ライフサイエンスコーパス: LRP-2

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1 sity lipoprotein receptor-related protein-2 (LRP-2).

2 mouse F9 cells, which express high levels of LRP-2.

3 teraction of the Abeta1-40-apoJ complex with LRP-2.

4 ed protein, an antagonist of apoJ binding to LRP-2.

5 quent endocytosis of the complex by LRP-1 or LRP-2.

6 to outline the recycling pathway of Megalin (LRP-2), an apical receptor with key developmental and re

7 in receptor-related proteins Ce-LRP-1 and Ce-LRP-2 and a cytoplasmic adaptor protein, Ce-DAB-1 (Disab

8 hat clusterin has discrete binding sites for LRP-2 and other (potentially toxic) molecules.

9 respectively, and (ii) the binding sites for LRP-2 and stressed proteins are likely to be in parts of

10 e that apoJ facilitates Abeta1-40 binding to LRP-2 and that the receptor mediates cellular clearance

11 he LDL receptor-related protein (LRP), GP330/LRP-2, and very low density lipoprotein (VLDL) receptors

12 nists of receptor function such as LRP-1 and LRP-2 antibodies and the 39-kDa receptor-associated prot

13 oth processes were inhibited with polyclonal LRP-2 antibodies.

14 s of recombinant subfragments of SVS-II, the LRP-2 binding site was mapped to a stretch of repeated 1

15 The results indicate that LRP-2 binds SVS-II and can mediate its endocytosis leadi

16 The findings support the possibility that LRP-2 can act in vivo to mediate clearance of the comple

17 When LRP-2-expressing cells were given 125I-Abeta1-40, cellul

18 onment and carries these to cells expressing LRP-2 for uptake and degradation.

19 -2 was inhibited using a known antagonist of LRP-2 function, the 39-kDa receptor-associated protein R

20 Megalin (LRP-2/GP330), a member of the LDL receptor family, is an

21 ed that Abeta alone did not bind directly to LRP-2; however, when Abeta1-40 was combined with apoJ to

22 obed seminal vesicle fluid with 125I-labeled LRP-2 in a gel-blot overlay assay.

23 mediate binding of Abeta1-40-apoJ complex to LRP-2 in vitro.

24 , immunohistochemical staining revealed that LRP-2 is also expressed by epithelial cells lining the d

25 oprotein receptor-related protein-2/megalin (LRP-2) is an endocytic receptor that is expressed on the

26 To identify LRP-2 ligands in the seminal vesicle, we probed seminal

27 th processes were inhibited by antibodies to LRP-2 or by RAP.

28 mately 600 kD, variously named gp600, gp330, LRP-2, or "megalin." This study was performed to identif

29 Ce-LRP-1 and Ce-LRP-2 possess a conserved intraluminal domain that can b

30 Using purified preparations of SVS-II and LRP-2, solid-phase binding assays were used to show that

31 ree independent classes of binding sites for LRP-2, stressed proteins, and unstressed ligands, respec

32 To evaluate the ability of LRP-2 to mediate 125I-SVS-II endocytosis and lysosomal d

33 ined with apoJ to form a complex, binding to LRP-2 took place.

34 The binding of SVS-II to LRP-2 was inhibited using a known antagonist of LRP-2 fu

35 oprotein receptor-related protein-2/megalin (LRP-2), which is expressed by choroid plexus epithelium

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