Identification of a neuronal laminin receptor: An Mr 200K/120K integrin heterodimer that binds laminin in a divalent cation-dependent manner
| Autor: | Michael J. Ignatius, Louis F. Reichardt |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Neurons
Integrins biology Cations Divalent General Neuroscience Protein subunit Integrin CD49c Molecular biology Rats Collagen receptor Cell biology Molecular Weight Receptors Laminin Neuroblastoma nervous system Integrin alpha M Laminin Tumor Cells Cultured biology.protein Animals Integrin beta 6 Receptors Immunologic G alpha subunit |
| Zdroj: | Neuron. 1:713-725 |
| ISSN: | 0896-6273 |
| DOI: | 10.1016/0896-6273(88)90170-5 |
| Popis: | Neuronal interactions with extracellular matrix (ECM) components are crucial for axon growth and guidance during development and nerve regeneration. Laminin (LN), a prominent ECM glycoprotein, promotes neuronal survival and axon growth. To identify neuronal receptors for LN, we looked for cell surface proteins on the neuronal cell line B50 that bind LN. An integrin alpha/beta 1 dimeric receptor was identified and purified using lectin and LN affinity chromatography. The purified integrin contains two subunits with Mrs of 200 K and 120 K that bind LN specifically in the presence, but not the absence, of divalent cations (Ca2+/Mg2+ or Ca2+/Mn2+). The Mr 120 K protein was identified as the rat integrin beta 1 subunit using two beta 1 subunit-specific antibodies, and was shown to form a noncovalent complex with the Mr 200K putative alpha subunit. Since neurons and neuronal cell lines express similar integrin beta 1-class heterodimers that mediate attachment and process outgrowth on LN, the Mr 200K/120K complex identified here is likely to be an important laminin receptor used by neurons. This integrin may also mediate binding to LN by many nonneuronal cell types. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|