beta-Amyloid precursor protein binds to the neurite-promoting IKVAV site of laminin
| Autor: | Benjamin S. Weeks, W E Van Nostrand, Rachael L. Neve, Mathias Jucker, Maura C. Kibbey, Hynda K. Kleinman |
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| Rok vydání: | 1993 |
| Předmět: |
Neurite
Genetic Vectors Molecular Sequence Data Peptide Biology Transfection PC12 Cells Epitope Amyloid beta-Protein Precursor Laminin mental disorders Neurites Animals RNA Antisense Amino Acid Sequence Nerve Growth Factors Peptide sequence chemistry.chemical_classification Binding Sites Multidisciplinary Binding protein RNA Molecular biology Peptide Fragments chemistry biology.protein Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 90:10150-10153 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.90.21.10150 |
| Popis: | We previously characterized a 110-kDa membrane-associated laminin-binding protein (LBP110) from brain which binds the laminin A chain -Ile-Lys-Val-Ala-Val-(IKVAV) site and increases in injury. Here we demonstrate that antisera directed against different epitopes of beta-amyloid precursor protein (APP) recognize LBP110 and that APP is recognized by LBP110 antiserum. APP specifically binds IKVAV and not another biologically active laminin-derived peptide containing the amino acid sequence -Tyr-Ile-Gly-Ser-Arg-. PC-12 cells transfected with antisense APP RNA produce less APP and LBP110, and they form fewer processes when cultured on either laminin or the IKVAV peptide. Thus, LBP110 is a member of the APP family and a function for APP in neurite outgrowth is now defined. |
| Databáze: | OpenAIRE |
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