Mathematics Course: Algebra 2

Total Page:16

File Type:pdf, Size:1020Kb

Mathematics Course: Algebra 2 Mathematics Course: Algebra 2 Overview: In addition to reviewing previous math topics, students will study rational exponents, polynomial and rational expressions, rational equations, complex numbers, functions and function notation, linear systems of equations, quadratic equations and functions. If time permits, students will get an introduction to non‐linear systems of equations and conic sections. Real Numbers and Algebraic Expressions Alg1.2 Algebraic Expressions and Sets of Numbers Alg1.2a Identify and evaluate algebraic expressions Alg1.2b Identify natural numbers, whole numbers, integers, and rational and irrational real numbers Alg1.2c Find the absolute value of a number Alg1.2d Find the opposite of a number Alg1.2e Write phrases as algebraic expressions Alg1.3 Operations on Real Numbers Alg1.3a Add and subtract real numbers Alg1.3b Multiply and divide real numbers Alg1.3c Evaluate expressions containing exponents Alg1.3d Find roots of numbers Alg1.3e Use the order of operations Alg1.3f Evaluate algebraic expressions Alg1.4 Properties of Real Numbers Alg1.4a Use operations and order symbols to write mathematical sentences Alg1.4b Identify identity numbers and inverses Alg1.4c Identify and use the commutative, associative, and distributive properties Alg1.4d Write and simplify algebraic expressions Equations, Inequalities, and Problem Solving Alg2.1 Linear Equations in One Variable Alg2.1a Solve linear equations using properties of equality Alg2.1b Solve linear equations that can be simplified by combining like terms Alg2.1c Solve linear equations containing fractions or decimals Alg2.1d Recognize identities and equations with no solutions Alg2.2 An Introduction to Problem Solving Alg2.2a Write algebraic expressions that can be simplified Alg2.2b Apply the steps for problem solving Alg2.3 Formulas and Problem Solving Alg2.3a Solve a formula for a specified variable Alg2.3b Use formulas to solve problems Alg2.4 Linear Inequalities and Problem Solving Alg2.4a Use interval notation Alg2.4b Solve linear inequalities using the addition property of inequality Alg2.4c Solve linear inequalities using the multiplication and the addition properties of inequality Alg2.4d Solve problems that can be modeled by linear inequalities Alg2.5 Compound Inequalities Alg2.5a Find the intersection of two sets Alg2.5b Solve compound inequalities containing and Alg2.5c Find the union of two sets Alg2.5d Solve compound inequalities containing or Alg2.6 Absolute Value Equations Alg2.6a Solve absolute value equations Alg2.7 Absolute Value Inequalities Alg2.7a Solve absolute value inequalities Graphs and Functions Alg3.1 Graphing Equations Alg3.1a Plot ordered pairs Alg3.1b Determine whether an ordered pair of numbers is a solution to an equation in two variables Alg3.1c Graph linear equations Alg3.1d Graph nonlinear equations Alg3.2 Introduction to Functions Alg3.2a Define relation, domain, and range Alg3.3b Identify functions Alg3.3c Use the vertical line test for functions Alg3.3d Find the domain and range of a function Alg3.3e Use function notation Alg3.3 Graphing Linear Functions Alg3.3a Graph linear functions Alg3.3b Graph linear functions by finding intercepts Alg3.3c Graph vertical and horizontal lines Alg3.4 The Slope of a Line Alg3.4a Find the slope of a line given two points on the line Alg3.4b Find the slope of a line given the equation of a line Alg3.4c Interpret the slope‐intercept form in an application Alg3.4d Find the slopes of horizontal and vertical lines Alg3.4e Compare the slopes of parallel and perpendicular lines Alg3.5 Equations of Lines Alg3.5a Use the slope‐intercept form to write the equation of a line Alg3.5b Graph a line using its slope and y‐intercept Alg3.5c Use the point‐slope form to write the equation of a line Alg3.5d Write equations of vertical and horizontal lines Alg3.5e Find equations of parallel and perpendicular lines Alg3.7 Graphing Linear Inequalities Alg3.7a Graph linear inequalities Alg3.7b Graph the intersection or union of two linear inequalities Systems of Equations Alg4.1 Solving Systems of Linear Equations in Two Variables Alg4.1a Determine whether an ordered pair is a solution of a system of two linear equations Alg4.1b Solve a system by graphing Alg4.1c Solve a system by substitution Alg4.1d Solve a system by elimination Alg4.2 Solving Systems of Linear Equations in Three Variables Alg4.2a Solve a system of three linear equations in three variables Alg4.3 Systems of Linear Equations and Problem Solving Alg4.3a Solve problems that can be modeled by a system of two linear equations Alg4.3b Solve problems with cost and revenue functions Alg4.3c Solve problems that can be modeled by a system of three linear equations Alg4.5 Systems of Linear Inequalities Alg4.5a Graph a system of linear inequalities Exponents, Polynomials, and Polynomial Functions Alg5.1 Exponents and Scientific Notation Alg5.1a Use the product rule for exponents Alg5.1b Evaluate expressions raised to the 0 power Alg5.1c Use the quotient rule for exponents Alg5.1d Evaluate expressions raised to the negative nth power Alg5.1e Convert between scientific notation and standard notation Alg5.2 More Work with Exponents and Scientific Notation Alg5.2a Use the power rules for exponents Alg5.2b Use exponent rules and definitions to simplify exponential expressions Alg5.2c Compute, using scientific notation Alg5.3 Polynomials and Polynomial Functions Alg5.3a Identify term, constant, polynomial, monomial, binomial, trinomial, and the degree of a term of a polynomial Alg5.3b Define polynomial functions Alg5.3c Review combining like terms Alg5.3d Add polynomials Alg5.3e Subtract polynomials Alg5.3f Recognize the graph of a polynomial function from the degree of the polynomial Alg5.4 Multiplying Polynomials Alg5.4a Multiplying two polynomials Alg5.4b Multiplying Binomials Alg5.4c Square Binomials Alg5.4d Multiply the sum and difference Alg5.4e Multiply three or more polynomials Alg5.4f Evaluate polynomial functions Alg5.5 The Greatest Common Factor and Factoring by Grouping Alg5.5a Identify the GCF Alg5.5b Factor out the GCF of a polynomial’s term Alg5.5c Factor polynomials by grouping Alg5.6 Factoring Trinomials Alg5.6a Factor trinomials with a lead coefficient of 1 Alg5.6b Factor trinomials with a lead coefficient not equal to 1 Alg5.6c Factor by substitution Alg5.7 Factoring by Special Products Alg5.7a Factor a Perfect Square trinomial Alg5.7b Factor the difference of two squares Alg5.7c Factor the sum or difference of two cubes Alg5.8 Solving Equations Alg5.8a Solve polynomial equations by factoring Alg5.8b Solve problems that can be modeled by polynomial equations Alg5.8c Find the x‐intercepts of a polynomial function Rational Expressions Alg6.1 Rational Functions and Multiplying and Dividing Rational Expressions Alg6.1a Find the domain of a rational expression Alg6.1b Simplify rational expressions Alg6.1c Multiply rational expressions Alg6.1d Divide rational expressions Alg6.1e Use rational functions in applications Alg6.2 Adding and Subtracting Polynomials Alg6.2a Define polynomial, monomial, binomial, trinomial and degree Alg6.2b Find the value of a polynomial given replacement values for the variables Alg6.2c Simplify a polynomial by combining like terms Alg6.2d Add and subtract polynomials Alg6.3 Multiplying Polynomials Alg6.3a Use the distributive property to multiply polynomials Alg6.3b Multiply polynomials vertically Alg6.4 Dividing Polynomials Alg6.4a Divide a polynomial by a monomial Alg6.4b Use long division to divide a polynomial by another polynomial Alg6.5 Special Products Alg6.5a Multiply two binomials using the FOIL method Alg6.5b Square a binomial Alg6.5c Multiply the sum and difference of two terms Factoring Polynomials Alg7.1 Greatest Common Factor and Factoring by Group Alg7.1a Find the greatest common factor of a list of integers Alg7.1b Find the greatest common factor of a list of terms Alg7.1c Factor out the greatest common factor from a polynomial Alg7.1d Factor a polynomial by grouping Alg7.2 Factoring Trinomials of the Form x^2 + bx + c Alg7.2a Factor trinomials of the form x^2 + bx + c Alg7.2b Factor out the greatest common factor and then factor a trinomial of the form x^2 + bx + c Alg7.3 Factoring Trinomials of the Form ax^2 + bx + c and Perfect Square Trinomials Alg7.3a Factor trinomials of the form ax^2 + bx + c, where a ≠ 1 Alg7.3b Factor out a GCF before factoring a trinomial of the form ax^2 + bx + c Alg7.3c Factor perfect square trinomials Alg7.4 Factoring Trinomials of the Form ax^2 + bx + c by Grouping Alg7.4a Use the grouping method to factor trinomials of the form ax^2 + bx + c Alg7.5 Factoring Binomials Alg7.5a Factor the difference of two squares Alg7.5b Factor the sum or difference of two cubes Alg7.6 Solving Quadratic Equations by Factoring Alg7.6a Solve quadratic equations by factoring Alg7.6b Solve equations with degree greater than 2 by factoring Alg7.6c Find the x‐intercepts of the graph of a quadratic equation in two variables Alg7.7 Quadratic Equations and Problem Solving Alg7.7a Solve Problems that can be Modeled by Quadratic Equations Rational Expressions Alg8.1 Simplify Rational Expressions Alg8.1a Find the value of a rational expression given a replacement number. Alg8.1b Identify values for which a rational expression is undefined Alg8.1c Simplify or write rational expressions in lowest terms. Alg8.1d Write equivalent rational expressions of the form ‐ = = Alg8.2 Multiply and Divide Rational Expressions Alg8.2a Multiply Rational Expressions Alg8.2b Divide Rational Expressions
Recommended publications
  • The Diversity of Dolichol-Linked Precursors to Asn-Linked Glycans Likely Results from Secondary Loss of Sets of Glycosyltransferases
    The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases John Samuelson*†, Sulagna Banerjee*, Paula Magnelli*, Jike Cui*, Daniel J. Kelleher‡, Reid Gilmore‡, and Phillips W. Robbins* *Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, 715 Albany Street, Boston, MA 02118-2932; and ‡Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01665-0103 Contributed by Phillips W. Robbins, December 17, 2004 The vast majority of eukaryotes (fungi, plants, animals, slime mold, to N-glycans of improperly folded proteins, which are retained in and euglena) synthesize Asn-linked glycans (Alg) by means of a the ER by conserved glucose-binding lectins (calnexin͞calreticulin) lipid-linked precursor dolichol-PP-GlcNAc2Man9Glc3. Knowledge of (13). Although the Alg glycosyltransferases in the lumen of ER this pathway is important because defects in the glycosyltrans- appear to be eukaryote-specific, archaea and Campylobacter sp. ferases (Alg1–Alg12 and others not yet identified), which make glycosylate the sequon Asn and͞or contain glycosyltransferases dolichol-PP-glycans, lead to numerous congenital disorders of with domains like those of Alg1, Alg2, Alg7, and STT3 (1, 14–16). glycosylation. Here we used bioinformatic and experimental Protists, unicellular eukaryotes, suggest three notable exceptions methods to characterize Alg glycosyltransferases and dolichol- to the N-linked glycosylation path described in yeast and animals PP-glycans of diverse protists, including many human patho- (17). First, the kinetoplastid Trypanosoma cruzi (cause of Chagas gens, with the following major conclusions. First, it is demon- myocarditis), fails to glucosylate the dolichol-PP-linked precursor strated that common ancestry is a useful method of predicting and so makes dolichol-PP-GlcNAc2Man9 (18).
    [Show full text]
  • Physical Interactions Between the Alg1, Alg2, and Alg11 Mannosyltransferases of the Endoplasmic Reticulum
    Glycobiology vol. 14 no. 6 pp. 559±570, 2004 DOI: 10.1093/glycob/cwh072 Advance Access publication on March 24, 2004 Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum Xiao-Dong Gao2, Akiko Nishikawa1, and Neta Dean1 begins on the cytosolic face of the ER, where seven sugars (two N-acetylglucoseamines and five mannoses) are added 1Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, sequentially to dolichyl phosphate on the outer leaflet of NY 11794-5215, and 2Research Center for Glycoscience, National the ER, using nucleotide sugar donors (Abeijon and Institute of Advanced Industrial Science and Technology, Tsukuba Hirschberg, 1992; Perez and Hirschberg, 1986; Snider and Downloaded from https://academic.oup.com/glycob/article/14/6/559/638968 by guest on 30 September 2021 Central 6, 1-1 Higashi, Tsukuba 305-8566, Japan Rogers, 1984). After a ``flipping'' or translocation step, the Received on January 26, 2004; revised on March 2, 2004; accepted on last seven sugars (four mannoses and three glucoses) are March 2, 2004 added within the lumen of the ER, using dolichol-linked sugar donors (Burda and Aebi, 1999). Once assembled, the The early steps of N-linked glycosylation involve the synthesis oligosaccharide is transferred from the lipid to nascent of a lipid-linked oligosaccharide, Glc3Man9GlcNAc2-PP- protein in a reaction catalyzed by oligosaccharyltransferase. dolichol, on the endoplasmic reticulum (ER) membrane. After removal of terminal glucoses and a single mannose, Prior to its lumenal translocation and transfer to nascent nascent glycoproteins bearing the N-linked Man8GlcNAc2 glycoproteins, mannosylation of Man5GlcNAc2-PP-dolichol core can exit the ER to the Golgi, where this core may is catalyzed by the Alg1, Alg2, and Alg11 mannosyltrans- undergo further carbohydrate modifications.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Yeast Genome Gazetteer P35-65
    gazetteer Metabolism 35 tRNA modification mitochondrial transport amino-acid metabolism other tRNA-transcription activities vesicular transport (Golgi network, etc.) nitrogen and sulphur metabolism mRNA synthesis peroxisomal transport nucleotide metabolism mRNA processing (splicing) vacuolar transport phosphate metabolism mRNA processing (5’-end, 3’-end processing extracellular transport carbohydrate metabolism and mRNA degradation) cellular import lipid, fatty-acid and sterol metabolism other mRNA-transcription activities other intracellular-transport activities biosynthesis of vitamins, cofactors and RNA transport prosthetic groups other transcription activities Cellular organization and biogenesis 54 ionic homeostasis organization and biogenesis of cell wall and Protein synthesis 48 plasma membrane Energy 40 ribosomal proteins organization and biogenesis of glycolysis translation (initiation,elongation and cytoskeleton gluconeogenesis termination) organization and biogenesis of endoplasmic pentose-phosphate pathway translational control reticulum and Golgi tricarboxylic-acid pathway tRNA synthetases organization and biogenesis of chromosome respiration other protein-synthesis activities structure fermentation mitochondrial organization and biogenesis metabolism of energy reserves (glycogen Protein destination 49 peroxisomal organization and biogenesis and trehalose) protein folding and stabilization endosomal organization and biogenesis other energy-generation activities protein targeting, sorting and translocation vacuolar and lysosomal
    [Show full text]
  • Congenital Disorders of Glycosylation from a Neurological Perspective
    brain sciences Review Congenital Disorders of Glycosylation from a Neurological Perspective Justyna Paprocka 1,* , Aleksandra Jezela-Stanek 2 , Anna Tylki-Szyma´nska 3 and Stephanie Grunewald 4 1 Department of Pediatric Neurology, Faculty of Medical Science in Katowice, Medical University of Silesia, 40-752 Katowice, Poland 2 Department of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, Poland; [email protected] 3 Department of Pediatrics, Nutrition and Metabolic Diseases, The Children’s Memorial Health Institute, W 04-730 Warsaw, Poland; [email protected] 4 NIHR Biomedical Research Center (BRC), Metabolic Unit, Great Ormond Street Hospital and Institute of Child Health, University College London, London SE1 9RT, UK; [email protected] * Correspondence: [email protected]; Tel.: +48-606-415-888 Abstract: Most plasma proteins, cell membrane proteins and other proteins are glycoproteins with sugar chains attached to the polypeptide-glycans. Glycosylation is the main element of the post- translational transformation of most human proteins. Since glycosylation processes are necessary for many different biological processes, patients present a diverse spectrum of phenotypes and severity of symptoms. The most frequently observed neurological symptoms in congenital disorders of glycosylation (CDG) are: epilepsy, intellectual disability, myopathies, neuropathies and stroke-like episodes. Epilepsy is seen in many CDG subtypes and particularly present in the case of mutations
    [Show full text]
  • We Consider the Ordinary Differential Equation Model of the Metal Rolling
    We consider the ordinary differential equation model of the metal rolling process defined in K. Gal- kowski, E. Rogers, W. Paszke and D. H. Owens, Linear repetitive process control theory applied to a physical example, Int. J. Appl. Comput. Sci., 13 (2003), 87-99. In order to do that, we firstly define the Ore algebra formed by the derivative D w.r.t. time t and by the shift operator S acting on the discrete variable k which denotes the pass number. > Alg1 := DefineOreAlgebra(diff=[D,t], dual_shift=[S,k], polynom=[t,k], > comm=[lambda,lambda1,lambda2,M]): The system matrix is defined by: > R1 := evalm([[D^2+lambda/M-(lambda/lambda1)*D^2*S-(lambda/M)*S, > lambda/(M*lambda2)]]); λ λ D2 S λ S λ R1 := D2 + − − M λ1 M M λ2 Then, the system is defined by the following equation > ApplyMatrix(R1, [y(t,k), FM(t,k)], Alg1)[1,1]=0; (λ y(t, k) λ1 λ2 − λ y(t, k − 1) λ1 λ2 + D1, 1(y)(t, k) M λ1 λ2 − λ D1, 1(y)(t, k − 1) M λ2 + λ FM(t, k) λ1)/(M λ1 λ2) = 0 which corresponds to (4) of the previously quoted paper. Let us check the structural properties of the previous system (e.g., controllability, parametrizability, flatness). > R1_adj := Involution(R1, Alg1): It is known that the Alg1 -module associated with the matrix R1 is torsion-free iff the first extension module of the Alg1 -module associated with R1 adj with values in Alg1 is 0. We compute this extension module by using Exti: > Ext1 := Exti(R1_adj, Alg1, 1); Ext1 := [ 1 , M λ D2 S λ2 − M D2 λ1 λ2 + λ S λ1 λ2 − λ λ1 λ2 −λ λ1 , −λ λ1 ] M D2 λ1 λ2 − M λ D2 S λ2 + λ λ1 λ2 − λ S λ1 λ2 As the first matrix Ext1 [1] is an identity matrix, we obtain that the Alg1 -module associated with R1 is torsion-free, and thus, the corresponding system is controllable and parametrizable.
    [Show full text]
  • Molecular Diagnostic Requisition
    BAYLOR MIRACA GENETICS LABORATORIES SHIP TO: Baylor Miraca Genetics Laboratories 2450 Holcombe, Grand Blvd. -Receiving Dock PHONE: 800-411-GENE | FAX: 713-798-2787 | www.bmgl.com Houston, TX 77021-2024 Phone: 713-798-6555 MOLECULAR DIAGNOSTIC REQUISITION PATIENT INFORMATION SAMPLE INFORMATION NAME: DATE OF COLLECTION: / / LAST NAME FIRST NAME MI MM DD YY HOSPITAL#: ACCESSION#: DATE OF BIRTH: / / GENDER (Please select one): FEMALE MALE MM DD YY SAMPLE TYPE (Please select one): ETHNIC BACKGROUND (Select all that apply): UNKNOWN BLOOD AFRICAN AMERICAN CORD BLOOD ASIAN SKELETAL MUSCLE ASHKENAZIC JEWISH MUSCLE EUROPEAN CAUCASIAN -OR- DNA (Specify Source): HISPANIC NATIVE AMERICAN INDIAN PLACE PATIENT STICKER HERE OTHER JEWISH OTHER (Specify): OTHER (Please specify): REPORTING INFORMATION ADDITIONAL PROFESSIONAL REPORT RECIPIENTS PHYSICIAN: NAME: INSTITUTION: PHONE: FAX: PHONE: FAX: NAME: EMAIL (INTERNATIONAL CLIENT REQUIREMENT): PHONE: FAX: INDICATION FOR STUDY SYMPTOMATIC (Summarize below.): *FAMILIAL MUTATION/VARIANT ANALYSIS: COMPLETE ALL FIELDS BELOW AND ATTACH THE PROBAND'S REPORT. GENE NAME: ASYMPTOMATIC/POSITIVE FAMILY HISTORY: (ATTACH FAMILY HISTORY) MUTATION/UNCLASSIFIED VARIANT: RELATIONSHIP TO PROBAND: THIS INDIVIDUAL IS CURRENTLY: SYMPTOMATIC ASYMPTOMATIC *If family mutation is known, complete the FAMILIAL MUTATION/ VARIANT ANALYSIS section. NAME OF PROBAND: ASYMPTOMATIC/POPULATION SCREENING RELATIONSHIP TO PROBAND: OTHER (Specify clinical findings below): BMGL LAB#: A COPY OF ORIGINAL RESULTS ATTACHED IF PROBAND TESTING WAS PERFORMED AT ANOTHER LAB, CALL TO DISCUSS PRIOR TO SENDING SAMPLE. A POSITIVE CONTROL MAY BE REQUIRED IN SOME CASES. REQUIRED: NEW YORK STATE PHYSICIAN SIGNATURE OF CONSENT I certify that the patient specified above and/or their legal guardian has been informed of the benefits, risks, and limitations of the laboratory test(s) requested.
    [Show full text]
  • Associated with Low Dehydrodolichol Diphosphate Synthase (DHDDS) Activity S
    Sabry et al. Orphanet Journal of Rare Diseases (2016) 11:84 DOI 10.1186/s13023-016-0468-1 RESEARCH Open Access A case of fatal Type I congenital disorders of glycosylation (CDG I) associated with low dehydrodolichol diphosphate synthase (DHDDS) activity S. Sabry1,2,3,4, S. Vuillaumier-Barrot1,2,5, E. Mintet1,2, M. Fasseu1,2, V. Valayannopoulos6, D. Héron7,8, N. Dorison8, C. Mignot7,8,9, N. Seta5,10, I. Chantret1,2, T. Dupré1,2,5 and S. E. H. Moore1,2* Abstract Background: Type I congenital disorders of glycosylation (CDG-I) are mostly complex multisystemic diseases associated with hypoglycosylated serum glycoproteins. A subgroup harbour mutations in genes necessary for the biosynthesis of the dolichol-linked oligosaccharide (DLO) precursor that is essential for protein N-glycosylation. Here, our objective was to identify the molecular origins of disease in such a CDG-Ix patient presenting with axial hypotonia, peripheral hypertonia, enlarged liver, micropenis, cryptorchidism and sensorineural deafness associated with hypo glycosylated serum glycoproteins. Results: Targeted sequencing of DNA revealed a splice site mutation in intron 5 and a non-sense mutation in exon 4 of the dehydrodolichol diphosphate synthase gene (DHDDS). Skin biopsy fibroblasts derived from the patient revealed ~20 % residual DHDDS mRNA, ~35 % residual DHDDS activity, reduced dolichol-phosphate, truncated DLO and N-glycans, and an increased ratio of [2-3H]mannose labeled glycoprotein to [2-3H]mannose labeled DLO. Predicted truncated DHDDS transcripts did not complement rer2-deficient yeast. SiRNA-mediated down-regulation of DHDDS in human hepatocellular carcinoma HepG2 cells largely mirrored the biochemical phenotype of cells from the patient.
    [Show full text]
  • Viruses Like Sugars: How to Assess Glycan Involvement in Viral Attachment
    microorganisms Review Viruses Like Sugars: How to Assess Glycan Involvement in Viral Attachment Gregory Mathez and Valeria Cagno * Institute of Microbiology, Lausanne University Hospital, University of Lausanne, 1011 Lausanne, Switzerland; [email protected] * Correspondence: [email protected] Abstract: The first step of viral infection requires interaction with the host cell. Before finding the specific receptor that triggers entry, the majority of viruses interact with the glycocalyx. Identifying the carbohydrates that are specifically recognized by different viruses is important both for assessing the cellular tropism and for identifying new antiviral targets. Advances in the tools available for studying glycan–protein interactions have made it possible to identify them more rapidly; however, it is important to recognize the limitations of these methods in order to draw relevant conclusions. Here, we review different techniques: genetic screening, glycan arrays, enzymatic and pharmacological approaches, and surface plasmon resonance. We then detail the glycan interactions of enterovirus D68 and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), highlighting the aspects that need further clarification. Keywords: attachment receptor; viruses; glycan; sialic acid; heparan sulfate; HBGA; SARS-CoV-2; EV-D68 Citation: Mathez, G.; Cagno, V. Viruses Like Sugars: How to Assess 1. Introduction Glycan Involvement in Viral This review focuses on methods for assessing the involvement of carbohydrates in Attachment. Microorganisms 2021, 9, viral attachment and entry into the host cell. Viruses often bind to entry receptors that are 1238. https://doi.org/10.3390/ not abundant on the cell surface; to increase their chances of finding them, they initially microorganisms9061238 bind to attachment receptors comprising carbohydrates that are more widely expressed.
    [Show full text]
  • Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
    BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in
    [Show full text]
  • Prenatal Testing Requisition Form
    BAYLOR MIRACA GENETICS LABORATORIES SHIP TO: Baylor Miraca Genetics Laboratories 2450 Holcombe, Grand Blvd. -Receiving Dock PHONE: 800-411-GENE | FAX: 713-798-2787 | www.bmgl.com Houston, TX 77021-2024 Phone: 713-798-6555 PRENATAL COMPREHENSIVE REQUISITION FORM PATIENT INFORMATION NAME (LAST,FIRST, MI): DATE OF BIRTH (MM/DD/YY): HOSPITAL#: ACCESSION#: REPORTING INFORMATION ADDITIONAL PROFESSIONAL REPORT RECIPIENTS PHYSICIAN: NAME: INSTITUTION: PHONE: FAX: PHONE: FAX: NAME: EMAIL (INTERNATIONAL CLIENT REQUIREMENT): PHONE: FAX: SAMPLE INFORMATION CLINICAL INDICATION FETAL SPECIMEN TYPE Pregnancy at risk for specific genetic disorder DATE OF COLLECTION: (Complete FAMILIAL MUTATION information below) Amniotic Fluid: cc AMA PERFORMING PHYSICIAN: CVS: mg TA TC Abnormal Maternal Screen: Fetal Blood: cc GESTATIONAL AGE (GA) Calculation for AF-AFP* NTD TRI 21 TRI 18 Other: SELECT ONLY ONE: Abnormal NIPT (attach report): POC/Fetal Tissue, Type: TRI 21 TRI 13 TRI 18 Other: Cultured Amniocytes U/S DATE (MM/DD/YY): Abnormal U/S (SPECIFY): Cultured CVS GA ON U/S DATE: WKS DAYS PARENTAL BLOODS - REQUIRED FOR CMA -OR- Maternal Blood Date of Collection: Multiple Pregnancy Losses LMP DATE (MM/DD/YY): Parental Concern Paternal Blood Date of Collection: Other Indication (DETAIL AND ATTACH REPORT): *Important: U/S dating will be used if no selection is made. Name: Note: Results will differ depending on method checked. Last Name First Name U/S dating increases overall screening performance. Date of Birth: KNOWN FAMILIAL MUTATION/DISORDER SPECIFIC PRENATAL TESTING Notice: Prior to ordering testing for any of the disorders listed, you must call the lab and discuss the clinical history and sample requirements with a genetic counselor.
    [Show full text]
  • Myo-Glyco Disease Biology: Genetic Myopathies Caused by Abnormal Glycan Synthesis and Degradation
    Journal of Neuromuscular Diseases 6 (2019) 175–187 175 DOI 10.3233/JND-180369 IOS Press Review Myo-Glyco disease Biology: Genetic Myopathies Caused by Abnormal Glycan Synthesis and Degradation Motoi Kanagawa∗ Division of Molecular Brain Science, Kobe University Graduate School of Medicine, Japan Abstract. Glycosylation is a major form of post-translational modification and plays various important roles in organisms by modifying proteins or lipids, which generates functional variability and can increase their stability. Because of the physiological importance of glycosylation, defects in genes encoding proteins involved in glycosylation or glycan degradation are sometimes associated with human diseases. A number of genetic neuromuscular diseases are caused by abnormal glycan modification or degeneration. Heterogeneous and complex modification machinery, and difficulties in structural and functional analysis of glycans have impeded the understanding of how glycosylation contributes to pathology. However, recent rapid advances in glycan and genetic analyses, as well as accumulating genetic and clinical information have greatly contributed to identifying glycan structures and modification enzymes, which has led to breakthroughs in the understanding of the molecular pathogenesis of various diseases and the possible development of therapeutic strategies. For example, studies on the relationship between glycosylation and muscular dystrophy in the last two decades have significantly impacted the fields of glycobiology and neuromyology. In this review, the basis of glycan structure and biosynthesis will be briefly explained, and then molecular pathogenesis and therapeutic concepts related to neuromuscular diseases will be introduced from the point of view of the life cycle of a glycan molecule. Keywords: Glycosylation, muscular dystrophy, neuromuscular disease, therapeutic strategy STRUCTURE AND CELL BIOLOGY OF of a glycoconjugate, such as a glycoprotein and GLYCANS – AN OVERVIEW glycolipid.
    [Show full text]