LRP1

LRP1
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген LRP1[d][1]
Молекуляр функция calcium ion binding[d][2][2], apolipoprotein binding[d][3][4], lipoprotein particle receptor binding[d][3], protein-containing complex binding[d][5][6], связывание с ионом металла[d][2], protease binding[d][2], связывание с белками плазмы[d][7][8][9][…], low-density lipoprotein particle receptor activity[d][10], RNA binding[d][11], amyloid-beta binding[d][2], RNA binding[d][12], scavenger receptor activity[d][13], coreceptor activity[d][2], alpha-2 macroglobulin receptor activity[d][14][15], apolipoprotein receptor activity[d][14], clathrin heavy chain binding[d][16], signaling receptor activity[d][17], cargo receptor activity[d][2][18][19], heparan sulfate proteoglycan binding[d][14] һәм cargo receptor activity[d][20][2][19][…]
Күзәнәк компоненты мембрана өлеше[d][2], endocytic vesicle membrane[d][2], эндосома[d][2], мембрана[d][21], фокальные контакты[d][22], receptor complex[d][23], күзәнәк мембранасы[d][2][24][2], күзәнәк мембранасы өлеше[d][2], lysosomal membrane[d][25], soma[d][2], дендрит[d][2], ядрышко[d][21], clathrin-coated pit[d][2], clathrin-coated vesicle[d][2], төш[2], цитоплазма[2], цитозоль[d][21], lysosomal membrane[d][26], early endosome[d][16], фокальные контакты[d][27], мембрана[d][28][2], basolateral plasma membrane[d][16], insulin-responsive compartment[d][2], axonal growth cone[d][2], apical part of cell[d][2] һәм plasma membrane protein complex[d][14]
Биологик процесс lipoprotein metabolic process[d][2], negative regulation of neuron apoptotic process[d][2], negative regulation of platelet-derived growth factor receptor-beta signaling pathway[d][2], negative regulation of neuron projection development[d][2], эндоцитоз[d][2], regulation of actin cytoskeleton organization[d][2], regulation of phospholipase A2 activity[d][2], amyloid-beta clearance[d][29], negative regulation of Wnt signaling pathway[d][2], кеше картаюы[d][2], negative regulation of smooth muscle cell migration[d][2], positive regulation of lipid transport[d][2], рецепторно-опосредованный эндоцитоз[d][21], aorta morphogenesis[d][2], retinoid metabolic process[d][2], regulation of cholesterol transport[d][2], positive regulation of protein transport[d][2], apoptotic cell clearance[d][2], развитие многоклеточного организма[d][2], protein kinase C-activating G protein-coupled receptor signaling pathway[d][2], positive regulation of cholesterol efflux[d][2], cerebral cortex development[d][2], пролиферация клеток[d][2], lipoprotein transport[d][20], regulation of extracellular matrix disassembly[d][24], astrocyte activation involved in immune response[d][2], липидный обмен[d][14], рецепторно-опосредованный эндоцитоз[d][2][2][19][…], Фагоцитоз[30][19], positive regulation of cytosolic calcium ion concentration[d][2], negative regulation of cell-substrate adhesion[d][2], positive regulation of cell death[d][28], positive regulation of neuron projection development[d][2], receptor internalization[d][31], positive regulation of protein binding[d][28], positive regulation of insulin secretion involved in cellular response to glucose stimulus[d][2], негативная регуляция апоптоза[d][2], cellular lipid catabolic process[d][2], Трансцитоз[d][31], positive regulation of axon extension[d][2], positive regulation of endocytosis[d][28], positive regulation of axon extension involved in regeneration[d][2], positive regulation of collateral sprouting of injured axon[d][2], positive regulation of phagocytosis[d][2], negative regulation of cytosolic calcium ion concentration[d][2], negative regulation of focal adhesion assembly[d][2], negative regulation of cell death[d][2], chemoattraction of axon[d][2], positive regulation of ERK1 and ERK2 cascade[d][2], amyloid-beta clearance[d][32][30], amyloid-beta clearance by transcytosis[d][16], amyloid-beta clearance by cellular catabolic process[d][2][19][18], positive regulation of Schwann cell migration[d][2], positive regulation of amyloid-beta clearance[d][33], positive regulation of protein localization to plasma membrane[d][28], positive regulation of cholesterol import[d][2], cellular response to amyloid-beta[d][2], positive regulation of vascular associated smooth muscle cell migration[d][2], positive regulation of lysosomal protein catabolic process[d][19] һәм lysosomal transport[d][2]

LRP1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[34][35]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 2,37 2,38 2,39 2,40 2,41 2,42 2,43 2,44 2,45 2,46 2,47 2,48 2,49 2,50 2,51 2,52 2,53 2,54 2,55 2,56 2,57 2,58 2,59 2,60 2,61 2,62 2,63 2,64 2,65 2,66 2,67 2,68 GOA
  3. ↑ 3,0 3,1 Dichlberger A., Schaap F. G., Lins L. et al. Effects of six APOA5 variants, identified in patients with severe hypertriglyceridemia, on in vitro lipoprotein lipase activity and receptor binding // Arteriosclerosis, Thrombosis, and Vascular Biology — Lippincott Williams & Wilkins, 2008. — ISSN 1079-5642; 1524-4636 — doi:10.1161/ATVBAHA.108.172866 — PMID:18635818
  4. ↑ U Beisiegel, W Weber, G Ihrke et al. The LDL-receptor-related protein, LRP, is an apolipoprotein E-binding protein // Nature / M. Skipper — NPG, Springer Science+Business Media, 1989. — ISSN 1476-4687; 0028-0836 — doi:10.1038/341162A0 — PMID:2779654
  5. ↑ S Stefansson, Lawrence D. A., Argraves W. S. Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.14.8215 — PMID:8626514
  6. ↑ S Stefansson, Lawrence D. A., Argraves W. S. Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.14.8215 — PMID:8626514
  7. ↑ H Muramatsu, K Zou, N Sakaguchi et al. LDL receptor-related protein as a component of the midkine receptor // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier, 2000. — ISSN 0006-291X; 1090-2104 — doi:10.1006/BBRC.2000.2549 — PMID:10772929
  8. ↑ Sinning I., Wild K. Phosphorylation of LRP1 regulates the interaction with Fe65 // FEBS Letters — Elsevier, 2011. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2011.09.028 — PMID:21968187
  9. ↑ Eugenin E. A., King J. E., Nath A. et al. HIV-tat induces formation of an LRP-PSD-95- NMDAR-nNOS complex that promotes apoptosis in neurons and astrocytes // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2007. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0611699104 — PMID:17360663
  10. ↑ Kim J., Castellano J. M., Holtzman D. M. Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance // Neuron / K. Brose — Cell Press, Elsevier, 2009. — 13 p. — ISSN 0896-6273; 1097-4199 — doi:10.1016/J.NEURON.2009.11.013 — PMID:20005821
  11. ↑ Preiss T., Beckmann B. M., Humphreys D. T. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins // Cell — Cell Press, Elsevier, 2012. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2012.04.031 — PMID:22658674
  12. ↑ Preiss T., Beckmann B. M., Humphreys D. T. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins // Cell — Cell Press, Elsevier, 2012. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2012.04.031 — PMID:22658674
  13. ↑ Husemann J, JD L., Kodama T et al. Scavenger receptor class B type I (SR-BI) mediates adhesion of neonatal murine microglia to fibrillar beta-amyloid // J. Neuroimmunol. — Elsevier, 2001. — ISSN 0165-5728; 1872-8421 — doi:10.1016/S0165-5728(01)00239-9 — PMID:11240025
  14. ↑ 14,0 14,1 14,2 14,3 14,4 Bu G. Heparan sulphate proteoglycan and the low-density lipoprotein receptor-related protein 1 constitute major pathways for neuronal amyloid-beta uptake, Heparan Sulphate Proteoglycan and the Low-Density Lipoprotein Receptor-Related Protein 1 Constitute Major Pathways for Neuronal Amyloid-β Uptake // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2011. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.5491-10.2011 — PMID:21289173
  15. ↑ Forsberg L., Baig S. M. Whole exome sequencing identifies LRP1 as a pathogenic gene in autosomal recessive keratosis pilaris atrophicans // J. Med. Genet. — BMJ, 2015. — ISSN 0022-2593; 1468-6244 — doi:10.1136/JMEDGENET-2014-102931 — PMID:26142438
  16. ↑ 16,0 16,1 16,2 16,3 Ma Q., Kisler K., Zhu D. et al. Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance // Nat. Neurosci. — NPG, 2015. — 10 p. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN.4025 — PMID:26005850
  17. ↑ A Kurdowska, Alden S. M., Noble J. M. et al. Involvement of alpha-2-macroglobulin receptor in clearance of interleukin 8-alpha-2-macroglobulin complexes by human alveolar macrophages // Cytokine — Elsevier, 2000. — ISSN 1043-4666; 1096-0023 — doi:10.1006/CYTO.1999.0640 — PMID:10880251
  18. ↑ 18,0 18,1 Holtzman D. M., Bu G. Neuronal Clearance of Amyloid-β by Endocytic Receptor LRP1 // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2013. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.3487-13.2013 — PMID:24305823
  19. ↑ 19,0 19,1 19,2 19,3 19,4 19,5 Bu G. LRP1 in Brain Vascular Smooth Muscle Cells Mediates Local Clearance of Alzheimer's Amyloid-β // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2012. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.3987-12.2012 — PMID:23152628
  20. ↑ 20,0 20,1 S Rogne, O Myklebost, S. Rogne et al. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor // EMBO J. — NPG, 1988. — ISSN 0261-4189; 1460-2075 — doi:10.1002/J.1460-2075.1988.TB03306.X — PMID:3266596
  21. ↑ 21,0 21,1 21,2 21,3 GOA
  22. ↑ Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  23. ↑ Ghai R., Coulson E. J., Collins B. M. et al. Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1216229110 — PMID:23382219
  24. ↑ 24,0 24,1 Rozanov D. V., Hahn-Dantona E., Strickland D. K. et al. The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M311569200 — PMID:14645246
  25. ↑ Schröder B., Wrocklage C., Pan C. et al. Integral and associated lysosomal membrane proteins // Traffic — Wiley-Blackwell, Wiley, 2007. — ISSN 1398-9219; 1600-0854 — doi:10.1111/J.1600-0854.2007.00643.X — PMID:17897319
  26. ↑ Schröder B., Wrocklage C., Pan C. et al. Integral and associated lysosomal membrane proteins // Traffic — Wiley-Blackwell, Wiley, 2007. — ISSN 1398-9219; 1600-0854 — doi:10.1111/J.1600-0854.2007.00643.X — PMID:17897319
  27. ↑ Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  28. ↑ 28,0 28,1 28,2 28,3 28,4 Hooper N. M. Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M112.400358 — PMID:23386614
  29. ↑ Deane R. SRF and myocardin regulate LRP-mediated amyloid-beta clearance in brain vascular cells // Nat. Cell Biol. — NPG, 2009. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1819 — PMID:19098903
  30. ↑ 30,0 30,1 Choucair-Jaafar N., Laporte V., Levy R. et al. Complement receptor 3 (CD11b/CD18) is implicated in the elimination of β-amyloid peptides // Fundamental and Clinical Pharmacology — Wiley-Blackwell, Wiley, 2011. — ISSN 0767-3981; 1472-8206 — doi:10.1111/J.1472-8206.2010.00811.X — PMID:20199584
  31. ↑ 31,0 31,1 Pflanzner T., Petsch B., André-Dohmen B. et al. Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier // J. Cereb. Blood Flow Metab. / International Society for Cerebral Blood Flow and Metabolism — NPG, 2012. — ISSN 0271-678X; 1559-7016 — doi:10.1038/JCBFM.2012.7 — PMID:22293988
  32. ↑ Deane R. SRF and myocardin regulate LRP-mediated amyloid-beta clearance in brain vascular cells // Nat. Cell Biol. — NPG, 2009. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1819 — PMID:19098903
  33. ↑ Holtzman D. M., Kim J. Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Aβ uptake and degradation by astrocytes, Low-density Lipoprotein Receptor Represents an Apolipoprotein E-independent Pathway of Aβ Uptake and Degradation by Astrocytes // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2012. — 13 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M111.288746 — PMID:22383525
  34. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  35. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)

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