Heparin binding protein-44 (HBP-44)/receptor-associated protein (RAP) mediates cell-substratum adhesion of mouse NIH/3T3 cells through its binding to low density lipoprotein (LDL) receptor-related protein (LRP)

1997 ◽  
Vol 14 (2) ◽  
pp. 81-86 ◽  
Author(s):  
H. Teradatt ◽  
J. Tsutsui ◽  
J. Sanada ◽  
T. Arima ◽  
M. Ozawa
Keyword(s):  
Low Density Lipoprotein ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Heparin Binding ◽  
Related Protein ◽  
3T3 Cells ◽  
Receptor Associated Protein ◽  
Heparin Binding Protein ◽  
Nih 3T3

scholarly journals The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein

2007 ◽  
Vol 402 (1) ◽  
pp. 17-23 ◽  
Author(s):  
David R. Taylor ◽  
Nigel M. Hooper
Keyword(s):  
Prion Protein ◽  
Low Density Lipoprotein ◽  
Neuronal Cells ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Adaptor Protein ◽  
Cellular Prion Protein ◽  
Low Density ◽  
Related Protein ◽  
Density Lipoprotein Receptor

PrPC (cellular prion protein) is located at the surface of neuronal cells in detergent-insoluble lipid rafts, yet is internalized by clathrin-dependent endocytosis. As PrPC is glycosyl-phosphatidylinositol-anchored, it requires a transmembrane adaptor protein to connect it to the clathrin endocytosis machinery. Using receptor-associated protein and small interfering RNA against particular LDL (low-density lipoprotein) family members, in combination with immunofluorescence microscopy and surface biotinylation assays, we show that the transmembrane LRP1 (LDL receptor-related protein 1) is required for the Cu2+-mediated endocytosis of PrPC in neuronal cells. We show also that another LRP1 ligand that can cause neurodegenerative disease, the Alzheimer's amyloid precursor protein, does not modulate the endocytosis of PrPC.

scholarly journals Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein

2003 ◽  
Vol 369 (2) ◽  
pp. 407-416 ◽  
Author(s):  
Ingrid A.M. RELOU ◽  
Liane A.B. BAX ◽  
Herman J.M. van RIJN ◽  
Jan-Willem N. AKKERMAN
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Low Density Lipoprotein ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Site Specific ◽  
Receptor Associated Protein ◽  
G Protein Coupled ◽  
Receptor Family

Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase implicated in signalling pathways mediated by integrins and G-protein-coupled receptors (GPCRs). Upon stimulation FAK is phosphorylated on six tyrosine residues. Here we report the site-specific phosphorylation by low-density lipoprotein (LDL), which is known to induce integrin-independent FAK phosphorylation, and compare this with the effect of thrombin, which phosphorylates FAK via integrin αIIbβ3. Stimulation with LDL reveals (i) a major role for Tyr-925 phosphorylation which surpasses the phosphorylation of the other residues, including Tyr-397, in rate and extent, (ii) αIIbβ3-independent phosphorylation of Tyr-925 and Tyr-397, and (iii) complex formation between FAK and the Src-kinase Fgr but not with c-Src. These patterns differ profoundly from those induced by thrombin. LDL-induced phosphorylation of Tyr-925 and Tyr-397 was inhibited by 60—75% by receptor-associated protein, an inhibitor of members of the LDL receptor family. Thus these findings reveal a novel mechanism of FAK phosphorylation by signalling cascades involving a member of the LDL receptor family.

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