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Human ANGPTL4 Protein expressed in Wheat germ - ABIN1345057
Basak, Duttaroy: cis-9,trans-11 conjugated linoleic acid stimulates expression of angiopoietin like-4 in the placental extravillous trophoblast cells. in Biochimica et biophysica acta 2013
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Recently two proteins, angiopoietin-like protein 3 and 4, have emerged from genetic studies as being factors that significantly modulate plasma triglyceride levels and coronary artery disease. ..Here we report the crystal structures of the fibrinogen-like domains of both proteins. These structures offer new insights into the reported loss of function mutations
G allele at the rs116843064 polymorphic locus of the ANGPTL4 gene was associated with a lower prevalence of metabolic syndrome (MetS).
valuable insights into the relationship between ANGPTL4 and LPL in human adipose tissue
Data suggest that angiopoietin like-4 (ANGPTL4) contributes to pathological vascular remodelling in capillary cerebral amyloid angiopathy and that detection of ANGPTL4 levels may improve current diagnostics.
Molecular mechanisms by which ANGPTL4 functions in eye diseases, such as diabetic retinopathy, age-related macular degeneration and uveal melanoma.[review]
ANGPTL4 is uniquely induced by hypoxia in cultured SGC cells and is essential for tumour growth and resistance to anoikis through different mechanisms.
Gastric antral vascular ectasia in liver cirrhosis is associated with increased expression of miR-3667 maybe linked with ANGPTL4 gene.
Adipocyte-derived ANGPTL4 drives disease progression under obese conditions and is a potential therapeutic target for treating obese breast cancer patients.
the action of PVT1 is moderately attributable to its repression of ANGPTL4 via association with the epigenetic repressor Ezh2.
Taken together, our data suggest that serum ANGPTL3 and 4 levels are influenced by nutritional status and fasting and could be involved in the metabolic disturbances present in obesity and anorexia nervosa.
ANGPTL4 was immunohistochemically detectable in 76 out of 109 osteosarcoma cases. ANGPTL4 was induced by hypoxia in 6 osteosarcoma cell lines, under the control of the HIF-1alpha transcription factor.
Carriers of p.E40K, a variant that abolishes ANGPTL4 ability to inhibit lipoprotein lipase, have lower odds of T2D (odds ratio 0.89, 95% confidence interval 0.85-0.92, p = 6.3 x 10(-10)), lower fasting glucose, and greater insulin sensitivity.
A relevant role of ANGPTL-4 in human obesity and its involvement in long-term body weight changes.
Data indicate that the angiopoietin-like protein 4 (ANGPTL4)-mediated upregulation of tristetraprolin expression regulates the stability of chemokines in human colon epithelial cells.
The data suggest that exercise-induced ANGPTL4 is secreted from the liver and driven by a glucagon-cAMP-PKA pathway in humans. These findings link the liver, insulin/glucagon, and lipid metabolism together.
Study data support dual roles for ANGPTL4 in urothelial carcinoma progression, either as a tumor suppressor or oncogene, in response to microenvironmental context.
ANGPTL4 levels are increased in both plasma and adipose tissues of subjects with hypertension.
Low ANGPTL4 expression is associated with childhood obesity.
SNP rs11672433, a high-frequency locus in the ANGPTL4 gene, does not influence the predisposition to brain arteriovenous malformation or its effect is too small to be detected in the present size sample set.
Levels of ANGPTL4 in the circulation and HDLs were increased in type 2 diabetics altering lipid metabolism.
Adipose Tissue ANGPTL4 in regulating peripheral lipid deposition, influencing whole-body lipid and glucose metabolism and the progression of atherosclerosis.
GPIHBP1-independent pathway for clearance of plasma TGs in Angptl4(-/-)Gpihbp1(-/-) mice
BAT specific deletion of ANGPTL4 results in enhanced lipoprotein lipase activity, circulating triglyceride clearance and thermogenesis. Absence of ANGPTL4 in BAT increased fatty acid oxidation and reduced fatty acid synthesis.
ANGPTL4 promotes PCSK-mediated intracellular cleavage of LPL in adipocytes, likely contributing to regulation of LPL in adipose tissue.The data provide further support for an intracellular action of ANGPTL4 in adipocytes.
inactivation of ANGPTL4 improves glucose tolerance, at least partly via a gut microbiota-dependent mechanism
miR-134 accelerates atherogenesis by promoting lipid accumulation and proinflammatory cytokine secretion via the ANGPTL4/LPL pathway
Functional studies in Angptl4-deficient mice confirm improved insulin sensitivity and glucose homeostasis.
Data show that angiopoietin-like protein 4 (ANGPTL4)deficiency in mice knockout (ANGPTL4(-/-)) exacerbated colonic inflammation induced by dextran sulfate sodium (DSS) or stearic acid.
Angptl4 is induced early in fasting to divert uptake of fatty acids and triglycerides away from adipose tissues.
haematopoietic ANGPTL4 deficiency increases atherogenesis through regulating myeloid progenitor cell expansion and differentiation, foam cell formation and vascular inflammation.
Following ANGPTL4 downregulation, the proliferation and invasion abilities of gastric cancer (GC)cell lines were suppressed as determined by MTT and Transwell assays, and cell apoptosis level and sensitivity to cisplatin were increased as determined by flow cytometry and MTT assay. In conclusion, these findings suggest that ANGPTL4 may be a new potential therapeutic target for GC
The influence of H2O2 on ANGPTL4 provided new insight into the mechanism of atherosclerosis.
The reduction of plasma triglyceride levels in Angptl4(-/-) mice and increase following Angptl4 overexpression suggest that changes in plasma triglyceride metabolism do not regulate alpha-cells in the pancreas. Our findings corroborate recent data showing that increased plasma amino acids and their transport into alpha-cells link glucagon receptor blockage to alpha-cell hyperplasia
study demonstrates the key role of Angptl4 in glucocorticoid-augmented hepatic ceramide production that induces whole-body insulin resistance.
1) ANGPTL4 is not involved in the triglyceride-lowering effect ofbile acids ; 2) ANGPTL4 promotes bile acids absorption during taurocholic acid supplementation via a mechanism dependent on the gut microbiota.
physiological changes in adipose tissue ANGPTL4 expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4(-/-) mice. We conclude that ANGPTL4 promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the endoplasmic reticulum (ER).
This study shows that TNF-alpha, by a Foxo1 dependent pathway, increases the transcription of ANGPTL4 which is secreted by the cells and causes inactivation of LPL.
Angptl4-deficient mice show impaired insulin secretion and dysmorphic pancreatic islets.
Angptl4 induces obesity-associated metabolic disorders. The present study suggested that Angptl4 promotes liver steatosis and lipolysis, in addition to impairing liver function; while Angptl4 improves glucose tolerance and insulin resistance, in addition to causing the downregulation of various insulin signaling pathway-associated genes.
The ANGPTL4 G/A polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) showed a significant effect on intramuscular fat
increase in angiopoietin-like protein 4 messenger RNA across multiple models of altered energy balance identifies it as an adipokine that is uniquely responsive to changes in energy balance in the lactating dairy cow
These findings indicate that liver and adipose tissue are key sources of ANGPTL4 in cattle; the protein was also highly abundant in ruminal epithelium, making it possible that commensal microbes may influence ANGPTL4 synthesis and secretion.
These results suggest that the microbiota might regulate host intestinal Angptl4 protein expression and peripheral fat storage by suppressing the activity of an intestine-specific transcriptional enhancer.
This gene is a member of the angiopoietin/angiopoietin-like gene family and encodes a glycosylated, secreted protein with a fibrinogen C-terminal domain. This gene is induced under hypoxic conditions in endothelial cells and is the target of peroxisome proliferation activators. The encoded protein is a serum hormone directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity and also acts as an apoptosis survival factor for vascular endothelial cells. The encoded protein may play a role in several cancers and it also has been shown to prevent the metastatic process by inhibiting vascular activity as well as tumor cell motility and invasiveness. Decreased expression of this protein has been associated with type 2 diabetes. Alternatively spliced transcript variants encoding different isoforms have been described. This gene was previously referred to as ANGPTL2 but has been renamed ANGPTL4.
PPARG angiopoietin related protein
, angiopoietin-like protein 4
, angiopoietin-related protein 4
, fasting-induced adipose factor
, hepatic angiopoietin-related protein
, hepatic fibrinogen/angiopoietin-related protein
, peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin-related protein
, fibrinogen/angiopoietin-related protein
, major histocompatibility complex region NG27
, secreted protein Bk89
, PPARG angiopoietin-related protein
, angiopoietin-like 4
, angiopoietin-like secreted glycoprotein 4
, angiopoietin-related protein 4-like
, angiopoietin-like 4 protein