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PMID: 18388328 As a constituent of plasma lipopoproteins, apoE directs movement of lipids from the periphery to the liver, where high affinity binding of apoE to the LDL receptor and other members of the LDL-receptor family facilitates uptake of the lipoprotein particles. PMID: 18388328, 10357834, 9541497 Cell surface apoE can also be bound to lipoprotein receptors, such that antiserum to the LDL receptor (LDLr) and suramin (which blocks ligand binding to the LDL-receptor related protein LRP) can reduce sequestration on the macrophage surface and increase apoE secretion.

Indirect

PMID: 18388328 As a constituent of plasma lipopoproteins, apoE directs movement of lipids from the periphery to the liver, where high affinity binding of apoE to the LDL receptor and other members of the LDL-receptor family facilitates uptake of the lipoprotein particles.

Indirect

PMID: 18388328 Transcription of macrophage apoE can be induced by differentiation, exposure to cytokines, hormones, and lipids such as cholesterol or oxysterols.

Indirect

PMID: 18388328 Transcription of macrophage apoE can be induced by differentiation, exposure to cytokines, hormones, and lipids such as cholesterol or oxysterols.

Indirect

PMID: 18388328 Transcription of macrophage apoE can be induced by differentiation, exposure to cytokines, hormones, and lipids such as cholesterol or oxysterols.

Indirect

PMID: 18388328 Transcription of macrophage apoE can be induced by differentiation, exposure to cytokines, hormones, and lipids such as cholesterol or oxysterols.

Indirect

Indirect

PMID: 18388328 The LXR/RXR heterodimer regulates apoE transcription in response to lipids through interaction with conserved LXR response elements in the multienhancer regions. PMID: 18388328, 17553793, 16601234, 11149950, 11439103 Transcription factors involved in the direct transcriptional regulation of apoE in macrophages included: AP-1, NF-kappaB LXR and PPARgamma.

PMID: 18388328 The LXR/RXR heterodimer regulates apoE transcription in response to lipids through interaction with conserved LXR response elements in the multienhancer regions.

PMID: 18388328, 11439103 Regulation of apoE transcription by PPARgamma is mediated via a PPRE element present in the intergenic region between the apoE and apoC1 genes, which is also well outside the proximal promoter.

Indirect

PMID: 18388328, 11439103 Regulation of apoE transcription by PPARgamma is mediated via a PPRE element present in the intergenic region between the apoE and apoC1 genes, which is also well outside the proximal promoter. PMID: 18388328, 17553793, 16601234, 11149950, 11439103 Transcription factors involved in the direct transcriptional regulation of apoE in macrophages included: AP-1, NF-kappaB LXR and PPARgamma.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter. PMID: 18388328, 17553793, 16601234, 11149950, 11439103 Transcription factors involved in the direct transcriptional regulation of apoE in macrophages included: AP-1, NF-kappaB LXR and PPARgamma.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter. PMID: 18388328, 17553793, 16601234, 11149950, 11439103 Transcription factors involved in the direct transcriptional regulation of apoE in macrophages included: AP-1, NF-kappaB LXR and PPARgamma.

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

PMID: 18388328, 17553793, 16601234 Other modulators of macrophage apoE transcription have been described, including transforming growth factor (TGF)-beta which stimulates apoE expression by promoting binding of c-Jun to AP-1 and lipopolysaccharide (LPS), which represses apoE gene expression via both Tpl-2 and MEKK1 signaling pathways, leading to c-Jun and NF-kappaB action on distinct regions in the proximal promoter.

Indirect

PMID: 18388328 Secretion via tubular and vesicular transport from the Golgi (G), after transport to the Golgi from the endoplasmic reticulum (ER). PMID: 18388328, 6325438 ApoE is synthesized as a 38 500 Mr protein designated preapoE, containing a NH2-terminal 18-AA extension23 which mediates entry into the ER.

PMID: 18388328 Secretion via tubular and vesicular transport from the Golgi (G), after transport to the Golgi from the endoplasmic reticulum (ER). PMID: 18388328, 6286633, 2498325 After cleavage of the signal peptide in the ER, the protein is trafficked to the Golgi, where apoE is O-glycosylated on threonine 194 and extensively sialylated. PMID: 18388328, 8576639 Brefeldin A, which perturbs ER to Golgi transport, inhibits apoE degradation and causes intracellular accumulation of unglycosylated apoE with lower molecular weight.

PMID: 18388328 Secretion via recycling endosomes (RE). PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE.

Indirect

PMID: 18388328 Secretion via recycling endosomes (RE). PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE. PMID: 18388328 Secretion of apoE (or displacement of cell surface apoE), releases apoE into extracellular medium. PMID: 18388328, 10671508 Cell surface pools may be reinternalized and subsequently degraded (Figure 1, pathways 3 and 4), or transported to the Golgi network for further modification22 (Figure 1, pathways 3 and 5), or released into the extracellular medium (Figure 1, pathway 3, 2, and 6). PMID: 18388328, 8662812 Increased secretion when proteoglycan synthesis is inhibited suggests that cell surface binding can sequester apoE and inhibit its secretion. PMID: 18388328, 10357834, 9541497 Cell surface apoE can also be bound to lipoprotein receptors, such that antiserum to the LDL receptor (LDLr) and suramin (which blocks ligand binding to the LDL-receptor related protein LRP) can reduce sequestration on the macrophage surface and increase apoE secretion.

PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE. PMID: 18388328 Poorly glycosylated apoE on cell surface can reenter the Golgi compartment to be further glycosylated, presumably via EE and then LE. PMID: 18388328, 10671508 Cell surface pools may be reinternalized and subsequently degraded (Figure 1, pathways 3 and 4), or transported to the Golgi network for further modification22 (Figure 1, pathways 3 and 5), or released into the extracellular medium (Figure 1, pathway 3, 2, and 6).

PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE. PMID: 18388328 Poorly glycosylated apoE on cell surface can reenter the Golgi compartment to be further glycosylated, presumably via EE and then LE.

PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE.

PMID: 18388328 Recycling of secreted apoE into early endosomes (EE), and thereafter degraded in lysosomes or proteasomes (Lys/P), transported to Golgi, or secreted via RE. PMID: 18388328, 10671508 Cell surface pools may be reinternalized and subsequently degraded (Figure 1, pathways 3 and 4), or transported to the Golgi network for further modification22 (Figure 1, pathways 3 and 5), or released into the extracellular medium (Figure 1, pathway 3, 2, and 6).

PMID: 18388328 Degradation of apoE in lysosomes or proteasomes (Lys/P), probably via late endosomes (LE). PMID: 18388328, 8576639 Brefeldin A, which perturbs ER to Golgi transport, inhibits apoE degradation and causes intracellular accumulation of unglycosylated apoE with lower molecular weight. PMID: 18388328, 8473293, 9388269 Degradation of apoE is inhibited by ALLN, an inhibitor of Ca2+ dependent proteases, in HepG2 cells, macrophages, and CHO cells expressing apoE. PMID: 18388328, 8576639 Concentrations of the lysosomal inhibitor chloroquine, which effectively inhibited apoE degradation (25 to 100 µmol/L), did not stimulate apoE secretion. PMID: 18388328, 15066991, 2072040, 1730636 However, as a number of studies have shown that stimulation of apoE secretion by HDL and apoA-I decreases net degradation of apoE, it is likely that there are other "uncommitted" pools of apoE otherwise destined for degradation which can be redirected to secretion. PMID: 18388328, 15066991 ApoA-I stimulates secretion and decreases degradation of Em without affecting Es.

Indirect

PMID: 18388328 Poorly glycosylated apoE on cell surface can reenter the Golgi compartment to be further glycosylated, presumably via EE and then LE. PMID: 18388328, 9488694, 8662812 As well as being released into the extracellular medium, a proportion of secreted apoE can be found bound to the cell surface (Figure 1, pathway 7), particularly in association with heparan sulfate proteoglycans. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 15066991 ApoA-I stimulates secretion and decreases degradation of Em without affecting Es. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328 As H89 is less effective at inhibiting apoA-I–induced apoE secretion than it is at inhibiting constitutive apoE secretion, a second, PKA-independent route of secretion of Em2 is also proposed. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

PMID: 18388328, 6286633, 2498325 After cleavage of the signal peptide in the ER, the protein is trafficked to the Golgi, where apoE is O-glycosylated on threonine 194 and extensively sialylated.

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xmlns:xlink="http://www.w3.org/1999/xlink" id="XMLID_45_" gradientUnits="userSpaceOnUse" gradientTransform="matrix(1 0 0 -1 0.1128 -116.7979)" x1="180.9333" y1="-116.7979" x2="180.9333" y2="-478.8857"><stop style="stop-color:#FFFFFF" offset="0"></stop><stop style="stop-color:#FFF8ED" offset="0.0424"></stop><stop style="stop-color:#FDE2B2" offset="0.1921"></stop><stop style="stop-color:#FCCF7F" offset="0.3414"></stop><stop style="stop-color:#FBC055" offset="0.4869"></stop><stop style="stop-color:#FAB435" offset="0.6279"></stop><stop style="stop-color:#F9AB1E" offset="0.7631"></stop><stop style="stop-color:#F9A610" offset="0.8898"></stop><stop style="stop-color:#F9A40B" offset="1"></stop></linearGradient><radialGradient xmlns:xlink="http://www.w3.org/1999/xlink" id="XMLID_46_" gradientUnits="userSpaceOnUse" gradientTransform="matrix(1 0 0 -1 0.0376 362.0234)" cx="194.7375" cy="177.3496" r="75.7176"><stop style="stop-color:#5EA3CC" offset="0"></stop><stop style="stop-color:#4B007D" offset="1"></stop></radialGradient></defs></svg> PMID: 18388328, 6286633, 2498325 After cleavage of the signal peptide in the ER, the protein is trafficked to the Golgi, where apoE is O-glycosylated on threonine 194 and extensively sialylated.

PMID: 18388328, 9488694, 8662812 As well as being released into the extracellular medium, a proportion of secreted apoE can be found bound to the cell surface (Figure 1, pathway 7), particularly in association with heparan sulfate proteoglycans.

PMID: 18388328, 15131109 These posttranslational modifications of apoE do not appear to affect receptor binding or lipoprotein clearance but may determine the preferential association with high density lipoprotein (HDL) particles.

Indirect

PMID: 18388328 Poorly glycosylated apoE on cell surface can reenter the Golgi compartment to be further glycosylated, presumably via EE and then LE. PMID: 18388328, 9488694, 8662812 As well as being released into the extracellular medium, a proportion of secreted apoE can be found bound to the cell surface (Figure 1, pathway 7), particularly in association with heparan sulfate proteoglycans. PMID: 18388328, 15131109 This is supported by other studies showing that oleic acid stimulates secretion of macrophage apoE while apparently reducing its sialylation. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328 As H89 is less effective at inhibiting apoA-I–induced apoE secretion than it is at inhibiting constitutive apoE secretion, a second, PKA-independent route of secretion of Em2 is also proposed. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328 Poorly glycosylated apoE on cell surface can reenter the Golgi compartment to be further glycosylated, presumably via EE and then LE. PMID: 18388328, 9488694, 8662812 As well as being released into the extracellular medium, a proportion of secreted apoE can be found bound to the cell surface (Figure 1, pathway 7), particularly in association with heparan sulfate proteoglycans. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 15066991, 2072040, 1730636 However, as a number of studies have shown that stimulation of apoE secretion by HDL and apoA-I decreases net degradation of apoE, it is likely that there are other "uncommitted" pools of apoE otherwise destined for degradation which can be redirected to secretion. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328 As H89 is less effective at inhibiting apoA-I–induced apoE secretion than it is at inhibiting constitutive apoE secretion, a second, PKA-independent route of secretion of Em2 is also proposed. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 11149950, 3624230, 1466652 As distinct from factors that increase apoE secretion by stimulating its synthesis (eg, LXR/RXR ligands, cholesterol enrichment, cytokines, a number of agents have been shown to directly increase apoE secretion (independent of transcription). PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 11149950, 3624230, 1466652 As distinct from factors that increase apoE secretion by stimulating its synthesis (eg, LXR/RXR ligands, cholesterol enrichment, cytokines, a number of agents have been shown to directly increase apoE secretion (independent of transcription). PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 11149950, 3624230, 1466652 As distinct from factors that increase apoE secretion by stimulating its synthesis (eg, LXR/RXR ligands, cholesterol enrichment, cytokines, a number of agents have been shown to directly increase apoE secretion (independent of transcription). PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 9388269, 1400506 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 15066991, 17303773, 9869653 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 15066991 Stimulation of apoE secretion is a general property of {alpha}-helix containing molecules including apoA-II, A-IV, and apoE. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 15066991, 17303773, 9869653 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 15066991 Stimulation of apoE secretion is a general property of {alpha}-helix containing molecules including apoA-II, A-IV, and apoE. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 15066991, 17303773, 9869653 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 15066991 Stimulation of apoE secretion is a general property of {alpha}-helix containing molecules including apoA-II, A-IV, and apoE. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 9488694, 8662812, 10671508 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 9488694, 8662812, 10671508 These include, LDL,HDL,apoA-I, A-II, A-IV, apoE,phospholipid vesicles (PLV), heparinase, oleic acid, and lactoferrin. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.

Indirect

PMID: 18388328, 15066991, 10441097 Exogenous apoE4 is less effective at stimulating apoE3 secretion from macrophages than are apoE3 and apoE2, which may be relevant for the increased atherosclerotic risk associated with the apoE4 phenotype.

Indirect

PMID: 18388328, 15066991, 10441097 Exogenous apoE4 is less effective at stimulating apoE3 secretion from macrophages than are apoE3 and apoE2, which may be relevant for the increased atherosclerotic risk associated with the apoE4 phenotype.

Indirect

PMID: 18388328, 15066991, 10441097 Exogenous apoE4 is less effective at stimulating apoE3 secretion from macrophages than are apoE3 and apoE2, which may be relevant for the increased atherosclerotic risk associated with the apoE4 phenotype.

Indirect

PMID: 18388328, 15066991, 6823554 Although the pathways stimulating apoE secretion and cholesterol efflux are distinct, apoE, whether added to cells or during its secretion from cells, can itself mediate cholesterol efflux.

Indirect

Indirect

PMID: 18388328, 16254198 There is evidence to suggest that exogenous apoE removes cholesterol via an ABCA1-mediated pathway, whereas secreted apoE may also remove cholesterol in an ABCA1-independent manner.

Indirect

PMID: 18388328, 15066991 Additionally, a range of synthetic alpha-helical peptides which stimulated apoE secretion to an extent similar to intact apoA-I were incapable of stimulating cholesterol efflux. PMID: 18388328, 8576639, 6823554 Monensin and brefeldin A inhibit endogenous apoE secretion, but fail to affect recycling of I-apoE-VLDL delivered to CHO cells, supporting the existence of different secretory pathways for endogenous and recycled apoE. PMID: 18388328, 17660382 The PKA inhibitor H89 inhibits secretion of apoE without increasing degradation and increases the stable pool Es. PMID: 18388328, 17660382 As inhibitors of phospholipase C (PLC) and the inositol triphosphate (IP3) receptor (IP3R) also decreased secretion of apoE, a role for PLC and IP3R in the mobilization of [Ca2+]i during secretion of apoE is most likely.