CR:atREs binds apoE and HSPG

Stable Identifier
Reaction [binding]
Homo sapiens
CR remnants bind to apoE, enhanced by HSPG, in preparation for internalisation
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When the low-density lipoprotein receptor (LDLR) is missing, saturated or inhibited, chylomicron remnants (CRs) containing all-trans-retinyl esters (atREs) bind apolioprotein E (apoE). ApoE, secreted by hepatocytes, acts as a high-affinity ligand for the LDL-related receptor protein (LRP) family. CR:atREs:apoE then binds to cell-surface heparan sulfate proteoglycan (HSPG), abundant in the space of Disse. HSPG/apoE binding plays a critical role in the capture of CR:atREs, ready for internalization via LRPs (Futamura et al. 2005, Yamauchi et al. 2008).

Literature References
PubMed ID Title Journal Year
18507396 Role of the N- and C-terminal domains in binding of apolipoprotein E isoforms to heparan sulfate and dermatan sulfate: a surface plasmon resonance study

Yamauchi, Y, Deguchi, N, Takagi, C, Tanaka, M, Dhanasekaran, P, Nakano, M, Handa, T, Phillips, MC, Lund-Katz, S, Saito, H

Biochemistry 2008
15583000 Two-step mechanism of binding of apolipoprotein E to heparin: implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces

Futamura, M, Dhanasekaran, P, Handa, T, Phillips, MC, Lund-Katz, S, Saito, H

J. Biol. Chem. 2005
Participant Of
Orthologous Events
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