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Low density lipoprotein-related protein 1 (alpha-2-macroglobulin receptor)

PDB rendering based on 1cr8.
Available structures
1cr8, 1d2l, 1j8e, 2fyj, 2fyl
Symbols LRP1; LRP; A2MR; APOER; APR; CD91; FLJ16451; MGC88725; TGFBR5
External IDs OMIM107770 MGI96828 HomoloGene1744 GeneCards: LRP1 Gene
RNA expression pattern
PBB GE LRP1 200785 s at tn.png
PBB GE LRP1 200784 s at tn.png
More reference expression data
Species Human Mouse
Entrez 4035 16971
Ensembl ENSG00000123384 ENSMUSG00000040249
UniProt Q07954 Q3U454
RefSeq (mRNA) NM_002332 NM_008512
RefSeq (protein) NP_002323 NP_032538
Location (UCSC) Chr 12:
55.81 - 55.89 Mb
Chr 10:
126.94 - 127.02 Mb
PubMed search [1] [2]

Low density lipoprotein receptor-related protein 1 (alpha-2-macroglobulin receptor), also known as LRP1 or CD91, is a protein forming a receptor found in the plasma membrane of human cells involved in receptor-mediated endocytosis.


LRP1 and Alzheimer's disease

Neurons require cholesterol to function. Cholesterol is imported into the neuron by the apolipoprotein apoE4 via LRP1 receptors on the cell surface. It is thought that a causal factor in Alzheimer's is the malfunction of this process which damages neurons by starving them of cholesterol.[1]


LRP1 has been shown to interact with Lipoprotein lipase,[2][3][4] Urokinase receptor,[5] MAPK8IP2,[6] Tissue plasminogen activator,[7][8] Thrombospondin 1,[9][10][11] SYNJ2BP,[6] DLG4,[6] NOS1AP,[6] Calcitonin receptor,[12] APBB1,[13] ITGB1BP1,[6] MAPK8IP1,[6] GIPC1[6] and SHC1.[14][15]


  1. ^ Liu Q, Zerbinatti CV, Zhang J, Hoe HS, Wang B, Cole SL, Herz J, Muglia L, Bu G. (2007) Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56(1):66-78. PMID 17920016
  2. ^ Williams, S E; Inoue I, Tran H, Fry G L, Pladet M W, Iverius P H, Lalouel J M, Chappell D A, Strickland D K (Mar. 1994). "The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP". J. Biol. Chem. (UNITED STATES) 269 (12): 8653–8. ISSN 0021-9258. PMID 7510694.  
  3. ^ Nykjaer, A; Nielsen M, Lookene A, Meyer N, Røigaard H, Etzerodt M, Beisiegel U, Olivecrona G, Gliemann J (Dec. 1994). "A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells". J. Biol. Chem. (UNITED STATES) 269 (50): 31747–55. ISSN 0021-9258. PMID 7989348.  
  4. ^ Chappell, D A; Fry G L, Waknitz M A, Iverius P H, Williams S E, Strickland D K (Dec. 1992). "The low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor binds and mediates catabolism of bovine milk lipoprotein lipase". J. Biol. Chem. (UNITED STATES) 267 (36): 25764–7. ISSN 0021-9258. PMID 1281473.  
  5. ^ Czekay, R P; Kuemmel T A, Orlando R A, Farquhar M G (May. 2001). "Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity". Mol. Biol. Cell (United States) 12 (5): 1467–79. ISSN 1059-1524. PMID 11359936.  
  6. ^ a b c d e f g Gotthardt, M; Trommsdorff M, Nevitt M F, Shelton J, Richardson J A, Stockinger W, Nimpf J, Herz J (Aug. 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. (UNITED STATES) 275 (33): 25616–24. doi:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.  
  7. ^ Zhuo, M; Holtzman D M, Li Y, Osaka H, DeMaro J, Jacquin M, Bu G (Jan. 2000). "Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation". J. Neurosci. (UNITED STATES) 20 (2): 542–9. PMID 10632583.  
  8. ^ Orth, K; Madison E L, Gething M J, Sambrook J F, Herz J (Aug. 1992). "Complexes of tissue-type plasminogen activator and its serpin inhibitor plasminogen-activator inhibitor type 1 are internalized by means of the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 89 (16): 7422–6. ISSN 0027-8424. PMID 1502153.  
  9. ^ Wang, Shuxia; Herndon Mary E, Ranganathan Sripriya, Godyna Svetlana, Lawler Jack, Argraves W Scott, Liau Gene (Mar. 2004). "Internalization but not binding of thrombospondin-1 to low density lipoprotein receptor-related protein-1 requires heparan sulfate proteoglycans". J. Cell. Biochem. (United States) 91 (4): 766–76. doi:10.1002/jcb.10781. ISSN 0730-2312. PMID 14991768.  
  10. ^ Mikhailenko, I; Krylov D, Argraves K M, Roberts D D, Liau G, Strickland D K (Mar. 1997). "Cellular internalization and degradation of thrombospondin-1 is mediated by the amino-terminal heparin binding domain (HBD). High affinity interaction of dimeric HBD with the low density lipoprotein receptor-related protein". J. Biol. Chem. (UNITED STATES) 272 (10): 6784–91. ISSN 0021-9258. PMID 9045712.  
  11. ^ Godyna, S; Liau G, Popa I, Stefansson S, Argraves W S (Jun. 1995). "Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1". J. Cell Biol. (UNITED STATES) 129 (5): 1403–10. ISSN 0021-9525. PMID 7775583.  
  12. ^ Orr, Anthony Wayne; Pedraza Claudio E, Pallero Manuel Antonio, Elzie Carrie A, Goicoechea Silvia, Strickland Dudley K, Murphy-Ullrich Joanne E (Jun. 2003). "Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly". J. Cell Biol. (United States) 161 (6): 1179–89. doi:10.1083/jcb.200302069. ISSN 0021-9525. PMID 12821648.  
  13. ^ Trommsdorff, M; Borg J P, Margolis B, Herz J (Dec. 1998). "Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein". J. Biol. Chem. (UNITED STATES) 273 (50): 33556–60. ISSN 0021-9258. PMID 9837937.  
  14. ^ Barnes, Helen; Ackermann Elizabeth J, van der Geer Peter (Jun. 2003). "v-Src induces Shc binding to tyrosine 63 in the cytoplasmic domain of the LDL receptor-related protein 1". Oncogene (England) 22 (23): 3589–97. doi:10.1038/sj.onc.1206504. ISSN 0950-9232. PMID 12789267.  
  15. ^ Loukinova, Elena; Ranganathan Sripriya, Kuznetsov Sergey, Gorlatova Natalia, Migliorini Mary M, Loukinov Dmitri, Ulery Paula G, Mikhailenko Irina, Lawrence Daniel A, Strickland Dudley K (May. 2002). "Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function betwenn LRP and the PDGF". J. Biol. Chem. (United States) 277 (18): 15499–506. doi:10.1074/jbc.M200427200. ISSN 0021-9258. PMID 11854294.  

See also

Further reading

  • Li Z, Dai J, Zheng H, et al. (2002). "An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response.". Front. Biosci. 7: d731–51. PMID 11861214.  
  • van der Geer P (2002). "Phosphorylation of LRP1: regulation of transport and signal transduction.". Trends Cardiovasc. Med. 12 (4): 160–5. doi:10.1016/S1050-1738(02)00154-8. PMID 12069755.  
  • May P, Herz J (2004). "LDL receptor-related proteins in neurodevelopment.". Traffic 4 (5): 291–301. PMID 12713657.  
  • Llorente-Cortés V, Badimon L (2005). "LDL receptor-related protein and the vascular wall: implications for atherothrombosis.". Arterioscler. Thromb. Vasc. Biol. 25 (3): 497–504. doi:10.1161/01.ATV.0000154280.62072.fd. PMID 15705932.  
  • Huang SS, Huang JS (2005). "TGF-beta control of cell proliferation.". J. Cell. Biochem. 96 (3): 447–62. doi:10.1002/jcb.20558. PMID 16088940.  
  • Lillis AP, Mikhailenko I, Strickland DK (2005). "Beyond endocytosis: LRP function in cell migration, proliferation and vascular permeability.". J. Thromb. Haemost. 3 (8): 1884–93. doi:10.1111/j.1538-7836.2005.01371.x. PMID 16102056.  

External links



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