I. Yoshida et al., Identification of a heparin binding site and the biological activities of the laminin alpha 1 chain carboxy-terminal globular domain, J CELL PHYS, 179(1), 1999, pp. 18-28
The carboxy-terminal globular domain (G-domain) of the laminin alpha 1 chai
n has been shown to promote heparin binding, cell adhesion, and neurite out
growth. In this study, we defined the potential sequences originating from
the G-domain of laminin alpha 1 chain which possess these functional activi
ties. A series of peptides were synthesized from the G-domain, termed LG pe
ptides (LG-1 to LG-6) and were tested far their various biological activiti
es. In the direct [H-3]heparin binding assays, LG-6 (residues 2,335-2,348:
KDFLSIELVRGRVK) mediated high levels of [H-3]heparin binding, and this pept
ide also directly promoted cell adhesion and spreading, including B16F10, M
2, HT1080, and PC12 cells. The peptide LG-6 also promoted the neurite outgr
owth of PC12 cells, mouse granule cells and chick telencephalic cells. An a
nti-peptide LG-6 antibody inhibited laminin-1 and peptide LG-6-mediated cel
l adhesion and neurite outgrowth. Furthermore, an anti-integrin alpha 2 ant
ibody also inhibited the cell adhesion activity. These results suggest that
peptide LG-6 plays a functional role as a heparin binding site in the G-do
main of the laminin alpha 1 chain, and this sequence was thus concluded to
play a crucial role in regulating cell adhesion and spreading and neurite o
utgrowth which is related to integrin alpha 2. J. Cell. Physiol. 179:18-28,
1999. (C) 1999 Wiley-Liss, Inc.