S100 Calcium Binding Protein A1, also known as S100A1, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions through EF-hand motifs, which are helix-loop-helix structural domains . S100A1 is highly expressed in cardiac and skeletal muscle tissues, as well as in the brain .
S100A1 contains four EF-hand calcium-binding motifs in its dimerized form . It can exist as either a heterodimer or a homodimer, with the homodimer being formed through hydrophobic interactions between specific helices . The protein’s structure allows it to undergo conformational changes upon binding calcium ions, which is crucial for its function .
S100A1 plays a significant role in various biological processes, including calcium homeostasis, chondrocyte biology, and cardiomyocyte regulation . In cardiomyocytes, S100A1 regulates a network controlling sarcoplasmic reticulum calcium cycling and mitochondrial function . It interacts with several key proteins, such as ryanodine receptors, sarcoplasmic reticulum calcium-ATPase, and mitochondrial F1-ATPase .
The expression of S100A1 has been implicated in several diseases. Reduced expression of this protein is associated with cardiomyopathies, which are diseases of the heart muscle that can lead to heart failure . Additionally, S100A1 has shown promise as a candidate for gene therapy to treat post-myocardial infarction cardiac tissue .