Many advances have occurred in the field of Barth Syndrome biology in the 26 
years since it was first described as an X-linked cardiomyopathy. Barth Syndrome 
is the first human disease recognized in which the primary causative factor is 
an alteration in cardiolipin remodeling. Cardiolipin is required for the optimal 
function of many proteins within the mitochondria, particularly in the 
respiratory chain and is involved in the mitochondrial-mediated apoptotic 
process. The appropriate content of cardiolipin appears to be critical for these 
functions. Cardiolipin is synthesized de novo in mitochondria and is rapidly 
remodeled to produce CL enriched in linoleic acid. The Barth Syndrome gene TAZ 
has been identified and expression of the gene yields proteins known as 
tafazzins. Mutations in TAZ result in a decrease in tetra-linoleoyl species of 
cardiolipin and an accumulation of monolysocardiolipin within cells from Barth 
Syndrome patients. Although the protein product of the TAZ gene shows sequence 
homology to the glycerolipid acyltransferase family of enzymes, its precise 
biochemical function remains to be elucidated. In this review we highlight some 
of the recent literature on cardiolipin metabolism and Barth Syndrome.