We have recently purified a novel nonmuscle α-actinin from chicken lung [Imamura and Masaki (1992)
J. Biol. Chem., (1992) 267, 25927-25933. in. press]. This lung α-actinin has Ca
2+ -sensitivity for interaction with F-actin. However, even in the presence of Ca
2+, its actin-gelation activity was much higher than that of Ca
2+-insensitive muscle-type α-actinin. Proteolytic cleavage analysis and the primary structure deduced from nucleotide sequence of cDNA showed that the lung α-actinin has structural divergence at COOH-terminal region that indudes Ca
2+-binding EF-hand motifs. This suggests that the low Ca
2+-sensitivity of the lung α-actinin is ascribed to the structural divergence.
View full abstract