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Apolipoprotein C1 (ApoC1) is a component of very-low-density lipoproteins (VLDLs), intermediate classes,and high-density lipoproteins (HDLs). It has severalpotential functions. It helps to maintain HDL structureand activates plasma lysolecithin acyltransferase. It isalso able to modulate the interaction of apolipoproteinE with b-migrating VLDLs and inhibit binding ofb-VLDL to low-density lipoprotein receptor-relatedprotein [1,2]. It is implicated in regulation of severallipase enzymes [3–5]. An N-terminal 38-residue form ofApoC1 is able to inhibit cholesterol ester transferase[6]. ApoC1 accounts for inhibition of cholesterol estertransferase by HDL [7]. Thus, ApoC1 has a number ofpotential functions that may be important in vivo.Known variants of the ApoC1 gene are limited to un-translated regions of the gene, synonymous mutationsof the coding sequence and a number of variants of theintron regions of the gene (NCBI database for ApoC1).An important functional variant is found in the promo-ter region where complex factors [8,9] may link ApoC1expression levels to familial dysbetalipoprotemia, car-diovascular disease, and Alzheimer’s disease [10–12].Overexpression of human ApoC1 in the mouse produ-ces a hyperlipidemic condition [4,13] with possiblebeneficial effects for diabetes [14,15]. Hyperlipidemiamay result from increased inhibition of b-VLDL bind-ing to the receptor and reduced clearance of VLDLsfrom the circulation. Variants of ApoC2 and ApoC3have been linked to metabolic disease [16–18]. Thisstudy reports the first case of a structural variant ofApoC1 as well as some protein properties that suggestthe functional significance of this residue change. They |
