Contribution of αLNNd to laminin accumulation on Schwann
cell (SC) surfaces. Cells were cultured with the indicated proteins for 1
h and immunostained for the laminin β1 subunit (E4-specific antibody).
Panels A and B, quantitation of laminin (A) and
corresponding entactin antigen (B) immunofluorescence summed cell
intensities for laminin (Lm, closed circles), αLNNd (constant
26 nm) with increasing LmΔαLN (closed inverted
triangles), nidogen-1 (26 nm) with increasing
LmΔαLN (open triangles), and LmΔαLN alone
(open circles) (average and S.D., n ≥ 5). The addition of
αLNNd, but not nidogen-1, to the non-polymerizing LmΔαLN
enabled self-assembly to a degree approaching that of intact laminin.
Panels C and D, cells were incubated with the indicated
proteins (constant 14 nm laminin and 14 nm αLNNd).
αLNNd enabled the cell surface assembly of laminins bearing deletions of
the αLN domain but not deletions of the βLN or γLN
domains.