Last edited by Munris
Thursday, July 9, 2020 | History

10 edition of Glycoproteins and disease found in the catalog.

Glycoproteins and disease

  • 268 Want to read
  • 22 Currently reading

Published by Elsevier in Amsterdam, New York .
Written in English

    Subjects:
  • Glycoproteins -- Metabolism -- Disorders,
  • Glycoproteins,
  • Disease -- etiology

  • Edition Notes

    Includes bibliographical references and index.

    Statementeditors, J. Montreuil, J.F.G. Vliegenthart, H. Schachter.
    SeriesNew comprehensive biochemistry ;, v. 30
    ContributionsMontreuil, Jean, 1920-, Vliegenthart, J. F. G., Schachter, H.
    Classifications
    LC ClassificationsQD415 .N48 vol. 30, RC632.G57 .N48 vol. 30
    The Physical Object
    Paginationxxvi, 486 p. :
    Number of Pages486
    ID Numbers
    Open LibraryOL994682M
    ISBN 100444823964, 0444803033
    LC Control Number96033252

    carbohydrate-deficiency; glycoproteins; A group of metabolic disorders characterised by a defect in the modification of glycoproteins by carbohydrates was first recognised in the early s.1 Four types of carbohydrate-deficient glycoprotein syndrome have been recognised, depending on the isoelectric focusing pattern of serum sialotransferrins.2The basic defect in type Ia is . Study Rationale:In Parkinson's disease (PD), the sticky protein alpha-synuclein clumps in the brain, causing cell death. Such toxic alpha-synuclein clumps can spread from cell to cell and multiply. It is not clear how cells take up toxic alpha-synuclein. We found that glycoproteins -- proteins with added chemical carbohydrate -- located on the outside of the cell may play a .

      Glycoproteins are also involved in many other diseases, including influenza, AIDS, rheumatoid arthritis, cystic fibrosis and peptic ulcer. Developments in the new field of glycomics are likely to provide much new information on the roles of sugars in health and disease and also indicate targets for drug and other types of therapies.   Alzheimer disease (AD), Parkinson disease (PD), and frontotemporal dementia (FTD) are associated with the accumulation of neurotoxic material in the brain. Potentially toxic material is normally restricted from the brain by P-glycoprotein, a transporter protein expressed by endothelial cells at the blood-brain barrier.

    Glycoproteins are often used in proteins that are at least in part located in extracellular space (that is, outside the cell). Glycoproteins are important for immune cell recognition, especially in mammals. Examples of glycoproteins in the immune system are: molecules such as antibodies (immunoglobulins) which interact directly with antigens. The plasma membrane is made up primarily of a bilayer of phospholipids with embedded proteins, carbohydrates, glycolipids, and glycoproteins, and, in animal cells, cholesterol. The amount of cholesterol in animal plasma membranes regulates the fluidity of the membrane and changes based on the temperature of the cell’s environment.


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Glycoproteins and disease Download PDF EPUB FB2

Purchase Glycoproteins and Disease, Volume 30 - 1st Edition. Print Book & E-Book. ISBNBook Edition: 1. Glycoproteins and Disease (Volume 30) (New Comprehensive Biochemistry (Volume 30)): Medicine & Health Science Books @ Disease specific glycosylation may contribute to the disease process by altering cellular functions, or may be exploited therapeutically.

Specific therapy may be aimed at correcting glycosylation abnormalities based on knowledge of the mechanisms leading to the disease phenotype and the three-dimensional interactions between carbohydrates and.

Role of Glycoproteins of the Immune and Blood Coagulation Systems.- Growth and Hormone-Related Functions of Glycoproteins and Cell Surface Receptors.- General Glycoprotein Functions.- Glycosylation in Leukemia and Blood Related Disorders.- Glycosylation in Cystic Fibrosis.- Inflammatory Diseases.- Carbohydrate.

Get this from a library. Glycoproteins and disease. [Jean Montreuil; J F G Vliegenthart; H Schachter;] -- The elucidation during the latter half of the 20th century of the mechanisms by which information flows from nucleic acids to proteins has completely changed the face of biological research.

Many. Glycoproteins play a part in important cellular functions like embryonic development, cell–cell recognition, cell adhesion, immune Glycoproteins and disease book, and pathogen identification. Many studies show that glycoproteins have a close association with serious human diseases like cancer, rheumatoid arthritis, and immunodeficiency diseases.

About this book Diverse alterations of glycosylation occur in diseases such as cancer, metastasis, leukemia, inflammatory and other diseases. The glycosylation abnormalities found in disease are the result of complex rearrangements of the oligosaccharide assembly by glycosyltransferases. The pathogenesis of many autoimmune diseases, such as immunoglobulin A (IgA) nephropathy, systemic lupus erythematosus and inflammatory bowel disease, involves abnormal glycosylation of one or more glycoproteins; diabetes involves abnormal O-linked N-acetylglucosamine-mediated signalling and enhanced glycation of multiple proteins.

Glycoprotein and Related Storage Diseases are very rare, progressive, largely untreatable metabolic enzymatic defects inherited by children from both parents. The worldwide incidence for these diseases as a group has not yet been determined accurately, though they can certainly be classified as ultra-rare.

The course of these disorders affects multiple systems of the body and. • A great many of the properties of the glycoproteins are due to the oligosachharide component.

SUMMARY (contd.) • Glycoproteins in Disease: – Pathophysiology of: • HEMPAS • LAD II • PNH • I-Cell Disease • CDGs – Role in adhesion of micro-organisms – Role in Chemotaxis and migration of leukocytes – Cancer Many glycoproteins are found on the surfaces of cells of the immune system and their functions may be greatly influenced by glycosylation.

1 For example, terminal sialic acid on lymphocytes helps to maintain normal homing patterns to tissues and organs; this function is altered following treatment of cells with neuraminidase.

2 Neuraminidase. Gregory Fischer MD, Linda Shore-Lesserson MD, in Anesthesia and Uncommon Diseases (Fifth Edition), Antithrombotic Drug Therapy.

The glycoprotein IIbIIIa (GPIIbIIIa) receptor is responsible for mediating platelet-platelet aggregation via fibrinogen bridging. Drugs that inhibit this receptor in a reversible or an irreversible fashion are potent inhibitors of platelet.

Glycans are components of many biotherapeutic agents, ranging from natural products to molecules based on rational design to recombinant glycoproteins. The glycan components of these agents can be important determinants of their biological activity and therapeutic efficacy.

This chapter provides a brief overview of some of the issues pertinent to glycan functions in. After an incubation period in humans lasting one to two weeks, the trypanosomes are found in significant numbers in the circulating blood.

Next the lymph nodes and spleen are invaded, becoming swollen, soft, and tender. The marked enlargement of the lymph nodes at the back of the neck (known as Winterbottom’s sign) is a common sign of the disease. G1 and G2 glycoproteins form heterodimers and are then transported from the endoplasmic reticulum to the Golgi complex, where glycosylation is completed.

The L protein produces nascent genomes by replication via a positive-sense RNA intermediate. The Centers for Disease Control and Prevention (CDC) cannot attest to the accuracy of a non. Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains.

The carbohydrate is attached to the protein in a cotranslational or posttranslational process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the. Protein glycosylation is an important posttranslational modification that confers both structural and functional properties to the molecules [].There are several types of glycosylation with various carbohydrate structures, and biosynthesis of each sugar chain, in general, is an elaborate process of addition and processing of carbohydrates in the.

O-linked carbohydrates may also bond to hydroxylysine or hydroxyproline. The process is termed O-glycosylation. O-linked glycoproteins are bound to sugar within the Golgi complex.

N-linked glycoproteins have a carbohydrate bonded to the nitrogen (N) of the amino group (-NH 2) of the R group of the amino acid asparagine. The R group is usually. Ebola virus glycoprotein (GP) is the only protein that is expressed on the surface of the virus. The GP proteins play critical roles in the entry of virus into cell and in the evasion of the immune system.

The GP gene transcript to membrane GP is constituted of two subunits GP1 and GP2, and the secretory GP (sGP). The main function of GP1/2 is to attach virus to target cell’s. Surface glycoproteins regulate nearly every extracellular event and they are dynamic for cells to adapt to the ever-changing extracellular environment.

These glycoproteins contain a wealth of information on cellular development and disease states, and have significant biomedical implications.

Systematic inve. The N-linked glycoproteins have a sugar attached to a nitrogen atom, and O-linked glycoproteins have a sugar attached to an oxygen atom. The different structure of N- and O-linked sugars give them.HGE82QOW3T ~ Platelet Membrane Glycoproteins > Kindle Platelet Membrane Glycoproteins By - Springer, United States, Paperback.

Book Condition: New. Softcover Reprint of the Origi ed. x mm. Language: English. Brand New Book ***** Print on Demand *****.It was just about ten years ago that platelet membrane glycoproteins were.The herpes simplex virus type 1 (HSV-1) glycoprotein N (gN/UL) is a type I transmembrane protein conserved throughout the herpesvirus family.

gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN are covalently linked by a single disulphide bond formed between cysteine 46 of gN and cysteine .