g to negatively charged phospholipids is thought to be mediated by Ca2+ ions.
Annexin A7 is unique in that it carries an extraordinarily long and hydrophobic amino terminus with more than 100 amino acids. Alternative splicing gives rise to two isoforms of 47 and 51 kDa. Both isoforms differ by an additional cassette exon located in the first third of the N-terminal domain. Most tissues harbor only the 47 kDa isoform, both forms are found in brain and heart, while the large isoform is exclusively expressed in mature skeletal muscle.
At the cellular level annexin A7 can be detected in the cytosol, at the plasma membrane, around the nucleus, at vesicular structures including adrenal chromaffin granules, and at the t-tubule system [5,6]. A