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Calcium-dependent self-association of the C-type lectin domain of versican

Ney, A ; Booms, P ; Epple, G ; Mörgelin, Matthias LU ; Guo, G ; Kettelgerdes, G ; Gessner, R and Robinson, PN (2006) In International Journal of Biochemistry & Cell Biology 38(1). p.23-29
Abstract
Versican is a large (1-2 x 10(6) Da) chondroitin-sulfate proteoglycan that can form large aggregates by means of interaction with hyaluronan and also binds to a series of other extracellular matrix proteins, chemokines and cell-surface molecules. Versican is a multifunctional molecule with roles in cell adhesion, matrix assembly, cell migration and proliferation. Characterization of the binding interactions mediated by the various domains of versican is a first step towards understanding the functions of versican and interacting molecules in the extracellular matrix. In this study we investigated a recombinant construct corresponding to the C-type lectin domain of versican and demonstrated a calcium-dependent self-association of this... (More)
Versican is a large (1-2 x 10(6) Da) chondroitin-sulfate proteoglycan that can form large aggregates by means of interaction with hyaluronan and also binds to a series of other extracellular matrix proteins, chemokines and cell-surface molecules. Versican is a multifunctional molecule with roles in cell adhesion, matrix assembly, cell migration and proliferation. Characterization of the binding interactions mediated by the various domains of versican is a first step towards understanding the functions of versican and interacting molecules in the extracellular matrix. In this study we investigated a recombinant construct corresponding to the C-type lectin domain of versican and demonstrated a calcium-dependent self-association of this region by blot overlay and plasmon surface resonance assays. Electron microscopy provided further evidence of the relevance of the binding reaction by demonstrating a mixture of monomers, dimers and complex aggregates of recombinant versican C-type lectin domain. This binding reaction could contribute to the ability of versican to organize formation of the proteoglycan extracellular matrix by inducing binding of individual versican molecules or by modulating binding reactions to other matrix components. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
connective tissue, extracellular matrix, surface plasmon resonance, versican, C-type lectin domain, electron microscopy
in
International Journal of Biochemistry & Cell Biology
volume
38
issue
1
pages
23 - 29
publisher
Elsevier
external identifiers
  • wos:000233553300005
  • pmid:16159712
  • scopus:27544498027
ISSN
1878-5875
DOI
10.1016/j.biocel.2005.07.007
language
English
LU publication?
yes
id
1b5120d6-32e8-439a-ba23-56d4db338052 (old id 693900)
date added to LUP
2016-04-01 15:53:50
date last changed
2020-01-12 18:50:22
@article{1b5120d6-32e8-439a-ba23-56d4db338052,
  abstract     = {Versican is a large (1-2 x 10(6) Da) chondroitin-sulfate proteoglycan that can form large aggregates by means of interaction with hyaluronan and also binds to a series of other extracellular matrix proteins, chemokines and cell-surface molecules. Versican is a multifunctional molecule with roles in cell adhesion, matrix assembly, cell migration and proliferation. Characterization of the binding interactions mediated by the various domains of versican is a first step towards understanding the functions of versican and interacting molecules in the extracellular matrix. In this study we investigated a recombinant construct corresponding to the C-type lectin domain of versican and demonstrated a calcium-dependent self-association of this region by blot overlay and plasmon surface resonance assays. Electron microscopy provided further evidence of the relevance of the binding reaction by demonstrating a mixture of monomers, dimers and complex aggregates of recombinant versican C-type lectin domain. This binding reaction could contribute to the ability of versican to organize formation of the proteoglycan extracellular matrix by inducing binding of individual versican molecules or by modulating binding reactions to other matrix components.},
  author       = {Ney, A and Booms, P and Epple, G and Mörgelin, Matthias and Guo, G and Kettelgerdes, G and Gessner, R and Robinson, PN},
  issn         = {1878-5875},
  language     = {eng},
  number       = {1},
  pages        = {23--29},
  publisher    = {Elsevier},
  series       = {International Journal of Biochemistry & Cell Biology},
  title        = {Calcium-dependent self-association of the C-type lectin domain of versican},
  url          = {http://dx.doi.org/10.1016/j.biocel.2005.07.007},
  doi          = {10.1016/j.biocel.2005.07.007},
  volume       = {38},
  year         = {2006},
}