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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. dans Biochimica et biophysica acta 2013
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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.
High expression of ANGPTL4 is associated with drug resistance in prostate cancer.
circulating ANGPTL3 and ANGPTL 4 expression was significantly elevated in hepatocellular carcinoma cases compared to chronic hepatitis patients and controls
this study suggests that the presence of C allele of rs1044250 and G allele of rs2278236 in ANGPTL4 gene is associated with higher risk of moderate/severe proteinuria in renal transplant patients
These results suggested that ANGPTL4 was essential for proliferation and metastasis of lung cancer cells.
The mutant tumors exhibited impaired proliferation, anoikis resistance, and migratory capability and had reduced adenylate energy charge. Further investigations also revealed that cANGPTL4 regulated the expression of Glut2
Data indicate angiopoietin-like 4 (ANGPTL4) as a key player that coordinates an increase in cellular energy flux crucial for EMT via an ANGPTL4/14-3-3gamma signaling axis.
The authors now show: (1) that ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 renders LPL largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 are required for this protective effect.
One of the variants, rs116843064, is a damaging missense variant within the ANGPTL4 gene.
reduced expression of one of the survival-associated transcripts, Angiopoietin-like 4, impairs growth of a gemcitabine-resistant pancreatic cancer cell line.
Serum ANGPTL4 is elevated in coronary artery disease, but levels do not reflect severity of disease.
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.
ANGPTL4 is part of a shuttling mechanism that directs fatty acids derived from circulating triglyceride-rich lipoproteins to brown adipose tissue during cold.
This model suggests a general mechanism by which TAG trafficking is coordinated by lipasin, Angptl3 and Angptl4 at different nutritional statuses.
These results reveal that FTO regulates fatty acid mobilization in adipocytes and thus body weight in part through posttranscriptional regulation of Angptl4.
these results suggest that IL-1beta increases Angptl4 expression through a mechanism dependent on the JNK-MAPK signaling pathway in MC3T3-E1 cells.
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