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Apolipoprotein L, 3

apoL-III, CG12_1, CG12-1
This gene is a member of the apolipoprotein L gene family, and it is present in a cluster with other family members on chromosome 6. The encoded protein is found in the cytoplasm, where it may affect the movement of lipids, including cholesterol, and/or allow the binding of lipids to organelles. In addition, expression of this gene is up-regulated by tumor necrosis factor-alpha in endothelial cells lining the normal and atherosclerotic iliac artery and aorta. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2009] (from NCBI)
Top mentioned proteins: apolipoprotein L-I, ACID, APOL3, apoL-IV, Rabkinesin-6
Papers on apoL-III
Family-based association analysis of 42 hereditary prostate cancer families identifies the Apolipoprotein L3 region on chromosome 22q12 as a risk locus.
Ostrander et al., Bethesda, United States. In Hum Mol Genet, 2010
An association between an single nucleotide polymorphisms within the APOL3 locus and prostate cancer risk, is revealed.
The apolipoprotein L gene cluster has emerged recently in evolution and is expressed in human vascular tissue.
Horrevoets et al., Amsterdam, Netherlands. In Genomics, 2002
APOL3 has been found only in humans and African green monkeys
Apolipoprotein L gene family: tissue-specific expression, splicing, promoter regions; discovery of a new gene.
Kane et al., San Francisco, United States. In J Lipid Res, 2001
The genes for all four proteins, apoL-I, apoL-II, apoL-III, and apoL-IV, are located at chromosome 22q12.1-13.1 within a 127,000-bp region.
Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes.
Pannekoek et al., Amsterdam, Netherlands. In Blood, 1999
These novel human cDNAs CA2_1, CG12_1, GG10_2, AG8_1, and GG2_1 encode inhibitor of apoptosis protein-1 (hIAP-1), homologues of apolipoprotein-L, mouse rabkinesin-6, rat stannin, and a novel 188 amino acid protein, respectively.
Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces.
Ryan et al., Edmonton, Canada. In J Biol Chem, 1998
These data provide insight into the spatial topography of apoLp-III alpha-helices in phospholipid disc complexes and support the concept that interaction with spherical lipoprotein particles results in superficial contact of apoL-III helical segments with the monolayer surface, providing a basis for its reversible binding ability.
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