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Galectin-8 specificity to cells: from broad outside to fine inside

Nordenfelt, Susanne LU (2007) In Lund University Faculty of Medicine Doctoral Dissertation Series
Abstract
Glycobiology is the world of sugars: how they are made, what they look like, and what they do. Despite the importance of glycan structures in life, knowledge has been hampered due to their inherent complexity. Lectins are nature's way to decipher the intricate code held by glycans, which makes them important players in both normal and pathological physiology. A key to the understanding of lectins and their cellular effects lies in the basis of their carbohydrate specificity and the multivalent interactions occurring at a cell surface. Also in the design and synthesis of new drugs, either to be used as future tools in fruitful glycobiology experiments, or as effective therapeutics in the clinic, such information is very helpful.

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Glycobiology is the world of sugars: how they are made, what they look like, and what they do. Despite the importance of glycan structures in life, knowledge has been hampered due to their inherent complexity. Lectins are nature's way to decipher the intricate code held by glycans, which makes them important players in both normal and pathological physiology. A key to the understanding of lectins and their cellular effects lies in the basis of their carbohydrate specificity and the multivalent interactions occurring at a cell surface. Also in the design and synthesis of new drugs, either to be used as future tools in fruitful glycobiology experiments, or as effective therapeutics in the clinic, such information is very helpful.



This thesis is aimed at investigating the fine specificity of the two carbohydrate recognition domains of a human lectin, galectin-8, and to relate this fine specificity with cell surface binding and induced cellular effects. In short, our experiments charted the individual ligand preference displayed by the two domains, in addition to explaining how the striking monovalent affinity for sialylated ?-galactosides, shown by the N-terminal domain, was achieved. Further, we showed that although cell surface binding of intact galectin-8 didn?t require the sialic acid binding ability of the N-terminal domain, intracellular targeting following endocytosis did. (Less)
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author
supervisor
opponent
  • Docent Holgersson, Jan, Karolinska Institutet, Huddinge, Sweden
organization
publishing date
type
Thesis
publication status
published
subject
keywords
Biomedical sciences, Biomedicinska vetenskaper, Intracellular targeting, Sialic acid, Galectin fine specificity
in
Lund University Faculty of Medicine Doctoral Dissertation Series
pages
132 pages
publisher
Institution of Laboratory Medicine, Section of Microbiology, Immunology and Glycobiology (MIG)
defense location
Rune Grubb lecture hall, Biomedical Center, Sölvegatan 23, Lund
defense date
2007-05-26 09:00:00
ISSN
1652-8220
ISBN
978-91-85559-72-5
language
English
LU publication?
yes
additional info
Santosh Kumar Patnaik, Barry Potvin, Susanne Carlsson, David Sturm, Hakon Leffler and Pamela Stanley. 2006. Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells Glycobiology, vol 16 pp 305-317. Oxford Journals
Susanne Carlsson, Christopher T Öberg, Michael C Carlsson, Anders Sundin, Ulf J Nilsson, David Smith, Richard D Cummings, Jenny Almkvist, Anna Karlsson and Hakon Leffler. 2007. Affinity of galectin-8 and its carbohydrate recognition domains for ligands in solution and at the cell surface Glycobiology, Oxford Journals (inpress)
Susanne Carlsson, Michael C Carlsson and Hakon Leffler. 2007. Intracellular sorting of galectin-8 based on fine specificity Glycobiology, Oxford Journals (submitted)
id
9c03345b-5e60-4901-8ce0-2f6f82cb9158 (old id 548629)
date added to LUP
2016-04-01 16:44:13
date last changed
2019-05-21 21:54:56
@phdthesis{9c03345b-5e60-4901-8ce0-2f6f82cb9158,
  abstract     = {{Glycobiology is the world of sugars: how they are made, what they look like, and what they do. Despite the importance of glycan structures in life, knowledge has been hampered due to their inherent complexity. Lectins are nature's way to decipher the intricate code held by glycans, which makes them important players in both normal and pathological physiology. A key to the understanding of lectins and their cellular effects lies in the basis of their carbohydrate specificity and the multivalent interactions occurring at a cell surface. Also in the design and synthesis of new drugs, either to be used as future tools in fruitful glycobiology experiments, or as effective therapeutics in the clinic, such information is very helpful.<br/><br>
<br/><br>
This thesis is aimed at investigating the fine specificity of the two carbohydrate recognition domains of a human lectin, galectin-8, and to relate this fine specificity with cell surface binding and induced cellular effects. In short, our experiments charted the individual ligand preference displayed by the two domains, in addition to explaining how the striking monovalent affinity for sialylated ?-galactosides, shown by the N-terminal domain, was achieved. Further, we showed that although cell surface binding of intact galectin-8 didn?t require the sialic acid binding ability of the N-terminal domain, intracellular targeting following endocytosis did.}},
  author       = {{Nordenfelt, Susanne}},
  isbn         = {{978-91-85559-72-5}},
  issn         = {{1652-8220}},
  keywords     = {{Biomedical sciences; Biomedicinska vetenskaper; Intracellular targeting; Sialic acid; Galectin fine specificity}},
  language     = {{eng}},
  publisher    = {{Institution of Laboratory Medicine, Section of Microbiology, Immunology and Glycobiology (MIG)}},
  school       = {{Lund University}},
  series       = {{Lund University Faculty of Medicine Doctoral Dissertation Series}},
  title        = {{Galectin-8 specificity to cells: from broad outside to fine inside}},
  url          = {{https://lup.lub.lu.se/search/files/4764968/548630.pdf}},
  year         = {{2007}},
}