Legume Lectin Structure
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Binding Partners for the Myelin-Associated Glycoprotein of N2A Neuroblastoma Cells
View metadata,FEBS 21505 citation and similar papers at core.ac.uk FEBS Letters 444brought (1999) to you 59^64 by CORE provided by Elsevier - Publisher Connector Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells Karen Strenge, Roland Schauer, SÖrge Kelm* Institute of Biochemistry, University of Kiel, Olshausenstrasse 40, 24098 Kiel, Germany Received 11 November 1998; received in revised form 4 January 1999 indicating that MAG plays a role in long-term maintenance of Abstract The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. the integrity of both myelin and axons [12,13]. For a better understanding of the interactions involved in the An interesting aspect of MAG is its in£uence on neuronal binding of MAG to neuronal axons, we performed this study to growth. In vitro, MAG promotes neurite outgrowth of em- identify the binding partners for MAG on neuronal cells. bryonal dorsal root ganglion neurones [14^16], whereas it in- Experiments with glycosylation inhibitors revealed that sialy- hibits the neurite outgrowth of cerebellar neurones, adult dor- lated N-glycans of glycoproteins represent the major binding sal root ganglion neurones [15] and neuroblastoma cells [17]. sites for MAG on the neuroblastoma cell line N2A. From The role of MAG as a neurone regeneration inhibiting 3 extracts of [ H]glucosamine-labelled N2A cells several glyco- molecule in vivo has remained controversial [6,7] since ¢rst proteins with molecular weights between 20 and 230 kDa were experiments with MAG3=3 mice gave no clear evidence for a affinity-precipitated using immobilised MAG. -
Concanavalin a (Cona) - Weigh 5 Mg of Concanavalin A
ConcNaFAnT aactivvataor lin A Catalog # inh-cona For research use only Version # 16I15-MM PRODUCT INFORMATION METHODS Content: Preparation of stock solution (2.5 mg/ml) • 100 mg Concanavalin A (ConA) - Weigh 5 mg of concanavalin A. Storage and stability: - Add 2 ml of sterile PBS (pH 7.5; not provided) to 5 mg of - Concanavalin A is shipped at room temperature. Store at -20 °C. concanavalin A. Vortex gently until completely dissolved. - Upon resuspension, prepare aliquots and store at -20 °C. Resuspended Note: The solution may appear hazy. product is stable for 12 months when properly stored. Avoid repeated freeze-thaw cycles. Reporter assay using Jurkat-Lucia ™ NFAT cells: Quality control: The following protocol describes the monitoring of NFAT activation - The biological activity of Concanavalin A has been confirmed by using Jurkat-Lucia ™ NFAT cells, a human T lymphocyte-based Jurkat assessing NFAT activation in Jurkat-Lucia ™ NFAT cells. cell line that has been stably transfected with an NFAT-inducible - The absence of bacterial contamination (e.g. lipoproteins and secreted Lucia luciferase reporter gene. endotoxins) has been confirmed using HEK-Blue ™ TLR2 and HEK -Blue ™ TLR4 cells. 1. Centrifuge cells at 1000-1500 RPM (RCF 200 - 300 g) for 5 minutes. 2. Remove supernatant and resuspend Jurkat-Lucia ™ NFAT cells DESCRIPTION 6 Concanavalin A (Con A), a mannose/glucose-binding lectin isolated at 2 x 10 cells/ml in fresh, pre-warmed growth medium. from Jack beans ( Canavalia ensiformis ), is a well-known T cell 3. Add 20 µl of Concanavalin A (1- 100 μg/ml) per well. mitogen that can activate the immune system, recruit lymphocytes 4. -
Plant Lectins: Targeting Programmed Cell Death Pathways As Antitumor Agents
See discussions, stats, and author profiles for this publication at: http://www.researchgate.net/publication/51529797 Plant lectins: targeting programmed cell death pathways as antitumor agents. Int J Biochem Cell Biol ARTICLE in THE INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY · JULY 2011 Impact Factor: 4.05 · DOI: 10.1016/j.biocel.2011.07.004 · Source: PubMed CITATIONS READS 56 232 6 AUTHORS, INCLUDING: Chengcheng Zhou Shun Yao Sichuan University Shanghai Institutes for Biological Sciences 2 PUBLICATIONS 61 CITATIONS 6 PUBLICATIONS 82 CITATIONS SEE PROFILE SEE PROFILE Available from: Chengcheng Zhou Retrieved on: 26 November 2015 This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues. Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier’s archiving and manuscript policies are encouraged to visit: http://www.elsevier.com/copyright Author's personal copy The International Journal of Biochemistry & Cell Biology 43 (2011) 1442–1449 Contents lists available at ScienceDirect The International Journal of Biochemistry & Cell Biology jo -
Investigation Into the Structures of a Lectin
INVESTIGATION INTO THE STRUCTURES OF A LECTIN FROM TRICHOSANTHES DIOICA AND ONE FROM ERYTHRINA INDICA & BIOPHYSICAL CHARACTERIZATION OF ARACEAE LECTINS FROM SAUROMATUM GUTTATUM AND ARISAEMA TORTUOSUM THESIS SUBMITTED TO THE UNIVERSITY OF PUNE FOR THE DEGREE OF DOCTOR OF PHILOSOPHY IN BIOTECHNOLOGY BY POORVA DHARKAR DIVISION OF BIOCHEMICAL SCIENCES NATIONAL CHEMICAL LABORATORY PUNE 411 008 INDIA April 2009 CERTIFICATE This is to certify that the work incorporated in the thesis entitled “Investigation into the structures of a lectin from Trichosanthes dioica and one from Erythrina indica & Biophysical characterization of araceae lectins from Sauromatum guttatum and Arisaema tortuosum.” submitted by Ms. Poorva Dharkar was carried out under my supervision. The material obtained from other sources has been duly acknowledged in the thesis. Date Dr. C. G. Suresh (Research Supervisor) Scientist Division of Biochemical Sciences National Chemical Laboratory Pune 411 008 DECLARATION I hereby declare that the thesis entitled “Investigation into the structures of a lectin from Trichosanthes dioica and one from Erythrina indica & Biophysical characterization of araceae lectins from Sauromatum guttatum and Arisaema tortuosum.” submitted by me to the University of Pune for the degree of Doctor of Philosophy is the record of original work carried out by me under the supervision of Dr. C. G. Suresh at the Division of Biochemical Sciences, National Chemical Laboratory, Pune 411008 and has not formed the basis for the award of any degree, diploma, associateship, fellowship, titles in this or any other University or Institution. I further declare that the material obtained from other sources has been duly acknowledged in the thesis. Poorva Dharkar Date Division of Biochemical Sciences National Chemical Laboratory Pune 411008 Dedicated to……. -
The Role of Weak Protein-Protein Interactions in Multivalent Lectin-Carbohydrate Binding: Crystal Structure of Cross-Linked FRIL
doi:10.1006/jmbi.2000.3785 available online at http://www.idealibrary.com on J. Mol. Biol. (2000) 299, 875±883 COMMUNICATION The Role of Weak Protein-Protein Interactions in Multivalent Lectin-Carbohydrate Binding: Crystal Structure of Cross-linked FRIL Thomas W. Hamelryck1*, Jeffrey G. Moore2, Maarten J. Chrispeels3, Remy Loris1 and Lode Wyns1 1Laboratorium voor Binding of multivalent glycoconjugates by lectins often leads to the for- Ultrastructuur, Vlaams mation of cross-linked complexes. Type I cross-links, which are Interuniversitair Instituut voor one-dimensional, are formed by a divalent lectin and a divalent glycocon- Biotechnologie, Vrije jugate. Type II cross-links, which are two or three-dimensional, occur Universiteit Brussel when a lectin or glycoconjugate has a valence greater than two. Type II Paardenstraat 65, B-1640, Sint- complexes are a source of additional speci®city, since homogeneous type Genesius-Rode, Belgium II complexes are formed in the presence of mixtures of lectins and glyco- conjugates. This additional speci®city is thought to become important 2Phylogix LLC, P.O. Box 6790 when a lectin interacts with clusters of glycoconjugates, e.g. as is present 69 U.S. Route One on the cell surface. The cryst1al structure of the Glc/Man binding legume Scarborough, ME 04074, USA lectin FRIL in complex with a trisaccharide provides a molecular snap- 3Department of Biology shot of how weak protein-protein interactions, which are not observed in University of California, San solution, can become important when a cross-linked complex is formed. Diego, 9500 Gilman Drive, La In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tet- Jolla, CA 92093-0116, USA ramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. -
Publications Imberty
Publications Dr Anne Imberty CERMAV-CNRS Databases for glycobiology 3D-lectin Database: our Internet database of 3 structures of lectins, and the carbohydrate energy parameters PIM for the TRIPOS force field 2021 346 - Kuhaudomlar S., Siebs E., Shanina E., Topin J., Joachim I., da Silva Figueiredo Celestino Gomes P., Varrot A., Rognan D., Rademacher C., Imberty A.* & Titz A* (in press) Non-carbohydrate glycomimetics as inhibitors of calcium(II)-binding lectins. Angew. Chem. in press, (doi: 10.1002/anie.202013217) [OpenAccess] [hal-03083693] 345 - Gajdos L., Forsyth V.T., Blakeley M.P., Haertlein,M., Imberty A.*, Samain E.*, & Devos J.M.* (2021) Production of perdeuterated fucose from glyco-engineered bacteria. Glycobiology 31, 151-158 (doi: 10.1093/glycob/cwaa059) [OpenAccess] [hal-02911649] 344 - Bonnardel F., Mariethoz J., Pérez S., Imberty A.* & Lisacek F.* (2021) LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification. Nucleic Ac. Res. 49, D1548-D1554 (doi: 10.1093/nar/gkaa1019) [OpenAccess] [hal- 03000205] 2020 343 - Suhaudomlarp S., Cerofolini L., Santarsia S., Gillon E., Denis M., Fallarini S., Giuntini S.,Valori C., Lombardi G., Fragai M*, Imberty A.*, Dondoni A. & Nativi C.* (2020) Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for Burkholderia ambifaria lectin (BambL). Biomolecules 10, 1660 (doi: 10.1039/d0sc03741a) [OpenAccess] [hal-02995036] 342 - Pérez S., Bonnardel F., Lisacek F., Imberty A., Ricard-Blum S. & Makshakova O. (2020) GAG- DB, the new interface of the three-dimensional landscape of glycosaminoglycans. Biomolecules 10, 1660 (doi: 10.3390/biom10121660) [OpenAccess] [hal-03083684] 341 - Zahorska E., Kuhaudomlarp S., Minervini S., Yousaf S., Lepsik M., Kinsinger T., Hirsch A.K.H., Imberty A &. -
Glycosylation Patterns of Kidney Proteins Differ in Rat Diabetic
http://www.kidney-international.org basic research & 2015 International Society of Nephrology Glycosylation patterns of kidney proteins differ in rat diabetic nephropathy Alessandra Ravida`1, Luca Musante1, Marjut Kreivi1, Ilkka Miinalainen1, Barry Byrne1, Mayank Saraswat1, Michael Henry2, Paula Meleady2, Martin Clynes2 and Harry Holthofer1 1Centre for BioAnalytical Sciences, Dublin City University, Dublin, Ireland and 2National Institute for Cellular Biotechnology, Dublin City University, Dublin, Ireland Diabetic nephropathy often progresses to end-stage kidney Diabetes mellitus is one of the leading noncommunicable disease and, ultimately, to renal replacement therapy. chronic diseases, with more than 340 million people affected Hyperglycemia per se is expected to have a direct impact on worldwide.1 The high level of blood glucose caused by either the biosynthesis of N- and O-linked glycoproteins. This study insulin deficiency (type 1 diabetes, ‘juvenile’) or insulin aims to establish the link between protein glycosylation and resistance (type 2 diabetes, ‘adult onset’) may lead, over time, progression of experimental diabetic kidney disease using to an array of complications, especially of the cardiovascular orthogonal methods. Kidneys of streptozotocin-diabetic and system.2 Diabetic kidney damage (diabetic nephropathy, DN) control rats were harvested at three different time points is one of the most burdensome of diabetic complications, post streptozotocin injection. A panel of 12 plant lectins was which, in a substantial segment of patients, leads to end-stage used in the screening of lectin blots. The lectins UEAI, PHA-E, kidney disease with consequent renal replacement, i.e., GSI, PNA, and RCA identified remarkable disease-associated dialysis and kidney transplantation, as the only therapeutic differences in glycoprotein expression. -
Different Patterns of Lectin Binding and Cell Surface Sialylation Detected on Related High- and Low-Metastatic Tumor Lines
(CANCER RESEARCH 43, 5138-5144, November 1983] Different Patterns of Lectin Binding and Cell Surface Sialylation Detected on Related High- and Low-Metastatic Tumor Lines Peter Altevogt,1 Mina Fogel, Rachanee Cheingsong-Popov, Jim Dennis, Peter Robinson, and Volker Schirrmacher2 Institut fur Immunologie und Genetik, Deutsches Krebsforschungszentrum, 6900 Heidelberg, Federal Republic of Germany [P. A., M. F., R. C-P. P. R., V. S.¡,and The Hospital for Sick Children, Toronto, Ontario, Canada [J. D.J ABSTRACT tation of metastatic tumor cells by heterotypic cell interactions; and (c) in the arrest in organs by specific interactions with the We have analyzed cell surface-bound carbohydrates in two target tissue. different model systems for metastasis composed of closely Such important involvements of carbohydrates in metastasis related tumor cell lines with differing metastatic potential. The formation would imply that tumor cells with different metastatic first system studied was that of the DBA/2-derived T-lymphoma potential possess distinct qualitative or quantitative differences lines (Eb/ESb) and some recently established sublines of ESb in their glycosylation of membrane glycoconjugates. A correlation with altered metastatic behavior (ESb-M and ESb-MR). The between the quantity of cell surface-exposed SA3 and metastatic second system consisted of the highly metastatic MDAY-D2 capacity was recently found by Yogeeswaran (36) for a variety cells, a wheat germ agglutinin-resistant low metastatic subline of different tumor cell lines. Of particular importance seemed to MDW40, and two metastatic revertants from the latter. The cells be SA residues in association with subterminal sugar moieties were stained with fluorescein isothiocyanate-conjugated lectins which could be oxidized by galactose oxidase and subsequently and analyzed by flow cytofluorography. -
Alterations in Human Colonic Mucin Occurring with Cellular
Proc. Natt Acad. Sci. USA Vol. 79, pp. 2051-2055, March 1982 Medical Sciences Alterations in human colonic mucin occurring with cellular differentiation and malignant transformation (colon cancer/fluorescein isothiocyanate-conjugated lectins/peanut agglutinin/transitional mucosa) C. RICHARD BOLAND*, CAROLYN K. MONTGOMERYt, AND YOUNG S. KIM* Gastrointestinal Research Unit, Veterans Administration Medical Center, Departments of *Medicine and tPathology, University of California, San Francisco, California 94121 Communicated by Rudi Schmid, December 9, 1981 ABSTRACT The binding of fluorescein isothiocyanate (FITC)- structures accompanies the process ofintestinal goblet cell dif- conjugated lectins to mucin in the human colon was studied by ferentiation. Because differentiation-dependent changes in gly- using fluorescence microscopy. In normal mucosa, lectins that coconjugates have not been investigated in the human colon, preferentially bind to exposed N-acetyl-galactosamine residues we first evaluated FITC-conjugated lectin binding to mucin in (Dolichos biflorus agglutinin and soybean agglutinin) bound se- normal human colonic mucosa. Based on the findings obtained, lectively to the goblet cell mucin ofwell-differentiated cells in the we then examined 21 human colon carcinomas to determine the upper colonic crypt. By contrast, lectins that require exposed non- changes in lectin binding to mucinous glycoproteins that occur reducing galactose residues for binding (Ricinus communis agglu- with malignant transformation. tinin, and Bauhinia purpurea agglutinin) preferentially labeled Mucin is the predominant the mucin of less-differentiated goblet cells located in the lower secreted glycoprotein in the colon portion of the colonic crypt. The lectin derived from Arachis hy- and is elaborated by most colon cancers. The mucin extracted pogaea (peanut agglutinin) has a high affinity for a carbohydrate from colon cancer is immunologically distinct from that in the structure not normally exposed in human tissues. -
Specific Interaction of Peanut Agglutinin with the Glycolipid Asialo Gm 1
Volume 141, number 1 FEBS LETTERS May 1982 SPECIFIC INTERACTION OF PEANUT AGGLUTININ WITH THE GLYCOLIPID ASIALO GM 1 Takashi MOMOI, Tohru TOKUNAGA* and Yoshitaka NAGAI Department of Pathobiochemical Cell Research, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108 and *Department of Tuberculosis, National Institute of Health, Shinagawa-ku, Tokyo 141, Japan Received 11 March 1982 1. Introduction Lectins have the ability to bind with glycolipids as well as with glycoproteins [3,4]. Peanut agglutinin Membrane glycoproteins that are involved in the (PNA) which has a specificity for Gal@1 -3)GalNac antigenicity of cell surface have been used as specific [S] has been used to characterize thymocyte subpop- markers for characterizing various subpopulations of ulations [6]. Although the Gal@l-3)GalNAc struc- lymphocytes [ 11. Their glycoconjugate portions have ture is present in many soluble glycoproteins among different affinities for various lectins. Therefore, lectins membrane glycocompounds, it has been identified in with different sugar specificities are capable of char- a few glycoproteins such as glycophorin, and in gly- acterizing the glycoproteins on celI surface membranes cosphingolipids, GM1 and asialo GM1 . PI. On the other hand, antibody against asialo GM1 , whose oligosaccharide structure is Gal@-3)GalNAc- Abbreviations: PBS, phosphate-buffered saline; buffer A, @l-4)Gal@l-4)Glc, has been used as a probe capable PBS containing 0.1% (w/v) sodium deoxycholate; buffer B, of distinguishing immunologically competent cells of PBS containing 0.05% (w/v) Tween 20; buffer C, buffer B a particular type, such as natural killer cells, fetal thy- containing 2% (w/v) BSA; BSA, bovine serum albumin; PNA, peanut agglutinin; TLMA, rat T lymphocyte macrophage- mocytes and suppressor cells of mice [7-lo]. -
Ricin a Chain from Ricinus Communis (Castor Bean)
Lectin from Ricinus communis Ricin, A Chain, deglycosylated Product Number L 4022 Storage Temperature 2-8 °C Product Description Sigma offers a range of lectins suitable for the above This lectin is a solution in 40% glycerol containing 10 applications. Most Sigma lectins are highly purified by mM phosphate buffer, pH 6.0, 150 mM NaCl, 10 mM affinity chromatography, but some are offered as galactose, and 0.5 mM dithioerythritol purified or partially purified lectins, suitable for specific applications. The Ricin A-chain shows two bands on an SDS-PAGE gel. The major band is at approximately 29 kDa, and a Ricinus communis agglutinin should have good minor doublet is seen at approximately 32 kDa.1 The binding affinity for lactose containing proteins, such as doublet consists of a major band at approximately 32 Lactosyl-BSA (Product No. A 5783).2 kDa and a minor band at approximately 34 kDa. Many of the lectins are available conjugated to Lectins are proteins or glycoproteins of non-immune (conjugation does not alter the specificity of the lectin): origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding 1. fluorochromes (for detection by fluorimetry). glycoproteins even in presence of various detergents.2 2. enzymes (for enzyme-linked assays). The agglutination activity of these highly specific 3. insoluble matrices (for use as affinity media). carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins, di, tri, Please refer to the table for general information on the and even polysaccharides are required. most common lectins. Lectins are isolated from a wide variety of natural This lectin has been deglycosylated using a sources, including seeds, plant roots and bark, fungi, metaperiodate-cyanoborohydride mixture. -
Purification and Characterization of a New Mannose-Specific Lectin from Sternbergia Lutea Bulbs
Glycoconjugate Journal (1997) 14: 889±896 Purification and characterization of a new mannose-specific lectin from Sternbergia lutea bulbs Keiko Saito1, Akira Misaki1 and Irwin J. Goldstein2* 1 Faculty of Human Life Science, Osaka City University, Osaka 558, Japan 2 Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA A new mannose-binding lectin was isolated from Sternbergia lutea bulbs by affinity chromatography on an a(1-2)man- nobiose-Synsorb column and purified further by gel filtration. This lectin (S. lutea agglutinin; SLA) appeared homogeneous by native-gel electrophoresis at pH 4.3, gel filtration chromatography on a Sephadex G-75 column, and SDS-polyacrylamide gel electrophoresis, These data indicate that SLA is a dimeric protein (20 kDa) composed of two identical subunits of 10 kDa which are linked by non-covalent interactions. The carbohydrate binding specificity of the lectin was investigated by quantitative precipitation and hapten inhibition assays. It is an a-D-mannose-specific lectin that interacts to form precipitates with various a-mannans, galactomannan and asialo-thyroglobulin, but not with a-glucans and thyroglobulin. Of the monosaccharides tested only D-mannose was a hapten inhibitor of the SLA-asialothryroglobulin precipitation system, whereas D-glucose, D-galactose and L-arabinose were not. The lectin appears to be highly specific for terminal a(1-3)-mannooligosaccharides. The primary structure of SLA appears to be quite similar to that of the snow drop (Galanthus nivalis) bulb lectin which is a mannose-binding lectin from the same plant family Amaryllidaceae. The N-terminal 46 amino acid sequence SLA showed 76% homology with that of GNA.