Recombinant αLNNd and mAgrin. Panel A,
αLNNd and mAgrin. The chimeric protein αLNNd is composed of the
N-terminal LN and LEa domains of the laminin α1 subunit (containing
laminin polymerization (P) activity) fused to the C-terminal G2, LE,
and G3 domains of nidogen-1 (containing type IV collagen-binding (C4)
and laminin γ1-binding (Lm) activities). The internally
truncated protein mAgrin consists of the laminin coiled-coil binding NtA
domain fused through the first follistatin (FS) domain to the
dystroglycan and sulfatide binding (DG/S) terminal laminin-like LG
and LE domain complex. Panel B, Coomassie Blue-stained gels
(SDS-PAGE, 8% acrylamide, reducing conditions) of mAgrin, αLNNd,
LmΔ(αLN&LG), LmΔαLN, and (wt) laminin-111.
Panel C, diagrammatic representations of the recombinant
heterotrimeric laminins used in this study.