The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Low-density-lipoprotein-receptor-related protein (LRP) interacts with a GTP-binding protein
Abstract
The low-density-lipoprotein-receptor-related protein (LRP) binds and internalizes numerous ligands, including lipoproteins, proteinase–inhibitor complexes and others. We have shown previously that LRP-mediated ligand internalization is dependent on cAMP-dependent protein kinase (PKA) activity. Here, we investigated whether ligation of LRP increases the intracellular cAMP level and PKA activity via a stimulatory GTP-binding protein. Treatment of LRP-expressing cell lines with the LRP ligands lactoferrin or urokinase-type plasminogen activator caused a significant elevation in cAMP and stimulated PKA activity in a dose-dependent manner. Addition of the 39 kDa receptor-associated protein (RAP), an antagonist for ligand interactions with LRP, blocked the lactoferrin-induced increase in PKA activity, demonstrating a requirement for ligand binding to LRP. Incubation of cell membrane fractions with lactoferrin increased GTPase activity in a time- and dose-dependent manner, and treatment with LRP ligands suppressed cholera-toxin-mediated ADP-ribosylation of the Gsα subunit of a heterotrimeric G-protein. Affinity precipitation of LRP with RAP resulted in co-precipitation of two isoforms of Gsα from detergent extracts. We thus conclude that LRP is a signalling receptor that associates directly with a stimulatory heterotrimeric G-protein and activates a downstream PKA-dependent pathway.
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The LRP tail interacts with a GTP-binding protein, and binding of at least two LRP ligands increases intracellular cAMP levels and the activity of cAMP-dependent protein kinase.
“Goretzki and Mueller (56) have shown that LRP tail interacts with a GTP-binding protein and that binding of at least two LRP ligands increases intracellular cAMP levels and the activity of cAMP-dependent protein kinase.”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [56]
The Discussion reports that two LRP ligands, lactoferrin and uPA, raise intracellular cAMP and stimulate cAMP-dependent protein kinase activity. It also describes a physical and functional association between LRP and a G-protein, but does not establish that the interaction occurs specifically at the LRP tail. (LLM, conf=0.88)
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Rohlmann, A., Gotthardt, M., Hammer, R. E., & Herz, J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1240 · Cited by 455
Willnow, T. E., Rohlmann, A., Horton, J., Otani, H., Braun, J. R., Hammer, R. E., & Herz, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00623.x · Cited by 276
Evidence for a second alpha 2-macroglobulin receptor.
Misra, U. K., Chu, C. T., Gawdi, G., & Pizzo, S. V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99909-6 · Cited by 102
Narita, M., Bu, G., Holtzman, D. M., & Schwartz, A. L. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68020587.x · Cited by 96
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Research works printed but not linked: 3
- Manning, D. R. (1990) in ADP-Ribosylating Toxins and G-proteins : Insights into Signal Transduction (Moss, J. and Vaughan, M., eds.), pp. 349-370, American Society for Microbiology, Washington, DC 16
- Wiley, H. S., Herbst, J. J., Walsh, B. J., Lauffenburger, D. A., Rosenfeld, M. G. and Gill, G. N. (1991) J. Biol. Chem. 266, 11083-11094
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Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures
LaDu, M. J., Shah, J. A., Reardon, C. A., Getz, G. S., Bu, G., Hu, J., Guo, L., & Van Eldik, L. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000602200 · Cited by 103
Donoso, M., Cancino, J., Lee, J., van Kerkhof, P., Retamal, C., Bu, G., Gonzalez, A., Cáceres, A., & Marzolo, M.-P. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0805 · Cited by 69
Metadata
- Authors
- GORETZKI, L., & MUELLER, B. M.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1998-12-01
- Volume
- 336
- Issue
- 2
- Pages
- 381-386
- ISSN
- 0264-6021
- 1470-8728
- Cited by
- 74
- References
- 4
- Language
- en
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