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Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor.

Strickland, D K, Ashcom, J D, Williams, S, Burgess, W H, Migliorini, M, Argraves, W S·1990·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)38172-9
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Abstract

Ten peptides, derived from human alpha 2-macroglobulin (alpha 2M) receptor by chemical or proteolytic digestion, were sequenced. Comparative analysis revealed that all of the resulting sequences were present within the cDNA-deduced structure of low density lipoprotein receptor-related protein (LRP) (Herz, J., Hamann, U., Rogne, S., Myklebost, O., Gausepohl, H., and Stanley, K. K. (1988) EMBO J. 7, 4119-4127). The findings provide evidence that the alpha 2M receptor and LRP are the same molecule. Further evidence comes from immunoprecipitation experiments using a monoclonal antibody specific for the alpha 2M receptor that show this molecule, like LRP, to contain two polypeptides of approximately 420 and 85 kDa that are noncovalently associated. An additional component of this receptor system is a 39-kDa polypeptide that co-purifies with the alpha 2M receptor during affinity chromatography. Solid phase binding studies reveal that the 39-kDa polypeptide binds with high affinity (Kd = 18 nM) to the 420-kDa component of the alpha 2M receptor. The apparent identity of LRP and the alpha 2M receptor suggests that this molecule is a multifunctional receptor with the capacity to bind diverse biological ligands and highlights a possible relationship between two previously unrelated biological processes, lipid metabolism and proteinase regulation.

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  • LRP1 is a plasma membrane receptor mediating endocytosis, phagocytosis, chemotaxis and signaling for extracellular ligands including ApoE, lipoproteins, α2-macroglobulin, proteases, extracellular matrix proteins, growth factors, complement factors, heat shock proteins and dozens of other natural ligands.

    “Low density lipoprotein (LDL) receptor related protein 1 (LRP1) is a plasma membrane receptor mediating endocytosis, phagocytosis, chemotaxis and signaling for extracellular ligands, including apolipoprotein E (ApoE), lipoproteins, α2-macroglobulin, proteases, extracellular matrix proteins, growth factors, complement factors, heat shock proteins and dozens of other natural ligands (1–5).”

    From LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation (2023) · cites this paper as [5]

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Metadata

Authors
Strickland, D. K., Ashcom, J. D., Williams, S., Burgess, W. H., Migliorini, M., & Argraves, W. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-10
Volume
265
Issue
29
Pages
17401-17404
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)38172-9
Cited by
558
References
0
Language
en
Licence

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