Alternative titles; symbols
HGNC Approved Gene Symbol: APOF
Cytogenetic location: 12q13.3 Genomic coordinates (GRCh38): 12:56,360,568-56,362,857 (from NCBI)
Apolipoprotein F is predominantly associated with low density lipoprotein and functions as an inhibitory regulator of cholesteryl ester transfer protein (CETP; 118470) (Wang et al., 1999).
Apolipoprotein F, a minor apolipoprotein in human plasma, was isolated and partially characterized by Olofsson et al. (1978).
By PCR of a human hepatoma cell line cDNA library using primers based on the N-terminal sequence of purified APOF, Day et al. (1994) cloned full-length APOF. The deduced 308-amino acid proprotein has a 22-amino acid N-terminal signal peptide, and its C-terminal half contains the mature APOF peptide, which is released by proteolytic processing. The mature 162-amino acid hydrophobic APOF peptide has a calculated molecular mass of 17.4 kD and contains sites for N- and O-glycosylation. Northern blot analysis detected a 2.0-kb transcript in human liver only.
Using Western blot analysis, Wang et al. (1999) detected endogenous APOF in human plasma at an apparent molecular mass of 33 kD.
Koren et al. (1982) studied the interaction of apoF with other apolipoproteins and lipids in human plasma. They suggested that apoF-containing lipoproteins may be involved in transport and/or esterification of cholesterol.
Wang et al. (1999) found that recombinant APOF secreted from transfected COS-7 cells suppressed transfer of triglyceride and cholesteryl ester by CETP in a dose-dependent manner. They suggested that APOF is a regulator of cholesterol transport between plasma lipoproteins that affects the sterol content of individual lipoprotein fractions.
By somatic cell hybrid analysis, Day et al. (1994) mapped the APOF gene to chromosome 12.
Gross (2013) mapped the APOF gene to chromosome 12q13.3 based on an alignment of the APOF sequence (GenBank BC026257) with the genomic sequence (GRCh37).
Day, J. R., Albers, J. J., Gilbert, T. L., Whitmore, T. E., McConathy, W. J., Wolfbauer, G. Purification and molecular cloning of human apolipoprotein F. Biochem. Biophys. Res. Commun. 203: 1146-1151, 1994. [PubMed: 8093033] [Full Text: https://doi.org/10.1006/bbrc.1994.2302]
Gross, M. B. Personal Communication. Baltimore, Md. 12/3/2013.
Koren, E., McConathy, W. J., Alaupovic, P. Isolation and characterization of simple and complex lipoproteins containing apolipoprotein F from human plasma. Biochemistry 21: 5347-5351, 1982. [PubMed: 6816269] [Full Text: https://doi.org/10.1021/bi00264a035]
Olofsson, S.-O., McConathy, W. J., Alaupovic, P. Isolation and partial characterization of a new acidic apolipoprotein (apolipoprotein F) from high density lipoproteins of human plasma. Biochemistry 17: 1032-1036, 1978. [PubMed: 204339] [Full Text: https://doi.org/10.1021/bi00599a014]
Wang, X., Driscoll, D. M., Morton, R. E. Molecular cloning and expression of lipid transfer inhibitor protein reveals its identity with apolipoprotein F. J. Biol. Chem. 274: 1814-1820, 1999. [PubMed: 9880564] [Full Text: https://doi.org/10.1074/jbc.274.3.1814]