Skip to main content
. 2007 May;18(5):1621–1633. doi: 10.1091/mbc.E06-09-0806

Figure 1.

Figure 1.

Domain structures of LN5 and recombinant γ2 proteins. (A) Schematic structure of LN5 molecule (α3β3γ2) and its proteolytic processing sites. Top closed arrow, cleavage site in the human laminin γ2 chain to produce the 105-kDa chain and the 45-kDa γ2 fragment (γ2pf); open arrow, second cleavage site in the rat laminin γ2 chain to produce the 80-kDa chain and the 25- and 45-kDa fragments; bottom arrow, cleavage site in the human laminin α3 chain to produce the 160-kDa α3 chain and a LG4–5 fragment; LG, laminin carboxyl-terminal globular domain of the α3 chain. Roman numerals indicate the domains of the γ2 chain: domains III (or LEb), IV (or L4), and V (or LEa). (B) Schematic diagram of the structures of the full-length human laminin γ2 chain and recombinant γ2 proteins. Numerals indicate the positions of amino acid residues from the NH2-terminus. Shadow boxes indicate the signal sequence. (C) SDS-PAGE of the purified γ2 chain short arm (γ2sa) on a 10% gel under reducing condition. Proteins were stained with silver.