Cleavage of laminin by thrombin and plasmin: alpha thrombin selectively cleaves the beta chain of laminin
LA Liotta, RH Goldfarb, VP Terranova - Thrombosis research, 1981 - Elsevier
Highly purified α-thrombin, plasmin and urokinase were incubated with laminin, type IV
collagen and type V collagen. At 25° C (1: 100 enzyme to substrate ratio on a weight/weight
basis) α-thrombin selectively degraded the β chain of native laminin, whereas plasmin
degraded both the α and β chains. The specific limited cleavage fragments of laminin
produced by α-thrombin and plasmin retained the ability to mediate binding of epithelial
cells to type IV collagen. These serine proteases failed to degrade native type IV or type V …
collagen and type V collagen. At 25° C (1: 100 enzyme to substrate ratio on a weight/weight
basis) α-thrombin selectively degraded the β chain of native laminin, whereas plasmin
degraded both the α and β chains. The specific limited cleavage fragments of laminin
produced by α-thrombin and plasmin retained the ability to mediate binding of epithelial
cells to type IV collagen. These serine proteases failed to degrade native type IV or type V …