Native ApoA-I is the principal protein component of high density lipoprotein (HDL). ApoA-I gives HDL its ability to transport cholesterol from the periphery to the liver, and thereby prevent cholesterol deposition in the arterial wall. This is why HDL is known as “good cholesterol.” Biochemically, ApoA-I contains an extra cysteine bridge, causing it to exist as a homodimer or as a heterodimer with ApoA-II. However, the enhanced cardioprotective activity of this mutant (which likely depends on cholesterol efflux) cannot easily be replicated by other cysteine mutants.

ApoA-I has recently been shown to be a better indicator of cardiovascular events than low density lipoprotein, revealing the powerful role played by this protein. Availability of the recombinant protein will allow investigators to further elucidate the function of ApoA-I and investigate potential therapeutic applications.

Defects in the gene encoding it are associated with HDL deficiencies, including Tangier disease, and with systemic non-neuropathic amyloidosis. In one study, a decrease in ApoA1 levels was detected in schizophrenia patients CSF, brain and peripheral tissues.

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