Identification of a heparin binding site and the biological activities of the laminin alpha 1 chain carboxy-terminal globular domain

Citation
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
Citations number
49
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF CELLULAR PHYSIOLOGY
ISSN journal
00219541 → ACNP
Volume
179
Issue
1
Year of publication
1999
Pages
18 - 28
Database
ISI
SICI code
0021-9541(199904)179:1<18:IOAHBS>2.0.ZU;2-8
Abstract
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.