Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
PD Yurchenco, YS Cheng - Journal of Biological Chemistry, 1993 - ASBMB
Laminin, a four-arm glycoprotein, polymerizes in vitro into networks similar to those found in
basement membranes. We have dissected this calcium-dependent assembly by analyzing
proteolytic fragment binding using equilibrium gel filtration, ultracentrifugation, and electron
microscopy. The cathepsin G fragment C1-4 (three short arms) was found to aggregate with
a critical concentration similar to that for laminin. Like laminin polymerization, this assembly
was inhibited by the smaller elastase short arm fragments E4 (B1 domains VI and V) and …
basement membranes. We have dissected this calcium-dependent assembly by analyzing
proteolytic fragment binding using equilibrium gel filtration, ultracentrifugation, and electron
microscopy. The cathepsin G fragment C1-4 (three short arms) was found to aggregate with
a critical concentration similar to that for laminin. Like laminin polymerization, this assembly
was inhibited by the smaller elastase short arm fragments E4 (B1 domains VI and V) and …