Formation of high molecular weight dermatan sulfate proteoglycan in bovine aortic endothelial cell cultures. Evidence for transglutaminase-catalyzed cross-linking to fibronectin.
1990
Abstract Three
glucuronate-rich
dermatan sulfateproteoglycan (DS-PG) subclasses were isolated and previously characterized from bovine aortic endothelial cell cultures (Kinsella, M. G., and
Wight, T. N. (1988) J. Biol. Chem. 263, 19222-19231). In the present study, pulse-chase experiments indicate that the DS-PG of highest apparent Mr (approximately 1 x 10(6)), denoted previously as HMW-DS, is a relatively stable component of the endothelial extracellular matrix and is formed at the expense of lower Mr DS-PG species. The formation of HMW-DS is reduced in a dose-dependent manner in the presence of dansylcadaverine, an inhibitor of transglutaminase-catalyzed protein
cross-linking, but not when the activity of other
cross-linkingenzymes such as
lysyl oxidaseis inhibited. The putative DS-PG precursor to HMW-DS accumulates during inhibition of
cross-linkingonly when lysosomal degradation is also inhibited by ammonium chloride, suggesting that the precursor is degraded rapidly in the absence of
cross-linking. HMW-DS is precipitable from endothelial cell monolayer extracts with antibodies against fibronectin, a known transglutaminase substrate. Thus, we conclude that the stability of HMW-DS in the subendothelial matrix in culture depends upon the
cross-linkingof a low Mr DS-PG precursor to matrical
protein(s), including fibronectin, resulting in the formation of a DS-PG subclass of high apparent molecular mass.
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