Back to Search
Start Over
Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the α2-macroglobulin receptor
- Source :
- FEBS Letters. 276:151-155
- Publication Year :
- 1990
- Publisher :
- Wiley, 1990.
-
Abstract
- The human placental receptor (alpha 2MR) for alpha 2-macroglobulin-proteinase complexes contains 3 polypeptides of approx. 500 kDa, 85 kDa, and 40 kDa. N-terminal sequence analysis of the 500 kDa and 85 kDa polypeptides, analysis of a random selection of peptides convering 536 residues from these polypeptides, and analysis of a 1772 bp cDNA encoding part of the 500 kDa polypeptide provide evidence that the 500 kDa and 85 kDa chains are the alpha- and beta-subunits, respectively, of a recently cloned hepatic membrane protein, termed the 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; Herz, J., Kowal, R.C., Goldstein, J.L. and Brown, M.S. (1990) EMBO J. 9, 1769-1776). N-terminal sequence analysis of the 40 kDa polypeptide shows that it is of distinct genetic origin. It is suggested that LRP is the functional receptor for alpha 2-macroglobulin-proteinase complexes (alpha 2MR) and in addition may have as yet unsettled functions in lipoprotein metabolism.
- Subjects :
- Sequence analysis
Placenta
Molecular Sequence Data
Biophysics
Low-density-lipoprotein receptor related protein
Biochemistry
α2-Macroglobulin receptor
LDL-receptor-related protein-associated protein
Pregnancy
Structural Biology
Cell surface receptor
Sequence Homology, Nucleic Acid
Complementary DNA
α2-Macroglobulin
HSPA2
Genetics
Humans
alpha-Macroglobulins
Amino Acid Sequence
Cloning, Molecular
Receptors, Immunologic
Receptor
Molecular Biology
biology
Cell Biology
Molecular biology
Membrane protein structure
Liver
Receptors, LDL
LDL receptor
biology.protein
Female
Low Density Lipoprotein Receptor-Related Protein-1
Cation-dependent mannose-6-phosphate receptor
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 276
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....7d0e7b68abd200b64445afbe5572559a