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Human Identification by Amelogenin Test in Libyans
American Journal of www.biomedgrid.com Biomedical Science & Research ISSN: 2642-1747 --------------------------------------------------------------------------------------------------------------------------------- Research Article Copyright@ Samir Elmrghni Human Identification by Amelogenin Test in Libyans Samir Elmrghni* and Mahmoud Kaddura Department of Forensic Medicine and Toxicology, University of Benghazi, Libya *Corresponding author: Samir Elmrghni, Faculty of Medicine, Department of Forensic Medicine and Toxicology, University of Benghazi-Libya, Benghazi, Libya. To Cite This Article: Samir Elmrghni. Human Identification by Amelogenin Test in Libyans. Am J Biomed Sci & Res. 2019 - 3(6). AJBSR. MS.ID.000737. DOI: 10.34297/AJBSR.2019.03.000737 Received: May 25, 2019 | Published: July 11, 2019 Abstract Sex typing is essential in medical diagnosis of sex-linked disease and forensic science. Gender for criminal evidence of offender is usually as reported the anomalous amelogenin results of 2 male samples (out of 238 males) represented as females (Y deletions) and another 2 samples the initial information for investigation. For individualization, identification of gender is performed in addition to the STR markers recently. We amelogenin results of the controversial samples, DNA was further used in SRY and Y-STR typing. All samples typed as males but two showed with with (X deletions) in Benghazi (Libya). The frequency in both was about 0.8%. Higher than those of the other populations reported. To confirm X chromosomes. From the results, it was highly suggested that for the controversial cases of human gender identification with amelogenin tests, amplificationKeywords: Amelogenin; of SRY gene Libyans or/and Y-STR markers will be adopted to confirm the gender [1]. Introduction gene (AMG) was precisely mapped in the p22 region on the X systems used to determine if the sample being tested is of male gene was first isolated and sequenced [2]. -
Mutational Analysis of Candidate Genes in 24 Amelogenesis
Eur J Oral Sci 2006; 114 (Suppl. 1): 3–12 Copyright Ó Eur J Oral Sci 2006 Printed in Singapore. All rights reserved European Journal of Oral Sciences Jung-Wook Kim1,2, James P. Mutational analysis of candidate genes Simmer1, Brent P.-L. Lin3, Figen Seymen4, John D. Bartlett5, Jan C.-C. in 24 amelogenesis imperfecta families Hu1 1University of Michigan School of Dentistry, University of Michigan Dental Research 2 Kim J-W, Simmer JP, Lin BP-L, Seymen F, Bartlett JD, Hu JC-C. Mutational analysis Laboratory, Ann Arbor, MI, USA; Seoul National University, College of Dentistry, of candidate genes in 24 amelogenesis imperfecta families. Eur J Oral Sci 2006; 114 Department of Pediatric Dentistry & Dental (Suppl. 1): 3–12 Ó Eur J Oral Sci, 2006 Research Institute, Seoul, Korea; 3UCSF School of Dentistry, Department of Growth and Amelogenesis imperfecta (AI) is a heterogeneous group of inherited defects in dental Development, San Francisco, CA, USA; 4 enamel formation. The malformed enamel can be unusually thin, soft, rough and University of Istanbul, Faculty of Dentistry, stained. The strict definition of AI includes only those cases where enamel defects Department of Pedodontics, apa, Istanbul, Turkey; 5The Forsyth Institute, Harvard-Forsyth occur in the absence of other symptoms. Currently, there are seven candidate genes for Department of Oral Biology, Boston, MA, USA AI: amelogenin, enamelin, ameloblastin, tuftelin, distal-less homeobox 3, enamelysin, and kallikrein 4. To identify sequence variations in AI candidate genes in patients with isolated enamel defects, and to deduce the likely effect of each sequence variation on Jan C.-C. -
Tooth Enamel and Its Dynamic Protein Matrix
International Journal of Molecular Sciences Review Tooth Enamel and Its Dynamic Protein Matrix Ana Gil-Bona 1,2,* and Felicitas B. Bidlack 1,2,* 1 The Forsyth Institute, Cambridge, MA 02142, USA 2 Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA 02115, USA * Correspondence: [email protected] (A.G.-B.); [email protected] (F.B.B.) Received: 26 May 2020; Accepted: 20 June 2020; Published: 23 June 2020 Abstract: Tooth enamel is the outer covering of tooth crowns, the hardest material in the mammalian body, yet fracture resistant. The extremely high content of 95 wt% calcium phosphate in healthy adult teeth is achieved through mineralization of a proteinaceous matrix that changes in abundance and composition. Enamel-specific proteins and proteases are known to be critical for proper enamel formation. Recent proteomics analyses revealed many other proteins with their roles in enamel formation yet to be unraveled. Although the exact protein composition of healthy tooth enamel is still unknown, it is apparent that compromised enamel deviates in amount and composition of its organic material. Why these differences affect both the mineralization process before tooth eruption and the properties of erupted teeth will become apparent as proteomics protocols are adjusted to the variability between species, tooth size, sample size and ephemeral organic content of forming teeth. This review summarizes the current knowledge and published proteomics data of healthy and diseased tooth enamel, including advancements in forensic applications and disease models in animals. A summary and discussion of the status quo highlights how recent proteomics findings advance our understating of the complexity and temporal changes of extracellular matrix composition during tooth enamel formation. -
Amelogenesis Imperfecta - Literature Review
IOSR Journal of Dental and Medical Sciences (IOSR-JDMS) e-ISSN: 2279-0853, p-ISSN: 2279-0861. Volume 13, Issue 1 Ver. IX. (Feb. 2014), PP 48-51 www.iosrjournals.org Amelogenesis Imperfecta - Literature Review GemimaaHemagaran1 ,Arvind. M2 1B.D.S.,Saveetha Dental College, Chennai, India 2B.D.S., M.D.S., Dip Oral medicine, Prof. of Oral Medicine, Saveetha Dental College, Chennai, India. Abstract: Amelogenesis Imperfecta (AI) is a group of inherited disorder of dental enamel formation in the absence of systemic manifestations. AI is also known as Hereditary enamel dysplasia, Hereditary brown enamel, Hereditary brown opalescent teeth. Since the mesodermal components of the teeth is normal, this defect is entirely ectodermal in origin. Variants of AI generally are classified as hypoplastic, hypocalcified, or hypomineralised types based on the primary enamel defect. The affected teeth may be discoloured, sensitive or prone to disintegration, leading to loss of occlusal vertical dimensions and very poor aesthetics. They exists in isolation or associated with other abnormalities in syndromes. It may show autosomal dominant, autosomal recessive, sex-linked and sporadic inheritance patterns. Mutations in the amelogenin, enamelin, and kallikrein-4 genes have been demonstrated to different types of AI. Keywords: AmelogenesisImperfecta, Hypoplastic, Hypocalcific, Hypomineralised. I. Introduction: Amelogenesis imperfecta (AI) is a term for a clinically and genetically heterogeneous group of conditions that affect the dental enamel, occasionally in conjunction with other dental, oral and extraoral tissues.[1] Dental enamel formation is divided into secretory, transition, and maturation stages. During the secretory stage, enamel crystals grow primarily in length. During the maturation stage, mineral is deposited exclusively on the sides of the crystallites, which grow in width and thickness to coalesce with adjacent crystals.[2]The main structural proteins in forming enamel are amelogenin, ameloblastin, and enamelin. -
Amelogenin Gene Influence on Enamel Defects of Cleft Lip and Palate Patients
ORIGINAL RESEARCH Genetic and Molecular Biology Amelogenin gene influence on enamel defects of cleft lip and palate patients Abstract: The aim of this study was to investigate the occurrence of mutations in the amelogenin gene (AMELX) in patients with cleft lip Fernanda Veronese OLIVEIRA(a) Thiago José DIONÍSIO(b) and palate (CLP) and enamel defects (ED). A total of 165 patients were Lucimara Teixeira NEVES(b) divided into four groups: with CLP and ED (n=46), with CLP and with- Maria Aparecida Andrade out ED (n = 34), without CLP and with ED (n = 34), and without CLP Moreira MACHADO(a) Carlos Ferreira SANTOS(b) or ED (n = 51). Genomic DNA was extracted from saliva followed by Thais Marchini OLIVEIRA(a) conducting a Polymerase Chain Reaction and direct DNA sequencing of exons 2 through 7 of AMELX. Mutations were found in 30% (n = 14), (a) Department of Pediatric Dentistry, 35% (n = 12), 11% (n = 4) and 13% (n = 7) of the subjects from groups 1, 2, Orthodontics and Community Health, Bauru 3 and 4, respectively. Thirty seven mutations were detected and distrib- School of Dentistry, University of São Paulo, Bauru, SP, Brazil. uted throughout exons 2 (1 mutation – 2.7%), 6 (30 mutations – 81.08%) and 7 (6 mutations – 16.22%) of AMELX. No mutations were found in (b) Department of Biological Sciences, Bauru School of Dentistry, University of São Paulo, exons 3, 4 or 5. Of the 30 mutations found in exon 6, 43.34% (n = 13), Bauru, SP, Brazil. 23.33% (n = 7), 13.33% (n = 4) and 20% (n = 6) were found in groups 1, 2, 3 and 4, respectively. -
Protein Nanoribbons Template Enamel Mineralization
Protein nanoribbons template enamel mineralization Yushi Baia, Zanlin Yub, Larry Ackermana, Yan Zhangc, Johan Bonded,WuLic, Yifan Chengb, and Stefan Habelitza,1 aDepartment of Preventative and Restorative Dental Sciences, School of Dentistry, University of California, San Francisco, CA 94143; bDepartment of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco, CA 94158; cDepartment of Oral and Craniofacial Sciences, School of Dentistry, University of California, San Francisco, CA 94143; and dDivision of Pure and Applied Biochemistry, Center for Applied Life Sciences, Lund University, Lund, SE-221 00, Sweden Edited by Patricia M. Dove, Virginia Tech, Blacksburg, VA, and approved July 2, 2020 (received for review April 22, 2020) As the hardest tissue formed by vertebrates, enamel represents early tissue-based transmission electron microscopy (TEM) nature’s engineering masterpiece with complex organizations of studies also show the presence of filamentous protein assemblies fibrous apatite crystals at the nanometer scale. Supramolecular (18–20) that share great structural similarity with the recombi- assemblies of enamel matrix proteins (EMPs) play a key role as nant amelogenin nanoribbons (7, 12). Even though previous the structural scaffolds for regulating mineral morphology during XRD and TEM characterizations suggest that nanoribbons may enamel development. However, to achieve maximum tissue hard- represent the structural nature of the in vivo observed filamen- ness, most organic content in enamel is digested and removed at tous proteins, they do not provide sufficient resolution to make the maturation stage, and thus knowledge of a structural protein detailed comparison. In addition, the filamentous proteins in the template that could guide enamel mineralization is limited at this DEM match the size and alignment of apatite crystal ribbons date. -
United States Patent (19) 11 Patent Number: 5,876,942 Cheng Et Al
USOO5876942A United States Patent (19) 11 Patent Number: 5,876,942 Cheng et al. (45) Date of Patent: Mar. 2, 1999 54 PROCESS FOR SEXING COW EMBRYOS Gibson et al., Biochemistry 30:1075–1079 (1991). 75 Inventors: Winston Teng-Kuei Cheng, Taipei; Shimokawa et al., J. of Biological Chemistry 262(9) : Chuan-Mu Chen, Tai Chung; Che-Lin 4042–4047 (1987). Hu, Taipei; Chih-Hua Wang, Taipei; Schafer et al., BioEssays 18(12):955-962 (1996). Kong-Bung Choo, Taipei, all of Taiwan Sullivan et al., BioTechniques 15(4):636-641 (1993). 73 Assignee: National Science Council of Republic Ennis et al., Animal Genetics 25:425-427 (1994). of China, Taipei, Taiwan Primary Examiner W. Gary Jones 21 Appl. No.: 899,811 ASSistant Examiner Ethan Whisenant Attorney, Agent, or Firm-Bacon & Thomas 22 Filed: Jul. 24, 1997 57 ABSTRACT 51) Int. Cl. ............................. C12Q 1/68; CO7H 21/02; CO7H 21/04 A rapid, highly reproducible and Sensitive technique has 52 U.S. Cl. ............................... 435/6; 536/231; 536/24.3 been Successfully developed for Sexing the cow embryos, by 58 Field of Search ................................ 435/6; 536/23.1, method of polymerase chain reaction (PCR) against the 536/24.3;985/77, 78 amelogenin (bAML) genes located on both X- and Y-chromosomes of the Holstein dairy cattle. Results from 56) References Cited DNA sequence analysis showed that there was only 45% homology between the intron 5 of AMLX and AMLY genes. U.S. PATENT DOCUMENTS Based on these Sequences a pair of Sex-Specific primers, 5,578,449 11/1996 Frasch et al. -
Implications of Male Amelogenin Dropouts in Forensics
Research Article J Forensic Sci & Criminal Inves Volume 15 Issue 2 - February 2021 Copyright © All rights are reserved by Anand Kumar DOI: 10.19080/JFSCI.2021.15.555908 Implications of Male Amelogenin Dropouts in Forensics Anand Kumar* DNA Division, State Forensic Science Laboratory, India Submission: February 06, 2021; Published: February 22, 2021 *Corresponding author: Anand Kumar, DNA Division, State Forensic Science Laboratory, Rajasthan, 302016, (INDIA) Abstract In forensic science STR loci are useful tools for reconstructing male lineages, paternity testing, forensic investigations, and population The samples used in this study were received at State Forensic Science Laboratory for routine examination. A combination of autosomal (Power Plexgenomics.®- Fusion They 5C cover system a widekit) and range Y-STR of genome-specific(Power Plex®- Y23 geographical system kit) distributions multiplexing duesystems to shortfall was used of forrecombination the genotyping during of the spermatogenesis. samples as per the manufacturer’s protocol. In electropherogram of male samples, male-derived amelogenin marker was not observed in the results of Power Plex®- Fusion 5C system kit. These samples were further analyzed by Power Plex®- Y23 system kit and a complete set of 23 Y STR markers was obtained. The failure rate of detection of amelogenin marker in Indian population is 0.23%. This clearly indicates the deletion in the short arm of Y chromosome related to amelogenin marker. Keywords: Amelogenin marker; Forensic genetics; Haplogroups; Deletion Introduction DNA analysis based on autosomal as well as sex chromosome STR is routinely used in forensic casework, population studies, identification [6], Thangaraj et al [7], reported 1.85% failure in Southern hybridization [5]. -
The Pitx2:Mir-200C/141:Noggin Pathway Regulates Bmp Signaling
3348 RESEARCH ARTICLE STEM CELLS AND REGENERATION Development 140, 3348-3359 (2013) doi:10.1242/dev.089193 © 2013. Published by The Company of Biologists Ltd The Pitx2:miR-200c/141:noggin pathway regulates Bmp signaling and ameloblast differentiation Huojun Cao1,*, Andrew Jheon2,*, Xiao Li1, Zhao Sun1, Jianbo Wang1, Sergio Florez1, Zichao Zhang1, Michael T. McManus3, Ophir D. Klein2,4 and Brad A. Amendt1,5,‡ SUMMARY The mouse incisor is a remarkable tooth that grows throughout the animal’s lifetime. This continuous renewal is fueled by adult epithelial stem cells that give rise to ameloblasts, which generate enamel, and little is known about the function of microRNAs in this process. Here, we describe the role of a novel Pitx2:miR-200c/141:noggin regulatory pathway in dental epithelial cell differentiation. miR-200c repressed noggin, an antagonist of Bmp signaling. Pitx2 expression caused an upregulation of miR-200c and chromatin immunoprecipitation assays revealed endogenous Pitx2 binding to the miR-200c/141 promoter. A positive-feedback loop was discovered between miR-200c and Bmp signaling. miR-200c/141 induced expression of E-cadherin and the dental epithelial cell differentiation marker amelogenin. In addition, miR-203 expression was activated by endogenous Pitx2 and targeted the Bmp antagonist Bmper to further regulate Bmp signaling. miR-200c/141 knockout mice showed defects in enamel formation, with decreased E-cadherin and amelogenin expression and increased noggin expression. Our in vivo and in vitro studies reveal a multistep transcriptional program involving the Pitx2:miR-200c/141:noggin regulatory pathway that is important in epithelial cell differentiation and tooth development. -
Amelogenin X Linked Chromosome
International Journal of Research in Medical Sciences Gupta B. Int J Res Med Sci. 2017 Oct;5(10):4214-4222 www.msjonline.org pISSN 2320-6071 | eISSN 2320-6012 DOI: http://dx.doi.org/10.18203/2320-6012.ijrms20174549 Review Article Amelogenin x linked chromosome Bhawani Gupta* Department of Oral Pathology, Saveetha University, Chennai, Tamil Nadu, India Received: 29 June 2017 Revised: 20 August 2017 Accepted: 21 August 2017 *Correspondence: Dr. Bhawani Gupta, E-mail: [email protected] Copyright: © the author(s), publisher and licensee Medip Academy. This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. ABSTRACT The AMELX gene provides instructions for making a protein called amelogenin, which is essential for normal tooth development. Amelogenin is involved in the formation of enamel, which is the hard, white material that forms the protective outer layer of each tooth. Using molecular genetic techniques, we have shown that there is no evidence that the AMGX gene is deleted in this case of the Nance-Horan syndrome. In affected members of a Michigan kindred of Eastern European ancestry segregating X-linked amelogenesis imperfecta with a characteristic snow-capped enamel phenotype. Keywords: Amelogenin, Chromosome, Hormone INTRODUCTION degradation by Proteolytic enzymes like matrix mettaloproteinases into smaller low molecular weight The AMELX gene provides instructions for making a fragments, like tyrosine rich amelogenin protein and protein called amelogenin, which is essential for normal leucine rich amelogenin polypeptide which are suggested tooth development. -
Polymerase Chain Reaction (PCR)-Based Sex Determination Using Unembalmed Human Cadaveric Skeletal Fragments from Sokoto, Northwestern Nigeria
IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS) e-ISSN: 2278-3008, p-ISSN:2319-7676. Volume 7, Issue 2 (Jul. – Aug. 2013), PP 01-08 www.iosrjournals.org Polymerase Chain Reaction (PCR)-Based Sex Determination Using Unembalmed Human Cadaveric Skeletal Fragments From Sokoto, Northwestern Nigeria. A A B C *Zagga Ad, Tadros Aa, Ismail Sm, And Ahmed H, Oon. A Department of Anatomy, College of Health Sciences, Usmanu Danfodiyo University, Sokoto, Sokoto State, Nigeria. B Department of Medical Molecular Genetics, Division of Human Genetics and Genome Research, National Research Centre, Cairo, Egypt. CDepartment of Paediatrics, College of Health Sciences, Usmanu Danfodiyo University, Sokoto, Sokoto State, Nigeria. Abstract: The strategy developed for sex determination in skeletal remains is to amplify the highly degraded DNA, by use of primers that span short DNA fragments. To determine sex of unembalmed human cadaveric skeletal fragments from Sokoto, North-western Nigeria, using Polymerase Chain Reaction (PCR). A single blind study of Polymerase Chain Reaction (PCR)-based sex determination using amelogenin gene and alphoid repeats primers on unembalmed human cadaveric skeletal fragments from Sokoto, North-western Nigeria, was undertaken. With amelogenin gene, genetic sex identification was achieved in four samples only. PCR Sensitivity = 40%, Specificity = 100%, Predictive value of positive test = 100%, Predictive value of negative test = 25%, False positive rate = 0%, False negative rate = 150%, Efficiency of test = 50%. Fisher’s exact probability test P = 1. Z-test: z-value = -1.0955, p>0.05; not statistically significant. With alphoid repeats primers, correct genetic sex identification was achieved in all the samples. PCR Sensitivity = 100%, Specificity = 0%, Predictive value of positive test = 100%, Predictive value of negative test = 0%, False positive rate = 0%, False negative rate = 0%, Efficiency of test = 100%. -
Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance S
Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance S. Delgado, D. Deutsch, J. Y. Sire To cite this version: S. Delgado, D. Deutsch, J. Y. Sire. Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance. Journal of Molecular Evolution, Springer Verlag, 2017, pp.1-11. 10.1007/s00239-017-9789-5. hal-01516886 HAL Id: hal-01516886 https://hal.sorbonne-universite.fr/hal-01516886 Submitted on 2 May 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Manuscript R4 Click here to download Manuscript Manuscript R4.docx Click here to view linked References 1 Evolutionary analysis of the mammalian tuftelin sequence reveals features of functional 1 2 importance 3 4 5 6 7 1* 2 1 8 S. Delgado , D. Deutsch and J.Y. Sire 9 10 11 1 12 Evolution et Développement du Squelette, UMR7138- Evolution Paris-Seine, Institut de 13 14 Biologie (IBPS), Université Pierre et Marie Curie, Paris, France. 15 16 17 2 Dental Research Laboratory, Faculty of Dental Medicine, Institute of Dental Sciences, The 18 19 Hebrew University of Jerusalem-Hadassah, Jerusalem, Israel. 20 21 22 23 * corresponding author: [email protected] 24 25 26 27 28 Running title: Evolutionary analysis of TUFT1 29 30 31 32 33 Keywords 34 35 36 Tuftelin, TUFT1, MYZAP, Evolution, Mineralization, Mammals 37 38 39 40 41 42 Acknowledgements 43 44 This collaborative study was initiated at the Tooth Morphogenesis and Differentiation 45 46 47 conference in Lalonde-les-Maures (France) in Spring 2013.