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- Table of Contents
1 Citations 5 Q&As
2 Citations 9 Q&As
3 Citations 7 Q&As
Facts about Fatty acid-binding protein, adipocyte.
Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. .
Human | |
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Gene Name: | FABP4 |
Uniprot: | P15090 |
Entrez: | 2167 |
Belongs to: |
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calycin superfamily |
Adipocyte lipid-binding protein; Adipocyte-type fatty acid-binding protein; AFABP; A-FABP; A-FABPAFABP; ALBP; aP2; FABP4; fatty acid binding protein 4, adipocyte; Fatty acid-binding protein 4; fatty acid-binding protein, adipocyte
Mass (kDA):
14.719 kDA
Human | |
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Location: | 8q21.13 |
Sequence: | 8; NC_000008.11 (81478419..81483233, complement) |
Cytoplasm. Nucleus. Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export.
FABP4 is an electron transport chain inhibitor that inhibits fatty acid trans-membrane transport. Its clinical relevance is not known. Read on to learn more about the FABP4 marker and its uses in immunoprecipitation. Boster Bio: The Most Effective uses of the FABP4 marker
FABP4 is known to exert an effect on fatty acid oxidation in adipocytes and mitochondrial function. Although the exact function of FABP4 in metabolism is not fully understood, FABP4 purportedly plays a physiological regulatory function in regulating fat oxidation. It blocks the electron transport chain in mitochondria, which causes an alteration of the synthesis of fatty acids.
It is an effective inhibitor of oxidation of fatty acids. It can block the Akt/mTOR signaling pathway, an essential stage in the oxidation process of fatty acids. In studies, FABP4 reduced the inflammatory effects of leptin, CPT-1 and AOX1. It also promotes the accumulation of lipids within cells and inhibits phosphorylation in the ACC1Ser79. This inhibition of oxidation of fatty acids may be helpful in the treatment of metabolic syndrome.
The findings of this study suggest that FABP5 was able to mitigate the toxicity of psychosine to the mitochondria. It also caused mitochondrial pores formation which triggers the release the cytochrome C as well as mtDNA. FABP5 prevents psychosine-induced cell deaths in KG-1C cell lines, suggesting that FABP5 blocks VDAC-1 oligomerization. Furthermore, FABP5 interacts with BAX and VDAC-1, which results in an important blockage of psychosine-induced cell death. This compound represents a promising therapeutic option for KD.
I/R-induced AKI is prevented by inhibiting FABP4 and tubular cell death is reduced and this is a vital step in AKI. The treatment for AKI is complex and requires a multi-faceted approach. It isn't known which treatment will be the most effective, however the company is confident that it has found a promising molecule that could help alleviate some of the symptoms of the disease.
Another type of mitochondrial enzyme which is inhibited by FABP4 is Complex II, also known as Succinate-CoenzymeQ Reductase. This enzyme is divided into two functional groups that are complex I and complex II, which create fumarate from succinate and coenzyme Q outside of the complex. These two enzymes play a crucial role in the production of energy.
Research suggests that neutralizing the release of FABP4 could be a feasible treatment option for patients suffering from type 2 diabetes, insulin resistance, or vascular injury. The drug could also inhibit the activity of the NLRP3 Inflammasome which stimulates sympathetic nerves. FABP4 clinical trials are expected to start in the next few years.
FABP4 is a protein which regulates the trans-membranation of fatty acids. It also creates an underlying system for fatty acid transport. FABP4 is involved in the movement of fatty acids from the plasma membrane to the cell's mitochondria. It also assists in the delivery and mix long-chain unsaturated fatty acids to mitochondria. FABP4 may also affect the flux of FA to the mitochondria. It could also act in conjunction with ACC or malonyl-CoA.
It is not known whether FABP4 is a tumor-suppressor. FABP4 has been linked with liver inflammation and liver fibrosis. The fat cells surrounding malignant cells also make use of FABP4 to encourage cell proliferation. Studies have also shown that the overexpression of FABP4 can cause cancer. FABP4 regulates CPT1, which regulates energy metabolism.
FABP4 isn't the sole role of FAS in the cell. It regulates several signaling pathways including PI3K/Akt. More research is needed to determine the mechanism behind it. This marker blocks the trans-membrane transport of fatty acid. This study is a significant improvement in our understanding of this important protein.
Although FABP4 plays various roles in cancer, only a handful of studies have focused on EC. Its ability suppress tumor growth and metastasis could be an attractive therapeutic target. This study highlights the importance of FABP4 for cancer research and the role it plays in the EC field. It also highlights the importance of FABP4 in cancer-suppressing proteins.
In a mouse model FABP4 overexpression can reduce tumor growth. Bioluminescence imaging has shown upregulation of FABP4 in the vivo. The tumors were derived from two cell lines that overexpress FABP4 in mice. The tumors were removed by nude mice at intervals of weekly time and the size of the tumors was measured. FABP4 is known to be involved in the development of inflammatory diseases as well as the growth of tumors. To fully understand the function of FABP4 in the progression of cancer more research is needed.
After two days of plasmid transmission the cell lines were removed. They were then fixed in 10% neutral formalin for thirty minutes. They were then incubated with rabbit anti-rat Cyt C antibody for 12 h at 4 degC. After the incubation, the Clones with the highest FABP4 expression levels were kept for further cellular experiments.
The clinical significance of the FABP4 marker is not fully understood. It is unclear whether FABP1 plays a role in risk assessment for psoriasis and/or cardiovascular disease (CVD). This marker could be used to determine patients who are high risk for hematological disease and could also be used as a marker of response to treatment for psoriasis. However, further research is needed to confirm the clinical significance of the FABP4 marker.
In clinical studies, the FABP4 marker has proved useful in assessing cardiovascular disease risk. However, it has not yet been widely used in clinical practice. This test requires careful analysis prior to its use as norepinephrine gets rapidly eliminated from the bloodstream. In addition, the concentrations in blood of catecholamines are influenced by a variety of factors, such as a patient's age, gender, and hepatic function.
The concentrations in the blood of FABP4 are dynamically controlled during acute myocardial injuries (AMI). They are at their highest at the time of hospital admission, and also immediately after percutaneous coronary interventions. Following that, it begins to decrease. Patients who had received resuscitation after an out-of-hospital cardiac arrest had significantly higher levels of FABP4 in their blood. The serum FABP4 concentration could be a crucial biomarker of the risk of cardiovascular disease in Thalassemia.
Serum FABP4 levels are related to the adipocyte-derived fat acids. The FABP4 marker has been associated with lipolysis. While it isn't an ideal biomarker for lipolysis, it is a reliable marker for lipolysis. This marker is particularly useful in metabolic conditions such as cardiovascular risk. It is also useful in detecting blood fatty acids of patients with coronary artery disease and diabetes.
Patients with FE have lower levels in serum of FABP4, but they are higher in patients who have had joint replacement. Postoperatively, the levels of FABP4 are higher than those in preoperative patients. FABP4 is an excellent diagnostic marker for FE. Further research is needed to determine the clinical value and usefulness of FABP4 markers for FE. We are pleased to present on the results of a brief study demonstrating that FABP4 is a valuable marker in FE.
FABP4 is a novel biomarker for the vascular damage. Recent studies suggest that FABP4 could play a role in vascular injury. By immunoprecipitating the protein, scientists can determine the cells that have FABP4 deposits and which do not. These studies could provide new insights into the development of combination therapies. However the use of this biomarker is not limited to damage to the vascular system.
A simple WesternTM method was used to make a mouse-derived lysate. The lysates were then loaded with 0.2 mg/mL FABP4/AFABP. The lysates were then diluted. An antibody coupled to the lysate served as the detection agent. The proteins that were eluted were separated by SDS PAGE and studied using western Blot.
By using this method we determined whether FABP4 was induced by the presence of ligands that target AKT. Both CD36 and FABP4 are shown to be able to bind to the ligand responsible for AKT. Inhibition of either of the two proteins can reduce FABP4 expression. We therefore conclude that FABP4 induction is mediated through an increase in phosphorylation of AKT.
Upregulation of FABP4 is linked to angiogenesis and insulin resistance and may act as an adipokine. In macrophages, FABP4 may be also regulated by PUFA oxidation products. Further studies are necessary to determine whether FABP4 can be involved in these metabolic processes. FABP4 could become intolerant to antiangiogenic therapy if the gene is regulated.
PMID: 2481498 by Baxa C.A., et al. Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA.
PMID: 15357969 by Lehmann F., et al. Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target.
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