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J. Biol. Chem., Vol. 276, Issue 2, 1253-1261, January 12, 2001
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From the Aggrecan, versican, neurocan, and brevican are
important components of the extracellular matrix in various tissues.
Their amino-terminal globular domains bind to hyaluronan, but the
function of their carboxyl-terminal globular domains has long remained elusive. A picture is now emerging where the C-type lectin motif of
this domain mediates binding to other extracellular matrix proteins. We
here demonstrate that aggrecan, versican, and brevican lectin domains
bind fibulin-2, whereas neurocan does not. As expected for a C-type
lectin, the interactions are calcium-dependent, with KD values in the nanomolar range as measured by
surface plasmon resonance. Solid phase competition assays with
previously identified ligands demonstrated that fibulin-2 and
tenascin-R bind the same site on the proteoglycan lectin domains.
Fibulin-1 has affinity for the common site on versican but may bind to
a different site on the aggrecan lectin domain. By using deletion mutants, the interaction sites for aggrecan and versican lectin domains
were mapped to epidermal growth factor-like repeats in domain II of
fibulin-2. Affinity chromatography and solid phase assays confirmed
that also native full-length aggrecan and versican bind the lectin
domain ligands. Electron microscopy confirmed the mapping and
demonstrated that hyaluronan-aggrecan complexes can be cross-linked by
the fibulins.
The Proteoglycans Aggrecan and Versican Form Networks with
Fibulin-2 through Their Lectin Domain Binding*
,,, and¶
Department of Cell and Molecular Biology,
Section for Connective Tissue Biology, Lund University,
BMC Plan C12, SE-221 84 Lund, Sweden and
§ Max-Planck-Institut für Biochemie,
D-82152 Martinsried, Germany
*
This work was supported by the Swedish Medical Research
Council, Crafoord's Stiftelse, Greta och Johan Kocks Stiftelser,
Konung Gustaf V's 80-Årsfond, Reumatikerförbundet, Åke Wibergs
Stiftelse, Alfred Österlunds Stiftelse, the Deutsche
Forschungsgemeinschaft Grant SFB 266, and by a grant from the program
"Glycoconjugates in Biological Systems" sponsored by the Swedish
Foundation for Strategic Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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