Premium
Active sites in the carboxyl‐terminal region of the laminin α chain in Drosophila neuronal cell spreading
Author(s) -
Takagi Yasumitsu,
Nomizu Motoyoshi,
UiTei Kumiko,
Tokushige Naoko,
Hirohashi Setsuo
Publication year - 2004
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20006
Subject(s) - laminin , biology , glycoprotein , neurite , cell , cell culture , microbiology and biotechnology , biochemistry , genetics , in vitro
An established Drosophila neuronal cell line (BG2‐c6) proved to be useful to analyze laminin‐mediated cell spreading and signal transduction [Takagi et al. (2000) Biochem Biophys Res Commun 270:482–487]. Here, we report, in addition to the whole molecule, the truncated α chain of Drosophila laminin (containing the entire carboxyl‐terminal globular domain) and two dodecapeptides corresponding to the cell‐binding sites identified in the α1 chain of mouse laminin were also active to stimulate BG2‐c6 cell spreading. Our previous study [Takagi et al. (1996) J Biol Chem 271:18074–18081] revealed that these recombinant protein and synthetic peptides promoted neurite outgrowth in the primary cell culture system prepared from Drosophila embryo. Therefore, the similar effects by these proteins and peptides suggest the presence of a common mechanism of laminin and neuronal cell interaction working in both primary and established cells. One of the two active peptides contains the sequence SIKVGV. Its murine counterpart carries the sequence SIKVAV by which the interaction of laminin and cells is mediated. Furthermore, laminin‐dependent BG2‐c6 cell spreading was inhibited by heparin. This observation suggests that cell surface glycoproteins participate in the interaction of laminin and BG2‐c6 cells. Arch. Insect Biochem. Physiol. 56:162–169, 2004. © 2004 Wiley‐Liss, Inc.