Claus Munck Petersen

The multiligand α2-macroglobulin receptor/low density lipoprotein receptor-related protein

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The fusion of separate lines of research has greatly helped in elucidating the function of the giant members of the low density lipoprotein (LDL) receptor (LDLR) supergene family. The cDNA encoding a large protein structurally closely related to LDLR, and hence named LDLR-related protein (LRP), was cloned by Herz et al. in 1988.'Evidence was provided demonstrating that LRP can function as a receptor for chylomicron remnants@-migrating very low density lipoproteins (P-VLDL) rich in apolipoprotein E (apoE)?' The a2-macroglobulin (a2M) receptor (a2MR) was purified from rat livep and human p l a~e n t ab~y. ~af finity chromatography using immobilized a2M in the receptor-active conformation (a2M*). The first fusion occurred with the demonstration of identity between a2MR and LRP.'.' The receptor was thought to play the role of a double agent: as symbolized by its double name. The next fusion arose from the observation that affinity-purified a2MR/LRP contains a 40-kDa5.8 or 39-kDa6.' protein, designated a2MRAP, in addition to the a2MFULRP a- and P-chains. cDNA cloning" disclosed the 323-residue protein as both the human homologue of mouse heparin binding protein 44 (see reference 11) and, interestingly, a sequence thought to be the pathogenic domain12 of rat epithelial glycoprotein 330 (gp330), the Heymann nephritis antigen. gp330 is another giant member of the LDLR family according to the sequence of the partially cloned cDNA.''
Original languageEnglish
JournalNew York Academy of Sciences. Annals
Volume737
Pages (from-to)20-38
ISSN0077-8923
DOIs
Publication statusPublished - 1994

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