English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/160491
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Members of the galectin network with deviations from the canonical sequence signature. 2. Galectin-related protein (GRP)

AuthorsManning, Joachim C.; García Caballero, Gabriel; Ruiz, Federico M. ; Romero, Antonio ; Kaltner, Herbert; Gabius, Hans-Joachim
KeywordsB cells
Bursa
Lectin
Lymphocytes
Phylogenesis
Issue Date31-Jan-2018
PublisherForum Carbohydrates Coming of Age
CitationTrends in Glycoscience and Glycotechnology 30(172)SE11–SE20 (2018)
AbstractGalectin-related protein (GRP) is present in vertebrates. Sequence comparisons between GRPs from diverse species reveal an unusually high degree of similarity indicative of a strong positive selection. In solution, human and chicken GRPs are monomers irrespective of the presence of the 36-amino-acid-long extension of the core structure at the N-terminus. They are devoid of ability to bind lactose due to severe deviations from the respective sequence signature. Crystallography disclosed distortion of the binding-site architecture that precludes accommodation of lactose. The recent characterization of expression of chicken GRP (C-GRP) enables complete galectin network analysis in this organism. When tested in a panel of developing and adult organs, C-GRP presence was detected in bursa of Fabricius. Its epithelium and vessels as well as bursal B cells are positive in immunohistochemistry. In the B lymphocytes, C-GRP was predominantly cytoplasmic, whereas the chicken tandem-repeat-type galectin, the second member of the galectin family expressed in these cells, was detected at the surface. Binding of labeled C-GRP to cells and sections was blocked by heparin. These data illustrate disparities in expression and ligand profiles within the galectin family and hereby stimulate interest to perform respective mapping for mammalian GRPs as step to define its physiological function(s).
Description19 p.-6 fig.-1 tab.
Publisher version (URL)https://doi.org/10.4052/tigg.1727.1SE
URIhttp://hdl.handle.net/10261/160491
DOI10.4052/tigg.1727.1SE
ISSN0915-7352
E-ISSN1883-2113
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
Trends Glycoscience Glycotech_Manning J.C._2018.docx Embargoed until January 31, 2021Postprint8,26 MBMicrosoft Word XMLView/Open    Request a copy
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.