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LRP2 — SERPINE1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Hprd Interaction: LRP2 — SERPINE1 (in vitro) Moestrup et al., J Biol Chem 1993*
• IRef Ophid Interaction: LRP2 — SERPINE1 (aggregation, confirmational text mining) Moestrup et al., J Biol Chem 1993*
• IRef Ophid Interaction: LRP2 — SERPINE1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Camani et al., Thromb Haemost 2000 : In five cell lines from different organs and species degradation of t-PA and t-PA/PAI-1 was mediated by LRP ( or LRP-like receptors )
Degryse et al., J Biol Chem 2004 : These results indicate that LRP is a signaling molecule, that it mediates the migration promoting activity of PAI-1, and that this activity does not require intact, biologically active PAI-1 ... Activation of this LRP dependent signaling pathway by PAI-1 may begin to explain how the inhibitor stimulates cell migration in a variety of normal and pathological processes
Whitley et al., Int J Oncol 2005 : By contrast, smooth muscle cell wound induced migration was promoted by exogenously added PAI-1 , but this enhancement was dependent on PAI-1 binding to LRP , not binding to VN
Balsara et al., Curr Drug Targets 2007 (Anoxia) : Furthermore, independent of its inhibitory activity PAI-1 mediates interactions with vitronectin (VN) and low density lipoprotein receptor related protein ( LRP ) which modifies basic cell behaviors of proliferation, migration, and attachment