Identification of Cell Adhesive Sequences in the N-terminal Region of the Laminin α2 Chain

Abstract

Background:The N-terminal region of the laminin ␣2 chain promotes laminin assembly and cell adhesion. Results: Screening of 218 peptides revealed that 11 sequences derived from N-terminal laminin ␣2 chain promote cell adhesion. Conclusion: Three amino acids in the N terminus LN domain are critical sites for integrin ␣2␤1 binding. Significance: Eleven active peptides may be useful as tools for the study of laminin-receptor interactions.

The laminin family

“…36,37 They are ligands for the a1β1 and a2β1 integrins, which are classical collagen receptors, and they have been mapped to the LN domain of the laminin a1 and a2 chains. [38][39][40][41] The biological relevance of these interactions remains to be elucidated.…”

Biological activity of peptide‐conjugated polyion complex matrices consisting of alginate and chitosan

“…Previously, we have identified various biologically active peptides from a set of synthetic peptides that covered the entire laminin sequences. These active peptides interacted with various cell surface receptors, including integrins and syndecans.…”

Identification of peptides derived from the C‐terminal domain of fibulin‐7 active for endothelial cell adhesion and tube formation disruption

“…However, fc10 was active for cell attachment when coated in the plate, but was not in the bead assay (Table ). Although this may seem controversial, differences in cell attachment activity on the plate assay and bead assay have been reported for a number of synthetic peptides derived from ECM proteins . This is the case of a peptide from the laminin α1 chain, the IKVAV peptide, which is active for cell adhesion and neurite outgrowth only when it is coated on the plate .…”

“…Thirteen peptides covering the C terminal part of Fbln7 (residues 332–440) were designed (Figure ). All peptides were manually synthesized by the N‐9‐fluorenylmethoxycarbonyl (Fmoc)‐based solid phase method with a C‐terminal amide, as previously described and were purified by reverse phase HPLC. The AG73 peptide (RKRLQVQLSIRT, mouse laminin α1 chain residues 2719–2730) and the EF1 peptide (DYATLQLQEGRLHFMFDLG, mouse laminin α1 chain residues 2747–2765), were synthesized as described above and used as controls for heparan sulfate‐mediated cell attachment, and for integrin‐mediated cell attachment, respectively.…”