Identifies and characterizes a novel 25-kDa actin-binding protein from bovine aorta that is a homolog of SM22 but uniquely binds F-actin and has a Ca(2+)-binding domain.
Characterizes novel aortic 25-kDa actin-binding protein; leaves open its role in human vascular smooth muscle regulation.
We have purified a Ca(2+)-sensitive 25-kDa protein from bovine aorta. The 25-kDa protein remains associated with the membrane fraction in the presence of Ca2+ and is dissociated by EGTA. The purified protein binds directly to F-actin at a ratio of 1:6 actin monomers, with a binding constant of 7.0 x 10(5) M-1. The partial sequence analysis revealed a high homology to predicted protein derived from mRNA, named WS3-10 and chicken SM22 protein. Although chicken SM22 had not any interaction with contractile proteins or Ca2+, the bovine homolog clearly binds to F-actin and has Ca(2+)-binding domain in its primary structure.
No takes yet. Share an insight, caveat, or question.
Kobayashi et al. (1994) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: