Search results for APOA5

Showing 14 results out of 14

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Species

Types

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Reaction types

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Protein (4 results from a total of 4)

Identifier: R-HSA-8956716
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: APOA5: Q6Q788
Identifier: R-HSA-174608
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: APOA5: Q6Q788
Identifier: R-HSA-6784664
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q6Q788
Identifier: R-HSA-8956979
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q6Q788

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5649925
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000110243

Reaction (5 results from a total of 5)

Identifier: R-HSA-1989761
Species: Homo sapiens
Compartment: nucleoplasm, extracellular region
The APOA5 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Identifier: R-HSA-6784622
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
Crebh(1-?) enters the nucleoplasm and induces the expression of APOA4, APOA5, APOC2, CIDEC and FGF21 (Lee et al. 2011). APOA4, APOA5 and APOC2 are known to augment lipoprotein lipase (LPL) activity. LPL is bound to the vascular endothelium, and hydrolyzes chylomicron and VLDL- associated TG to facilitate the transport of hydrolyzed fatty acids to peripheral cells. Patients with genetic defects in AOPC2, APOA5 or LPL display high circulating TG levels due to impaired TG clearance. Identification of APOA4, APOA5 and APOC2 as CREB-H target genes suggests that CREB-H might be involved in TG catabolism. CREB-H also strongly induces FGF21, a liver expressed hormone that has antidiabetic and TG- lowering effects, and CIDEC which encodes a lipid droplet-associated protein (Lee 2012).
Identifier: R-HSA-2395768
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Lipoprotein lipase dimers (LPL:LPL) are tethered to heparan sulfate proteoglycans (HSPG) at endothelial cell surfaces (Fernandez-Borja et al. 1996; Peterson et al. 1992). Both syndecan 1 (Rosenberg et al. 1997) and perlecan (Goldberg 1996) HSPG molecules are capable of tethering LPL. The LPL enzyme catalyzes the hydrolysis and release of triacylglycerols (TG) associated with circulating chylomicrons to leave a CM remnant (CR). This reaction is annotated here as causing the hydrolysis and release of 50 molecules of TG. In vivo, the number is much larger, and TG depletion probably occurs in the course of multiple encounters between a chylomicron and endothelial LPL. This reaction is strongly activated by chylomicron-associated apo C-II protein both in vivo and in vitro (Jackson et al. 1986). Chylomicron-associated apoC-II protein inhibits LPL activity in vitro (Brown and Baginsky 1972), and recent studies have indicated a positive regulatory role for apoA-5 protein, though its molecular mechanism of action remains unclear (Marcais et al. 2005; Merkel and Heeren 2005). CRs can then be taken up by liver parenchymal cells in two ways; 1) directly by the LDL receptor or 2) apoE/HSPG-directed uptake by LDL receptor-related proteins.
Identifier: R-HSA-174757
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Lipoprotein lipase dimers (LPL:LPL) are tethered to heparan sulfate proteoglycans (HSPG) at endothelial cell surfaces (Fernandez-Borja et al. 1996; Peterson et al. 1992). Both syndecan 1 (Rosenberg et al. 1997) and perlecan (Goldberg 1996) HSPG molecules are capable of tethering LPL. The LPL enzyme catalyzes the hydrolysis and release of triacylglycerols (TG) associated with circulating chylomicrons to leave a CM remnant (CR). This reaction is annotated here as causing the hydrolysis and release of 50 molecules of TG. In vivo, the number is much larger, and TG depletion probably occurs in the course of multiple encounters between a chylomicron and endothelial LPL. This reaction is strongly activated by chylomicron-associated apo C-II protein both in vivo and in vitro (Jackson et al. 1986). Chylomicron-associated apoC-II protein inhibits LPL activity in vitro (Brown and Baginsky 1972), and recent studies have indicated a positive regulatory role for apoA-5 protein, though its molecular mechanism of action remains unclear (Marcais et al. 2005; Merkel and Heeren 2005). CRs can then be taken up by liver parenchymal cells in two ways; 1) directly by the LDL receptor or 2) apoE/HSPG-directed uptake by LDL receptor-related proteins.
Identifier: R-HSA-6784648
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
The N-terminal fragment of CREB3L3 is released to the cytosol and translocates to the nucleus (Chan et al. 2010, Chin et al. 2005) to induce the transcriptional activation of different genes such as Apoa4, Apoa5, and Apoc2 apolipoproteins which exhibit stimulatory effects on lipoprotein lipase (LPL). Consistent with the essential role of LPL in TG clearance, CREB3L3-deficient mice showed hypertriglyceridemia, associated with defective production of these apolipoproteins and decreased LPL activity.

Set (2 results from a total of 2)

Identifier: R-HSA-6784718
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6784668
Species: Homo sapiens
Compartment: nucleoplasm

Pathway (2 results from a total of 2)

Identifier: R-HSA-8963889
Species: Homo sapiens
Lipoprotein lipase (LPL) and hepatic triacylglycerol lipase (LIPC) enzymes on the lumenal surfaces of capillary endothelia mediate the hydrolysis of triglyceride molecules in circulating lipoprotein particles.
LPL is widely expressed in the body and is especially abundant in adipocytes and skeletal and cardiac myocytes. Activation of the protein requires glycosylation, dimerization, and glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1), which delivers it to heparan sulfate proteoglycan (HSPG) associated with the plasma membrane. It is inactivated by proteolytic cleavage (Berryman & Bensadoun 1995; Sukonina et al. 2006; Young et al. 2011).
Expression of the LPL gene is transcriptionally regulated by Cyclic AMP-responsive element-binding protein 3-like protein 3 (CREB3L3), which also regulates the expression of APOA4, APOA5, APOC2, CIDEC and FGF21 (Lee et al. 2011).
Maturation of LIPC enzyme requires association with LMF1 protein (or possibly, inferred from sequence similarity, LMF2). Heparin binding stabilizes LIPC in its active dimeric form (Babilonia-Rosa & Neher 2014; Ben-Zeev et al. 2011).
Identifier: R-HSA-1989781
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane, extracellular region, lipid droplet, mitochondrial inner membrane, mitochondrial matrix, mitochondrial outer membrane, nucleoplasm, peroxisomal matrix, peroxisomal membrane, plasma membrane
The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include:
1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2);
2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2);
3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1);
4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5);
5) genes involved in triglyceride clearance ( Angptl4);
6) genes involved in glycerol metabolism (Gpd1 in mouse);
7) genes involved in glucose metabolism (Pdk4);
8) genes involved in peroxisome proliferation (Pex11a);
9) genes involved in lipid storage (Plin, Adfp).
Many other genes are known to be regulated by PPAR-alpha but whether their regulation is direct or indirect remains to be found. These genes include: ACACA, FAS, SREBP1, FADS1, DGAT1, ABCA1, PLTP, ABCB4, UGT2B4, SULT2A1, Pnpla2, Acsl1, Slc27a4, many Acot genes, and others (reviewed in Rakhshandehroo et al. 2010).
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