia Yilin Lee 2,3, Hui Ying Lai3,4, Accepted: 12 January 2018 Kee Woei Ng3,4,7, Siu Kwan Sze 1 & Artur Schmidtchen2,5,6 Published: xx xx xxxx Human hair is laminar-fbrous tissue and an evolutionarily old keratinization product of follicle trichocytes. Studies on the hair proteome can give new insights into hair function and lead to the development of novel biomarkers for hair in health and disease. Human hair proteins were extracted by detergent and detergent-free techniques. We adopted a shotgun proteomics approach, which demonstrated a large extractability and variety of hair proteins after detergent extraction. We found an enrichment of keratin, keratin-associated proteins (KAPs), and intermediate flament proteins, which were part of protein networks associated with response to stress, innate immunity, epidermis development, and the hair cycle. Our analysis also revealed a signifcant deamidation of keratin type I and II, and KAPs. The hair shafts were found to contain several types of histones, which are well known to exert antimicrobial activity. Analysis of the hair proteome, particularly its composition, protein abundances, deamidated hair proteins, and modifcation sites, may ofer a novel approach to explore potential biomarkers of hair health quality, hair diseases, and aging. Hair is an important and evolutionarily conserved structure. It originates from hair follicles deep within the der- mis and is mainly composed of hair keratins and KAPs, which form a complex network that contributes to the rigidity and mechanical properties. -
University of Alberta
University of Alberta T cell-mediated inflammation is stereotyped: mouse delayed-type hypersensitivity reaction and mouse T cell-mediated rejection of renal allografts share common molecular mechanisms by Jeffery M. Venner A thesis submitted to the Faculty of Graduate Studies and Research in partial fulfillment of the requirements for the degree of Master of Science in Experimental Medicine Department of Medicine ©Jeffery M. Venner Fall 2011 Edmonton, Alberta Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission. Dedicated to those who have inspired me: My family and friends, my teachers and mentors. You laid the foundation – my success is guaranteed ABSTRACT Genome-wide gene expression analysis of diseases has revealed large-scale changes in the expression of thousands of genes (transcripts) representing biological processes. The processes that occur during T cell-mediated rejection (TCMR) of renal allografts in mice and humans have been previously delineated, and they appear to be independent of cytotoxic mechanisms; thus, TCMR is analogous to delayed-type hypersensitivity (DTH). -
Supplementary Information
Supplementary Information A genomics approach reveals insights into the importance of gene losses for mammalian adaptations Sharma et al. The Supplementary Information contains - Supplementary Figures 1 - 35 - Supplementary Tables 1 - 8 - Supplementary Notes 1 - 8 1 A reference species with B annotated functional genes ? ? ? ? ? ? use Dollo parsimony ? ? to infer gene ancestry ? search for gene losses reference ? in query species ? ? ? ? ? non-ancestral branches Supplementary Figure 1: General framework for detecting gene losses in genome alignments. (A) Our approach considers all coding genes that are annotated and thus likely functional in a chosen reference species. We detect loss of a given gene in other query species by searching genome alignments for gene-inactivating mutations. Genome alignments are well-suited to detect gene losses for the following reasons. First, genome alignments can reveal the remnants of inactivated but not completely deleted genes, even if these genes are not expressed anymore and thus are not contained in a transcriptome or in mRNA/protein databases. Second, splice site mutations, which are one important class of inactivating mutations, can only be detected at the genomic but not at the mRNA/protein level. Third, information about missing sequence (assembly gaps, regions of low sequencing quality) are only visible by direct genome analysis. This is important as the absence of a gene in a gene/protein database or in a genomic BLAST run cannot distinguish between artifacts that perfectly mimic absence of a gene (such as large assembly gaps) and the complete deletion of a gene. Since gene loss in a query species requires that the common ancestor of the reference and this query species possessed the gene, we used Dollo parsimony to infer gene ancestry based on query species where the gene lacks any gene-inactivating mutations. -
Identification of Novel Wool Keratin Intermediate Filament Genes in Sheep Skin Z-D
222 Yu et al. – Wool keratin genes Identification of novel wool keratin intermediate filament genes in sheep skin Z-D. YU1*, S.W. GORDON1, 2, J.E. WILDERMOTH1, O.A.M. WALLACE1, A.J. NIXON1 and A.J. PEARSON1 1AgResearch Ruakura, Private Bag 3123, Hamilton 3240, New Zealand 2Excerpta Medica, Sing Pao Building New Wing, 101 King's Road, North Point, Hong Kong *Corresponding author: [email protected] ABSTRACT Keratin intermediate filament (KIF) genes encode key proteins for hair and wool formation. A total of 17 expressed human KIF genes involved in hair formation are annotated. However, to date, only eight wool KIF genes have been reported. In this study, six new cDNA sequences (KRT32, KRT33B, KRT34, KRT39, KRT40 and KRT82) representing previously unreported wool KIFs were identified using a contiguous ovine sequence library constructed primarily from ESTs. The expression of three other KIF genes (KRT36, KRT84 and KRT87) was confirmed by PCR using sheep skin total RNA. The analogue of human KRT37 (type I) was unable to be identified, while KRT87 (type II) was present in sheep but not in humans. Therefore 10 type I and seven type II KIF family members have been identified in sheep in comparison to 11 and six KIFs in the human. These 17 KIF genes are likely to represent the complete or near-complete set involved in wool formation. The annotation of these genes will facilitate investigation into their patterns of expression in wool follicles and their roles in the determination of fibre attributes. Key words: keratin intermediate filament; wool; gene expression. -
The Genetics of Hair Shaft Disorders
CONTINUING MEDICAL EDUCATION The genetics of hair shaft disorders AmyS.Cheng,MD,a and Susan J. Bayliss, MDb,c Saint Louis, Missouri Many of the genes causing hair shaft defects have recently been elucidated. This continuing medical education article discusses the major types of hair shaft defects and associated syndromes and includes a review of histologic features, diagnostic modalities, and findings in the field of genetics, biochemistry, and molecular biology. Although genetic hair shaft abnormalities are uncommon in general dermatology practice, new information about genetic causes has allowed for a better understanding of the underlying pathophysiologies. ( J Am Acad Dermatol 2008;59:1-22.) Learning objective: At the conclusion of this article, the reader should be familiar with the clinical presentation and histologic characteristics of hair shaft defects and associated genetic diseases. The reader should be able to recognize disorders with hair shaft abnormalities, conduct appropriate referrals and order appropriate tests in disease evaluation, and select the best treatment or supportive care for patients with hair shaft defects. EVALUATION OF THE HAIR progresses via interactions with the mesenchymal For the student of hair abnormalities, a full review dermal papillae, leading to the formation of anagen of microscopic findings and basic anatomy can be hairs with complete follicular components, including found in the textbook Disorders of Hair Growth by sebaceous and apocrine glands.3 Elise Olsen,1 especially the chapter on ‘‘Hair Shaft Anagen hair. The hair shaft is composed of three Disorders’’ by David Whiting, which offers a thor- layers, called the medulla, cortex, and cuticle (Fig 1). ough review of the subject.1 The recognition of the The medulla lies in the center of the shaft and anatomic characteristics of normal hair and the effects contains granules with citrulline, an amino acid, of environmental factors are important when evalu- which is unique to the medulla and internal root ating a patient for hair abnormalities. -
Exploring Molecular Mechanisms Controlling Skin Homeostasis and Hair Growth
Exploring Molecular Mechanisms Controlling Skin Homeostasis and Hair Growth. MicroRNAs in Hair-cycle-Dependent Gene Regulation, Hair Growth and Associated Tissue Remodelling. Item Type Thesis Authors Ahmed, Mohammed I. Rights <a rel="license" href="http://creativecommons.org/licenses/ by-nc-nd/3.0/"><img alt="Creative Commons License" style="border-width:0" src="http://i.creativecommons.org/l/by- nc-nd/3.0/88x31.png" /></a><br />The University of Bradford theses are licenced under a <a rel="license" href="http:// creativecommons.org/licenses/by-nc-nd/3.0/">Creative Commons Licence</a>. Download date 02/10/2021 08:52:54 Link to Item http://hdl.handle.net/10454/5204 University of Bradford eThesis This thesis is hosted in Bradford Scholars – The University of Bradford Open Access repository. Visit the repository for full metadata or to contact the repository team © University of Bradford. This work is licenced for reuse under a Creative Commons Licence. Exploring Molecular Mechanisms Controlling Skin Homeostasis and Hair Growth MicroRNAs in Hair-cycle-Dependent Gene Regulation, Hair Growth and Associated Tissue Remodelling Mohammed Ikram AHMED BSc, MSc Submitted for the degree of Doctor of Philosophy Centre for Skin Sciences Division of Biomedical Sciences School of life Sciences University of Bradford 2010 Dedicated To my daughter Misba Ahmed and my Family II Abud-Darda (May Allah be pleased with him) reported; The messenger of Allah (PBUH) said, “He who follows a path in quest of knowledge, Allah will make the path of Jannah (heaven) easy to him. The angels lower their wings over the seeker of knowledge, being pleased with what he does. -
The Effects of Organic and Harsh Cleaners on Anolis Carolinensis
THE EFFECTS OF ORGANIC AND HARSH CLEANERS ON ANOLIS Formatted: Font:Italic CAROLINENSIS INTEGUMENT Formatted: Font:Italic A Report of a Senior Study by Kristen Rolston Major: Biology Maryville College Spring, 2017 Date approved , by Faculty Supervisor Date approved , by Division Chair ABSTRACT Household bleach has been used in the home for cleaning hard surfaces since the 18th century and has caused a number of injuries over time. This study further investigates how detrimental this caustic substance can be to the epidermis of Anolis carolinensis in Formatted: Font:Italic comparison to organically branded products claiming to be safer. Bleach cause significantly Deleted: It was determined that there was a significant effect reduced cell width (p=0.001) and number (p=0.009) on stratum corneum , whereas the Deleted: cell width (p=2.59x10-14) and number (p=0.009) organic cleaner showed no difference. This study illustrates that Anolis carolinensis are an Deleted: between the bleach and control groups appropriate model organism to examine the effects of certain substances on the Deleted: By understanding integumentary system and how the skin recovers could lead to valuable insight in the fields of dermatology and stem cell research. PAGE NUMBERS ARE INCORRECT THROUGHOUT 2 ACKNOWLEDGEMENTS ADD ACKNOWLEDGEMENTS HERE Deleted: [This section is not required. If included, it has a 2” top margin.] 3 TABLE OF CONTENTS Page List of Tables vi List of Figures vii Chapter I Introduction 1 Chapter II Title of Chapter 2 Chapter III Title of Chapter 3 Chapter IV Title of Chapter 4 Appendix (or Appendices, as appropriate) 5 Works Cited 7 FIX THIS Deleted: [This section has a 2” top margin.] 4 LIST OF TABLES Table Page 1. -
Characterization of a Novel Human Type II Epithelial Keratin K1b, Specifically Expressed in Eccrine Sweat Glands
Characterization of a Novel Human Type II Epithelial Keratin K1b, Specifically Expressed in Eccrine Sweat Glands Lutz Langbein,Ã Michael A. Rogers,w Silke Praetzel,Ã Bernard Cribier,z Bernard Peltre,z Nikolaus Gassler,y and Ju¨ rgen Schweizerw ÃDivision of Cell Biology and wSection of Normal and Neoplastic Epidermal Differentiation, German Cancer Research Center, Heidelberg, Germany; zDepartment of Dermatology, University of Strasbourg, Strasbourg, France; yInstitute of Pathology, University of Heidelberg, Heidelberg, Germany In this study, we show that a novel human type II epithelial keratin, K1b, is exclusively expressed in luminal duct cells of eccrine sweat glands. Taking this luminal K1b expression as a reference, we have used antibodies against a plethora of epithelial keratins to systematically investigate their expression in the secretory globule and the two- layered sweat duct, which was divided into the intraglandular, intradermal, and intraepidermal (acrosyringium) segments, the latter being further subdivided into the sweat duct ridge and upper intraepidermal duct. We show that (i) each of the eccrine sweat gland tissue compartments expresses their own keratin patterns, (ii) the peripheral and luminal duct layers exhibit a sequential keratin expression, with both representing self-renewing cell layers, (iii) the intradermal duct and the sweat duct ridge display hitherto unknown length variations, and (iv) out of all cell layers, the luminal cell layer is the most robust layer and expresses the highest number of keratins, these being concentrated at the apical side of the cells to form the cuticle. We provide evidence that the cellular and inter- cellular properties of the peripheral and the luminal layers reflect adaptations to different functions. -
TABLE 5. Proteins Identified in Cumulus and Oocyte. GI Number
TABLE 5. Proteins identified in Cumulus and Oocyte. GI Cell Protein DDF Protein name Peptides number typea categoryb fraction 30523262 100 kDa coactivator C K 5 2 2852383 14-3-3 protein beta C K 2 4 2852385 14-3-3 protein gamma C K 14 4 298639 155 kda myosin light chain kinase homolog O K 1 1 576 17,000 dalton myosin light chain CO K 5 3 8118661 17-beta-hydroxysteroid dehydrogenase type 1 C K 2 3 17864970 17-beta-hydroxysteroid dehydrogenase type 1 CO K 38 3 59857747 1-acylglycerol-3-phosphate O-acyltransferase 4 O K 1 3 30017445 2',5'-oligoadenylate synthetase 1, 40/46kDa C K 2 4,3 66792906 2'-5' oligoadenylate synthetase 2 C K 1 1 7271506 2-amino-3-ketobutyrate coenzyme A ligase O K 2 1 31414871 2-enoyl thioester reductase C K 2 4,1 45219953 5-hydroxytryptamine receptor 2A C K 2 4,1 47564115 5-oxo-L-prolinase CO K 5 1 34392345 90-kDa heat shock protein beta CO K 54 1 56967054 A Chain A, Crystal Structure Of Bosus Mitochondrial Elongation Factor TuT O K 2 3 27807141 A disintegrin-like and metalloprotease (reprolysin type) with thrombos O K 1 3 89579 A23707 aminomethyltransferase (EC 2.1.2.10) precursor C K 3 3 89381 A29600 alkaline phosphatase (EC 3.1.3.1) precursor, hepatic - bovine O K 1 1 108687 A36623 gap junction protein Cx43 C K 3 4 89346 A40981 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17), cGMP-stimulated C K 1 4 1363022 A56351 cleavage and polyadenylation specificity factor 100K chain C K 1 3 1363051 A56534 interferon-induced double-stranded RNA-activated protein kinase inhibitor C K 1 4 14194421 AAKG1_BOVIN 5'-AMP-activated protein kinase, gamma-1 subunit C K 1 4 62751897 Abhydrolase domain containing 2 CO K 2 1 61554426 Abl-philin 2 isoform 2 CO K 2 3 63092048 Acetyl-CoA carboxylase, type beta C K 1 3 6006405 Acetyl-CoA-carboxylase C K 3 1 163596 Acid phosphatase C K 1 4 1649041 Acidic ribosomal phosphoprotein C K 2 1 2293577 Acidic ribosomal phosphoprotein PO C K 6 1 600177 Acidic ribosomal protein P2 C K 9 4 1351857 ACON_BOVIN Aconitate hydratase, mitochondrial precursor CO K 27 1 58013001 Actin [Cryptosporidium sp. -
Genetic Variation and Functional Analysis of the Cardiomedin Gene
TECHNISCHE UNIVERSITÄT MÜNCHEN LEHRSTUHL FÜR EXPERIMENTELLE GENETIK Genetic Variation and Functional Analysis of the Cardiomedin Gene Zasie Susanne Schäfer Vollständiger Abdruck der von der Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften genehmigten Dissertation. Vorsitzende: Univ.-Prof. A. Schnieke, Ph.D. Prüfer der Dissertation: 1. apl. Prof. Dr. J. Adamski 2. Univ.-Prof. Dr. Dr. H.-R. Fries 3. Univ.-Prof. Dr. Th. Meitinger Die Dissertation wurde am. 31.05.2011 bei der Technischen Universität München eingereicht und durch die Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt am 02.04.2012 angenommen. Table of Contents Table of contents Abbreviations ........................................................................................................................ 7 1. Summary ..........................................................................................................................10 Zusammenfassung ...............................................................................................................11 2. Introduction ......................................................................................................................12 2.1 Genome-wide association studies (GWAS) and post-GWAS functional genomics ......12 2.2 Genetic influences on cardiac repolarization and sudden cardiac death syndrome in GWAS and the chromosome -
In Vitro Assembly Properties of Human Type I and II Hair Keratins
CELL STRUCTURE AND FUNCTION 39: 31–43 (2014) © 2014 by Japan Society for Cell Biology In vitro Assembly Properties of Human Type I and II Hair Keratins Yuko Honda1, Kenzo Koike2, Yuki Kubo3, Sadahiko Masuko1, Yuki Arakawa4, and Shoji Ando4* 1Department of Anatomy and Physiology, Faculty of Medicine, Saga University, Nabeshima 5-1-1, Saga 849-8501, Japan, 2Beauty Research Center, KAO Corporation, Bunka 2-1-3, Sumida-ku, Tokyo 131-8501, Japan, 3Department of Biomolecular Sciences, Faculty of Medicine, Saga University, Nabeshima 5-1-1, Saga 849-8501, Japan, 4Faculty of Biotechnology and Life Science, Sojo University, Ikeda 4-22-1, Nishi-ku, Kumamoto 860-0082, Japan ABSTRACT. Multiple type I and II hair keratins are expressed in hair-forming cells but the role of each protein in hair fiber formation remains obscure. In this study, recombinant proteins of human type I hair keratins (K35, K36 and K38) and type II hair keratins (K81 and K85) were prepared using bacterial expression systems. The heterotypic subunit interactions between the type I and II hair keratins were characterized using two- dimensional gel electrophoresis and surface plasmon resonance (SPR). Gel electrophoresis showed that the heterotypic complex-forming urea concentrations differ depending on the combination of keratins. K35-K85 and K36-K81 formed relatively stable heterotypic complexes. SPR revealed that soluble K35 bound to immobilized K85 with a higher affinity than to immobilized K81. The in vitro intermediate filament (IF) assembly of the hair keratins was explored by negative-staining electron microscopy. While K35-K81, K36-K81 and K35-K36-K81 formed IFs, K35-K85 afforded tight bundles of short IFs and large paracrystalline assemblies, and K36-K85 formed IF tangles. -
KRT81 Gene Keratin 81
KRT81 gene keratin 81 Normal Function The KRT81 gene provides instructions for making the type II hair keratin K81 protein ( K81). This protein belongs to a group of proteins known as keratins, which are tough, fibrous proteins that form the structural framework of cells that make up the hair, skin, and nails. Each keratin protein partners with another keratin protein to form molecules called intermediate filaments. These filaments assemble into strong networks that provide strength and resiliency to the tissues and protect them from being damaged by everyday physical stresses. The K81 protein is found in cells that make up the inner compartment of the hair shaft known as the cortex, and this protein helps give hair its strength and elasticity. Health Conditions Related to Genetic Changes Monilethrix At least two mutations in the KRT81 gene have been identified in people with monilethrix, a hair condition characterized by strands of hair with a beaded appearance and short, brittle hair that breaks easily. Mutations associated with this condition change a single protein building block (amino acid) in the K81 protein. The amino acid changes usually occur in a region of the K81 protein thought to be important in intermediate filament formation. In people with monilethrix, the cortex of the affected hair shaft appears abnormal. However, it is unclear how mutations in the KRT81 gene are related to the abnormality in the cortex or the beaded appearance of the hair. Other Names for This Gene • ghHb1 • hair keratin K2.9 • hard keratin, type II,