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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1990-7-6
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pubmed:abstractText |
The low density lipoprotein receptor-related protein (LRP) is a cell surface glycoprotein that binds and transports plasma lipoproteins enriched in apolipoprotein E. It is synthesized in the endoplasmic reticulum as a transmembrane glycosylated precursor that migrates with an apparent molecular mass of about 600 kd on SDS-polyacrylamide gels. After it reaches the Golgi complex, the protein is cleaved to generate two subunits with apparent molecular masses of approximately 515 and 85 kd respectively. The larger NH2-terminal alpha-subunit lacks a membrane-spanning region. It remains attached to the membrane through noncovalent association with the smaller COOH-terminal beta-subunit. Proteolysis occurs at the sequence RHRR, which resembles the sequence RKRR at the proteolytic site in the receptors for insulin and insulin-like growth factor-1 (IGF-1), the only other cell surface receptors known to undergo proteolytic processing. Proteolysis of LRP occurs coincident with the conversion of the N-linked carbohydrates to the mature endoglycosidase H-resistant, neuraminidase-sensitive form. Proteolysis is prevented by brefeldin A, which blocks transport to the Golgi complex. These data raise the possibility that LRP and the receptors for insulin and IGF-1 are processed by a specific endoprotease that recognizes protein with extended basic sequences and resides in the trans-Golgi complex or in post-Golgi vesicles of the constitutive secretory pathway.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2594771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2647301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2697236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2762297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2779654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2877871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2983222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-2988123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3266596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3366784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3417658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3494949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3611052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-3896128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6321901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6322002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6327078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6363328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6411700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-6526384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2112085-7016338
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclopentanes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Low Density Lipoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosyl-Glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1769-76
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2112085-Acetylglucosaminidase,
pubmed-meshheading:2112085-Amino Acid Sequence,
pubmed-meshheading:2112085-Animals,
pubmed-meshheading:2112085-Antibodies, Monoclonal,
pubmed-meshheading:2112085-Brefeldin A,
pubmed-meshheading:2112085-Cells, Cultured,
pubmed-meshheading:2112085-Cyclopentanes,
pubmed-meshheading:2112085-Fluorescent Antibody Technique,
pubmed-meshheading:2112085-Glycoside Hydrolases,
pubmed-meshheading:2112085-Golgi Apparatus,
pubmed-meshheading:2112085-Humans,
pubmed-meshheading:2112085-Liver,
pubmed-meshheading:2112085-Low Density Lipoprotein Receptor-Related Protein-1,
pubmed-meshheading:2112085-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:2112085-Mice,
pubmed-meshheading:2112085-Molecular Sequence Data,
pubmed-meshheading:2112085-Molecular Weight,
pubmed-meshheading:2112085-Neuraminidase,
pubmed-meshheading:2112085-Protein Conformation,
pubmed-meshheading:2112085-Rabbits,
pubmed-meshheading:2112085-Rats,
pubmed-meshheading:2112085-Receptors, Immunologic
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pubmed:year |
1990
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pubmed:articleTitle |
Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment.
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pubmed:affiliation |
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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