Apolipoprotein(a): structural and functional consequences of mutations in kringle type 10 (or kringle 4-37)

The size polymorphism of Lp(a) is well recognized. It is now apparent that there is an additional polymorphism resulting from mutations occurring at the kringle level. One of these mutations involves a trp72 to arg substitution in apo(a) kringle type 10 and is attended by a defective binding of Lp(a) to immobilized lysine/fibrin. Other mutations affecting the other amino acids of the "lysine-binding pocket" may have similar functional consequences and may be important at the clinical level in terms of thrombogenesis.