| First Author | Sasaki T | Year | 2010 |
| Journal | Matrix Biol | Volume | 29 |
| Issue | 6 | Pages | 484-93 |
| PubMed ID | 20566382 | Mgi Jnum | J:163713 |
| Mgi Id | MGI:4829569 | Doi | 10.1016/j.matbio.2010.05.004 |
| Citation | Sasaki T, et al. (2010) Laminin-121-Recombinant expression and interactions with integrins. Matrix Biol 29(6):484-93 |
| abstractText | Laminin-121, previously referred as to laminin-3, was expressed recombinantly in human embryonic kidney (HEK) 293 cells by triple transfection of full-length cDNAs encoding mouse laminin alpha1, beta2 and gamma1 chains. The recombinant laminin-121 was purified using Heparin-Sepharose followed by molecular sieve chromatography and shown to be correctly folded by electron microscopy and circular dichroism (CD). The CD spectra of recombinant laminin-121 were very similar to those of laminin-111 isolated from Engelbreth-Holm-Swarm tumor (EHS-laminin) but its T(m) value was smaller than EHS-laminin and recombinant lamnin-111 suggesting that the replacement of the beta chain reduced the stability of the coiled-coil structure of laminin-121. Its binding to integrins was compared with EHS-laminin, laminin-3A32 purified from murine epidermal cell line and recombinantly expressed laminins-111, -211 and -221. Laminin-121 showed the highest affinity to alpha6beta1 and alpha7beta1 integrins and furthermore, laminin-121 most effectively supported neurite outgrowth. Together, this suggests that the beta2 laminins have higher affinity for integrins than the beta1 laminins. |
