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J Biol Chem, Vol. 274, Issue 29, 20444-20449, July 16, 1999
,
From the The aggregating proteoglycans (aggrecan,
versican, neurocan, and brevican) are important components of many
extracellular matrices. Their N-terminal globular domain binds to
hyaluronan, but the function of their C-terminal region containing a
C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as
fibulin-1. This extracellular matrix glycoprotein is strongly expressed
in tissues where versican is expressed (blood vessels, skin, and
developing heart), and also expressed in developing cartilage and bone.
It is thus likely to interact with these proteoglycans in
vivo. Surface plasmon resonance measurements confirmed that aggrecan and versican lectin domains bind fibulin-1, whereas brevican and neurocan do not. As expected for a C-type lectin, the interactions with fibulin-1 are Ca2+-dependent, with
KD values in the low nanomolar range. Using various
deletion mutants, the binding site for aggrecan and versican lectin
domains was mapped to the epidermal growth factor-like repeats in
domain II of fibulin-1. No difference in affinity was found for
deglycosylated fibulin-1, indicating that the proteoglycan C-type
lectin domains bind to the protein part of fibulin-1.
Department of Cell and Molecular Biology,
Section for Connective Tissue Biology, Lund University, P. O. Box
94, SE-221 00 Lund, Sweden and the ¶ Max-Planck-Institut für
Biochemie, D-82152 Martinsried, Germany
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