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Vol. 11, Issue 5, 1499-1507, May 2000
Department of Cell Biology and Physiology, Washington University
School of Medicine, St. Louis, Missouri 63110
MAGP-1 and fibrillin-1, two protein components of extracellular
microfibrils, were shown by immunoprecipitation studies to interact
with the chondroitin sulfate proteoglycan decorin in the medium of
cultured fetal bovine chondrocytes. Decorin interacted with each
protein individually and with both proteins together to form a ternary
complex. Expression of truncated fibrillin-1 proteins in Chinese
hamster ovary cells localized proteoglycan binding to an amino-terminal
region near the proline-rich domain. A spatially analogous fibrillin-2
truncated protein did not coprecipitate the same sulfated molecule,
suggesting that chondroitin sulfate proteoglycan binding in this region
is specific for fibrillin-1. An interaction between fibrillin and
MAGP-1 was also observed under culture conditions that abrogated
decorin secretion, suggesting that the two microfibrillar proteins can
associate in the absence of the proteoglycan. Sulfation of matrix
proteins is important for elastic fiber assembly because inhibition of
sulfation was shown to prevent microfibrillar protein incorporation
into the extracellular matrix of cultured cells.
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