CCAAT-Enhancer-Binding Protein-alpha
CCAAT-Enhancer-Binding Proteins
CCAAT-Enhancer-Binding Protein-beta
CCAAT-Enhancer-Binding Protein-delta
Enhancer Elements, Genetic
Promoter Regions, Genetic
DNA-Binding Proteins
Transcription Factors
Nuclear Proteins
Transcription Factor CHOP
Gene Expression Regulation
Base Sequence
Adipocytes
Transcription, Genetic
Molecular Sequence Data
Cell Differentiation
RNA, Messenger
Binding Sites
Transcriptional Activation
Electrophoretic Mobility Shift Assay
3T3-L1 Cells
Protein Binding
Response Elements
Transfection
Cells, Cultured
Granulocytes
Cell Nucleus
3T3 Cells
PPAR gamma
Myelopoiesis
Gene Expression
Liver
Down-Regulation
Chromatin Immunoprecipitation
Genes, Reporter
Trans-Activators
Leucine Zippers
Adipose Tissue
Luciferases
Endrin
Signal Transduction
Blotting, Western
DNA
Up-Regulation
Tumor Cells, Cultured
Gene Expression Regulation, Enzymologic
Mutation
Regulatory Sequences, Nucleic Acid
Hepatocyte Nuclear Factor 3-beta
DNA Primers
Mice, Knockout
Acute-Phase Reaction
NF-kappa B p50 Subunit
Protein Isoforms
RNA Polymerase Sigma 54
Cyclic AMP Response Element-Binding Protein
HeLa Cells
Reverse Transcriptase Polymerase Chain Reaction
U937 Cells
Mice, Transgenic
Transcription Factor AP-2
Carrier Proteins
NF-kappa B
Oligonucleotides
Receptors, Cytoplasmic and Nuclear
Phosphorylation
Glucocorticoids
Blotting, Northern
Amino Acid Sequence
Gene Expression Regulation, Leukemic
Leukemia, Myeloid, Acute
Transcription Factor AP-1
Recombinant Fusion Proteins
Endoplasmic Reticulum Stress
RNA, Small Interfering
Epithelial Cells
Gene Expression Regulation, Neoplastic
Mutagenesis, Site-Directed
HL-60 Cells
Hepatocytes
Interleukin-6
Monocyte-Macrophage Precursor Cells
Repressor Proteins
Immunohistochemistry
Lipopolysaccharides
Endoplasmic Reticulum
Apoptosis
Monosaccharide Transport Proteins
Carcinoma, Hepatocellular
Proto-Oncogene Proteins
Plasmids
Gene Expression Profiling
Poly(A)-Binding Proteins
Fatty Acid-Binding Proteins
Deoxyribonuclease I
Cell Division
Fibroblasts
Macrophages
Phenotype
Rats, Sprague-Dawley
Inflammation
Oligonucleotide Array Sequence Analysis
Cloning, Molecular
Hypertonic Solutions
Proteins
DNA Footprinting
Insulin
Sterol Regulatory Element Binding Protein 1
Gene Expression Regulation, Developmental
CCAAT-Binding Factor
Chloramphenicol O-Acetyltransferase
Dimerization
Keratinocytes
Polymerase Chain Reaction
Myxococcus xanthus
Consensus Sequence
Homeodomain Proteins
NFATC Transcription Factors
Cyclic AMP
Sp1 Transcription Factor
Lymphoid Enhancer-Binding Factor 1
Tacrolimus Binding Proteins
Gene Knockdown Techniques
Tumor Necrosis Factor-alpha
Core Binding Factor Alpha 2 Subunit
Cell Cycle
Histone Deacetylase 1
Interleukin-1beta
Poly(A)-Binding Protein I
Enzyme Inhibitors
RNA-Binding Proteins
NIH 3T3 Cells
Nuclear Factor 90 Proteins
Mutagenesis
MEF2 Transcription Factors
Insulin-Like Growth Factor Binding Proteins
Stromal Cells
Unfolded Protein Response
Neoplasm Proteins
Myogenic Regulatory Factors
Protein Biosynthesis
Genes, Regulator
Leptin
Receptors, TNF-Related Apoptosis-Inducing Ligand
RNA Interference
Immunoblotting
Sequence Homology, Nucleic Acid
Hematopoiesis
Models, Biological
Stem Cells
Membrane Proteins
Isoenzymes
Proto-Oncogene Proteins c-jun
Restriction Mapping
Sequence Homology, Amino Acid
Protein Structure, Tertiary
Heat-Shock Proteins
TATA Box
Chromatin
Introns
Oligodeoxyribonucleotides
Sequence Alignment
Leukemia, Myeloid
HIV Enhancer
Poly(A)-Binding Protein II
Kidney
Osmolar Concentration
Organ Specificity
Bone Marrow Cells
Gene Expression Regulation, Bacterial
Oligonucleotide Probes
Gene Expression Regulation, Viral
DNA, Complementary
Conserved Sequence
Core Binding Factor alpha Subunits
Insulin-Like Growth Factor Binding Protein 3
Calcium-Binding Proteins
Drosophila Proteins
Repetitive Sequences, Nucleic Acid
Periplasmic Binding Proteins
COS Cells
CREB-Binding Protein
Y-Box-Binding Protein 1
Chickens
Exons
Tacrolimus Binding Protein 1A
C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (1/2395)
C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP. (+info)A critical role for cAMP response element-binding protein (CREB) as a Co-activator in sterol-regulated transcription of 3-hydroxy-3-methylglutaryl coenzyme A synthase promoter. (2/2395)
3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, a key regulatory enzyme in the pathway for endogenous cholesterol synthesis, is a target for negative feedback regulation by cholesterol. When cellular sterol levels are low, the sterol regulatory element-binding proteins (SREBPs) are released from the endoplasmic reticulum membrane, allowing them to translocate to the nucleus and activate SREBP target genes. However, in all SREBP-regulated promoters studied to date, additional co-regulatory transcription factors are required for sterol-regulated activation of transcription. We have previously shown that, in addition to SREBPs, NF-Y/CBF is required for sterol-regulated transcription of HMG-CoA synthase. This heterotrimeric transcription factor has recently been shown to function as a co-regulator in several other SREBP-regulated promoters, as well. In addition to cis-acting sites for both SREBP and NF-Y/CBF, the sterol regulatory region of the synthase promoter also contains a consensus cAMP response element (CRE), an element that binds members of the CREB/ATF family of transcription factors. Here, we show that this consensus CRE is essential for sterol-regulated transcription of the synthase promoter. Using in vitro binding assays, we also demonstrate that CREB binds to this CRE, and mutations within the CRE that result in a loss of CREB binding also result in a loss of sterol-regulated transcription. We further show that efficient activation of the synthase promoter in Drosophila SL2 cells requires the simultaneous expression of all three factors: SREBPs, NF-Y/CBF, and CREB. To date this is the first promoter shown to require CREB for efficient sterol-regulated transcription, and to require two different co-regulatory factors in addition to SREBPs for maximal activation. (+info)CCAAT/enhancer-binding protein beta is an accessory factor for the glucocorticoid response from the cAMP response element in the rat phosphoenolpyruvate carboxykinase gene promoter. (3/2395)
The cyclic AMP response element (CRE) of the rat phosphoenolpyruvate carboxykinase (PEPCK) gene promoter is required for a complete glucocorticoid response. Proteins known to bind the PEPCK CRE include the CRE-binding protein (CREB) and members of the CCAAT/enhancer-binding protein (C/EBP) family. We took two different approaches to determine which of these proteins provides the accessory factor activity for the glucocorticoid response from the PEPCK CRE. The first strategy involved replacing the CRE of the PEPCK promoter/chloramphenicol acetyltransferase reporter plasmid (pPL32) with a consensus C/EBP-binding sequence. This construct, termed pDeltaCREC/EBP, binds C/EBPalpha and beta but not CREB, yet it confers a nearly complete glucocorticoid response when transiently transfected into H4IIE rat hepatoma cells. These results suggest that one of the C/EBP family members may be the accessory factor. The second strategy involved co-transfecting H4IIE cells with a pPL32 mutant, in which the CRE was replaced with a GAL4-binding sequence (pDeltaCREGAL4), and various GAL4 DNA-binding domain (DBD) fusion protein expression vectors. Although chimeric proteins consisting of the GAL4 DBD fused to either CREB or C/EBPalpha are able to confer an increase in basal transcription, they do not facilitate the glucocorticoid response. In contrast, a fusion protein consisting of the GAL4 DBD and amino acids 1-118 of C/EBPbeta provides a significant glucocorticoid response. Additional GAL4 fusion studies were done to map the minimal domain of C/EBPbeta needed for accessory factor activity to the glucocorticoid response. Chimeric proteins containing amino acid regions 1-84, 52-118, or 85-118 of C/EBPbeta fused to the GAL4 DBD do not mediate a glucocorticoid response. We conclude that the amino terminus of C/EBPbeta contains a multicomponent domain necessary to confer accessory factor activity to the glucocorticoid response from the CRE of the PEPCK gene promoter. (+info)CCAAT/enhancer-binding proteins. A role in regulation of human involucrin promoter response to phorbol ester. (4/2395)
The phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) is a potent inducer of keratinocyte differentiation and of involucrin gene expression. In the present study we show that a CCAAT/enhancer-binding protein (C/EBP) site in the proximal regulatory region is required for the phorbol ester response. Mutation of the C/EBP site results in the loss of basal and TPA-responsive activity. Gel mobility supershift analysis shows that C/EBPalpha binding to this site is increased by TPA treatment. Moreover, cotransfection of the human involucrin reporter plasmid with C/EBPalpha increases promoter activity to an extent comparable with TPA treatment. Mutation of the C/EBP-binding site eliminates these responses. Transfection experiments using GADD153 to create C/EBP-null conditions confirm that C/EBP factors are absolutely required for promoter activity and TPA responsiveness. C/EBPbeta and C/EBPdelta inhibit both TPA- and C/EBPalpha-dependent promoter activation, indicating functional differences among C/EBP family members. These results suggest that C/EBP transcription factor activity is necessary for basal promoter activity and TPA response of the involucrin gene. (+info)The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. (5/2395)
When mammalian cells are subjected to calcium depletion stress or protein glycosylation block, the transcription of a family of glucose-regulated protein (GRP) genes encoding endoplasmic reticulum (ER) chaperones is induced to high levels. The consensus mammalian ER stress response element (ERSE) conserved among grp promoters consists of a tripartite structure CCAAT(N9)CCACG, with N being a strikingly GC-rich region of 9 bp. The ERSE, in duplicate copies, can confer full stress inducibility to a heterologous promoter in a sequence-specific but orientation-independent manner. In addition to CBF/NF-Y and YY1 binding to the CCAAT and CCACG motifs, respectively, we further discovered that an ER stress-inducible complex (ERSF) from HeLa nuclear extract binds specifically to the ERSE. Strikingly, the interaction of the ERSF with the ERSE requires a conserved GGC motif within the 9 bp region. Since mutation of the GGC triplet sequence also results in loss of stress inducibility, specific sequence within the 9 bp region is an integral part of the tripartite structure. Finally, correlation of factor binding with stress inducibility reveals that ERSF binding to the ERSE alone is not sufficient; full stress inducibility requires integrity of the CCAAT, GGC and CCACG sequence motifs, as well as precise spacing among these sites. (+info)Tumour necrosis factor-alpha regulates expression of the CCAAT-enhancer-binding proteins (C/EBPs) alpha and beta and determines the occupation of the C/EBP site in the promoter of the insulin-responsive glucose-transporter gene in 3T3-L1 adipocytes. (6/2395)
We have demonstrated previously that treatment of 3T3-L1 adipocytes with tumour necrosis factor-alpha (TNF) results in a rapid (4 h) and significant (75-80%) reduction in the rate of transcription of the GLUT4 gene. Control of GLUT4 gene transcription has been suggested at least in part to reside with the CCAAT-enhancer-binding protein (C/EBP) family (alpha, beta and delta isoforms) of transcription factors. Using electrophoretic mobility shift assays, we have examined the ability of TNF to alter the occupation of the C/EBP site in the GLUT4 promoter. The data suggest that in fully differentiated adipocytes the C/EBP site is a ligand for predominantly alpha/alpha homodimers; however, after exposure to TNF, a shift in occupancy of the site occurs and the ligands become alpha/beta heterodimers and beta/beta homodimers. Partner selection in dimer formation appears to be controlled by selective translocation of the beta-isoform from the cytosol to the nucleus after exposure of the cells to TNF. (+info)A novel splicing isoform of mouse sterol regulatory element-binding protein-1 (SREBP-1). (7/2395)
We cloned a cDNA encoding the NH2-terminal portion of mouse SREBP-1. The deduced amino acid sequence was 76% and 90% identical to human and hamster SREBP-1, respectively. We found out a novel splicing isoform of mouse SREBP-1 that lacks 42 amino acid residues composing a PEST sequence observed in unstable proteins. It has been reported that SREBP-1 is rapidly turned over in the nucleus. Although this isoform was not a dominant isoform, it might be possible that the produced protein functions differently from other isoforms including a complete PEST sequence. (+info)Transcription factors CCAAT/enhancer-binding protein beta and nuclear factor-Y bind to discrete regulatory elements in the very low density lipoprotein receptor promoter. (8/2395)
Expression of the very low density lipoprotein receptor (VLDL-R) is barely detectable in liver, but occurs in adipose tissue, skeletal muscle, heart, and placenta, where it is postulated to supply triglyceride to tissues that utilize fatty acids. To investigate its tissue-specific expression, cell lines were transfected with luciferase reporter gene constructs driven by the 5'-flanking region of the VLDL-R gene. Transcriptional activity of a 4.2-kb promoter fragment was 5-fold higher in BeWo placental cells than in Huh-7 hepatoma cells, consistent with relative endogenous expression of the VLDL-R. By deletion analysis, DNase I protection assays and site-directed mutagenesis, two regulatory elements were essential for maximal promoter activity in BeWo cells: footprint site D (-856 to -830) and an inverted CCAAT box (-703 to -707). Mutation of either element reduced promoter activity by 60% in BeWo cells, but had little effect in Huh-7 cells, suggesting that these elements direct cell-type specific transcription. Electrophoretic mobility-shift assays with BeWo nuclear extracts revealed that the inverted CCAAT box binds transcription factor NF-Y, and site D binds CCAAT/enhancer-binding protein b (C/EBPbeta) and minor amounts of C/EBPalpha and C/EBPdelta. Overexpression of a dominant negative NF-YA vector confirmed involvement of NF-Y in the regulation of the VLDL-receptor gene through the CCAAT box. However overexpression of C/EBP could not stimulate transcription from the VLDL-receptor promoter nor from site D fused to a heterologous promoter, suggesting that the simultaneous binding of an accessory factor(s) may be necessary for C/EBP transactivation via the D site. (+info)The term "acute-phase" describes the rapid onset and short duration of this reaction, which typically lasts for hours to days before resolving as the body's inflammatory response subsides. APR is characterized by a series of molecular events that result in altered expression of genes involved in inflammation, immune response, and tissue repair.
Some key components of an acute-phase reaction include:
1. Cytokine production: Cytokines are signaling molecules released by immune cells, such as white blood cells, that coordinate the immune response. During an APR, cytokine levels increase, triggering a cascade of downstream effects.
2. Leukocyte trafficking: White blood cells migrate towards sites of inflammation or infection, where they phagocytose (engulf and digest) pathogens and cellular debris. This process helps to limit the spread of infection and initiate tissue repair.
3. Coagulation cascade: The APR triggers a complex series of events involving blood coagulation factors, leading to the formation of blood clots and preventing excessive bleeding.
4. Anti-inflammatory response: As the APR progresses, anti-inflammatory cytokines, such as interleukin-10 (IL-10), are produced to dampen the inflammatory response and promote tissue repair.
5. Cellular proliferation: To replace damaged cells and tissues, the APR stimulates cellular proliferation and tissue regeneration.
6. Nutrient mobilization: The APR enhances nutrient uptake and utilization by immune cells, allowing them to mount an effective response to the stress.
7. Hormonal changes: The APR is accompanied by changes in hormone levels, such as the increase in corticotropin-releasing factor (CRF) and cortisol, which help to mobilize energy resources and regulate metabolism.
8. Immune tolerance: The APR helps to establish immune tolerance, preventing excessive or inappropriate immune responses that can lead to autoimmune diseases or allergies.
9. Tissue remodeling: The APR stimulates the remodeling of damaged tissues, allowing for the restoration of normal tissue function.
10. Memory formation: The APR sets the stage for the formation of immunological memory, which enables the immune system to mount a more effective response to future infections or stressors.
AML is a fast-growing and aggressive form of leukemia that can spread to other parts of the body through the bloodstream. It is most commonly seen in adults over the age of 60, but it can also occur in children.
There are several subtypes of AML, including:
1. Acute promyelocytic leukemia (APL): This is a subtype of AML that is characterized by the presence of a specific genetic abnormality called the PML-RARA fusion gene. It is usually responsive to treatment with chemotherapy and has a good prognosis.
2. Acute myeloid leukemia, not otherwise specified (NOS): This is the most common subtype of AML and does not have any specific genetic abnormalities. It can be more difficult to treat and has a poorer prognosis than other subtypes.
3. Chronic myelomonocytic leukemia (CMML): This is a subtype of AML that is characterized by the presence of too many immature white blood cells called monocytes in the blood and bone marrow. It can progress slowly over time and may require ongoing treatment.
4. Juvenile myeloid leukemia (JMML): This is a rare subtype of AML that occurs in children under the age of 18. It is characterized by the presence of too many immature white blood cells called blasts in the blood and bone marrow.
The symptoms of AML can vary depending on the subtype and the severity of the disease, but they may include:
* Fatigue
* Weakness
* Shortness of breath
* Pale skin
* Easy bruising or bleeding
* Swollen lymph nodes, liver, or spleen
* Bone pain
* Headache
* Confusion or seizures
AML is diagnosed through a combination of physical examination, medical history, and diagnostic tests such as:
1. Complete blood count (CBC): This test measures the number and types of cells in the blood, including red blood cells, white blood cells, and platelets.
2. Bone marrow biopsy: This test involves removing a small sample of bone marrow tissue from the hipbone or breastbone to examine under a microscope for signs of leukemia cells.
3. Genetic testing: This test can help identify specific genetic abnormalities that are associated with AML.
4. Immunophenotyping: This test uses antibodies to identify the surface proteins on leukemia cells, which can help diagnose the subtype of AML.
5. Cytogenetics: This test involves staining the bone marrow cells with dyes to look for specific changes in the chromosomes that are associated with AML.
Treatment for AML typically involves a combination of chemotherapy, targeted therapy, and in some cases, bone marrow transplantation. The specific treatment plan will depend on the subtype of AML, the patient's age and overall health, and other factors. Some common treatments for AML include:
1. Chemotherapy: This involves using drugs to kill cancer cells. The most commonly used chemotherapy drugs for AML are cytarabine (Ara-C) and anthracyclines such as daunorubicin (DaunoXome) and idarubicin (Idamycin).
2. Targeted therapy: This involves using drugs that specifically target the genetic abnormalities that are causing the cancer. Examples of targeted therapies used for AML include midostaurin (Rydapt) and gilteritinib (Xospata).
3. Bone marrow transplantation: This involves replacing the diseased bone marrow with healthy bone marrow from a donor. This is typically done after high-dose chemotherapy to destroy the cancer cells.
4. Supportive care: This includes treatments to manage symptoms and side effects of the disease and its treatment, such as anemia, infection, and bleeding. Examples of supportive care for AML include blood transfusions, antibiotics, and platelet transfusions.
5. Clinical trials: These are research studies that involve testing new treatments for AML. Participating in a clinical trial may give patients access to innovative therapies that are not yet widely available.
It's important to note that the treatment plan for AML is highly individualized, and the specific treatments used will depend on the patient's age, overall health, and other factors. Patients should work closely with their healthcare team to determine the best course of treatment for their specific needs.
There are several risk factors for developing HCC, including:
* Cirrhosis, which can be caused by heavy alcohol consumption, viral hepatitis (such as hepatitis B and C), or fatty liver disease
* Family history of liver disease
* Chronic obstructive pulmonary disease (COPD)
* Diabetes
* Obesity
HCC can be challenging to diagnose, as the symptoms are non-specific and can be similar to those of other conditions. However, some common symptoms of HCC include:
* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Loss of appetite
* Abdominal pain or discomfort
* Weight loss
If HCC is suspected, a doctor may perform several tests to confirm the diagnosis, including:
* Imaging tests, such as ultrasound, CT scan, or MRI, to look for tumors in the liver
* Blood tests to check for liver function and detect certain substances that are produced by the liver
* Biopsy, which involves removing a small sample of tissue from the liver to examine under a microscope
Once HCC is diagnosed, treatment options will depend on several factors, including the stage and location of the cancer, the patient's overall health, and their personal preferences. Treatment options may include:
* Surgery to remove the tumor or parts of the liver
* Ablation, which involves destroying the cancer cells using heat or cold
* Chemoembolization, which involves injecting chemotherapy drugs into the hepatic artery to reach the cancer cells
* Targeted therapy, which uses drugs or other substances to target specific molecules that are involved in the growth and spread of the cancer
Overall, the prognosis for HCC is poor, with a 5-year survival rate of approximately 20%. However, early detection and treatment can improve outcomes. It is important for individuals at high risk for HCC to be monitored regularly by a healthcare provider, and to seek medical attention if they experience any symptoms.
There are several key features of inflammation:
1. Increased blood flow: Blood vessels in the affected area dilate, allowing more blood to flow into the tissue and bringing with it immune cells, nutrients, and other signaling molecules.
2. Leukocyte migration: White blood cells, such as neutrophils and monocytes, migrate towards the site of inflammation in response to chemical signals.
3. Release of mediators: Inflammatory mediators, such as cytokines and chemokines, are released by immune cells and other cells in the affected tissue. These molecules help to coordinate the immune response and attract more immune cells to the site of inflammation.
4. Activation of immune cells: Immune cells, such as macrophages and T cells, become activated and start to phagocytose (engulf) pathogens or damaged tissue.
5. Increased heat production: Inflammation can cause an increase in metabolic activity in the affected tissue, leading to increased heat production.
6. Redness and swelling: Increased blood flow and leakiness of blood vessels can cause redness and swelling in the affected area.
7. Pain: Inflammation can cause pain through the activation of nociceptors (pain-sensing neurons) and the release of pro-inflammatory mediators.
Inflammation can be acute or chronic. Acute inflammation is a short-term response to injury or infection, which helps to resolve the issue quickly. Chronic inflammation is a long-term response that can cause ongoing damage and diseases such as arthritis, asthma, and cancer.
There are several types of inflammation, including:
1. Acute inflammation: A short-term response to injury or infection.
2. Chronic inflammation: A long-term response that can cause ongoing damage and diseases.
3. Autoimmune inflammation: An inappropriate immune response against the body's own tissues.
4. Allergic inflammation: An immune response to a harmless substance, such as pollen or dust mites.
5. Parasitic inflammation: An immune response to parasites, such as worms or fungi.
6. Bacterial inflammation: An immune response to bacteria.
7. Viral inflammation: An immune response to viruses.
8. Fungal inflammation: An immune response to fungi.
There are several ways to reduce inflammation, including:
1. Medications such as nonsteroidal anti-inflammatory drugs (NSAIDs), corticosteroids, and disease-modifying anti-rheumatic drugs (DMARDs).
2. Lifestyle changes, such as a healthy diet, regular exercise, stress management, and getting enough sleep.
3. Alternative therapies, such as acupuncture, herbal supplements, and mind-body practices.
4. Addressing underlying conditions, such as hormonal imbalances, gut health issues, and chronic infections.
5. Using anti-inflammatory compounds found in certain foods, such as omega-3 fatty acids, turmeric, and ginger.
It's important to note that chronic inflammation can lead to a range of health problems, including:
1. Arthritis
2. Diabetes
3. Heart disease
4. Cancer
5. Alzheimer's disease
6. Parkinson's disease
7. Autoimmune disorders, such as lupus and rheumatoid arthritis.
Therefore, it's important to manage inflammation effectively to prevent these complications and improve overall health and well-being.
Liver neoplasms, also known as liver tumors or hepatic tumors, are abnormal growths of tissue in the liver. These growths can be benign (non-cancerous) or malignant (cancerous). Malignant liver tumors can be primary, meaning they originate in the liver, or metastatic, meaning they spread to the liver from another part of the body.
There are several types of liver neoplasms, including:
1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and arises from the main cells of the liver (hepatocytes). HCC is often associated with cirrhosis and can be caused by viral hepatitis or alcohol abuse.
2. Cholangiocarcinoma: This type of cancer arises from the cells lining the bile ducts within the liver (cholangiocytes). Cholangiocarcinoma is rare and often diagnosed at an advanced stage.
3. Hemangiosarcoma: This is a rare type of cancer that originates in the blood vessels of the liver. It is most commonly seen in dogs but can also occur in humans.
4. Fibromas: These are benign tumors that arise from the connective tissue of the liver (fibrocytes). Fibromas are usually small and do not spread to other parts of the body.
5. Adenomas: These are benign tumors that arise from the glandular cells of the liver (hepatocytes). Adenomas are usually small and do not spread to other parts of the body.
The symptoms of liver neoplasms vary depending on their size, location, and whether they are benign or malignant. Common symptoms include abdominal pain, fatigue, weight loss, and jaundice (yellowing of the skin and eyes). Diagnosis is typically made through a combination of imaging tests such as CT scans, MRI scans, and ultrasound, and a biopsy to confirm the presence of cancer cells.
Treatment options for liver neoplasms depend on the type, size, location, and stage of the tumor, as well as the patient's overall health. Surgery may be an option for some patients with small, localized tumors, while others may require chemotherapy or radiation therapy to shrink the tumor before surgery can be performed. In some cases, liver transplantation may be necessary.
Prognosis for liver neoplasms varies depending on the type and stage of the cancer. In general, early detection and treatment improve the prognosis, while advanced-stage disease is associated with a poorer prognosis.
Myeloid leukemia can be classified into several subtypes based on the type of cell involved and the degree of maturity of the abnormal cells. The most common types of myeloid leukemia include:
1. Acute Myeloid Leukemia (AML): This is the most aggressive form of myeloid leukemia, characterized by a rapid progression of immature cells that do not mature or differentiate into normal cells. AML can be further divided into several subtypes based on the presence of certain genetic mutations or chromosomal abnormalities.
2. Chronic Myeloid Leukemia (CML): This is a slower-growing form of myeloid leukemia, characterized by the presence of a genetic abnormality known as the Philadelphia chromosome. CML is typically treated with targeted therapies or bone marrow transplantation.
3. Myelodysplastic Syndrome (MDS): This is a group of disorders characterized by the impaired development of immature blood cells in the bone marrow. MDS can progress to AML if left untreated.
4. Chronic Myelomonocytic Leukemia (CMML): This is a rare form of myeloid leukemia that is characterized by the accumulation of immature monocytes in the blood and bone marrow. CMML can be treated with chemotherapy or bone marrow transplantation.
The symptoms of myeloid leukemia can vary depending on the subtype and severity of the disease. Common symptoms include fatigue, weakness, fever, night sweats, and weight loss. Diagnosis is typically made through a combination of physical examination, blood tests, and bone marrow biopsy. Treatment options for myeloid leukemia can include chemotherapy, targeted therapies, bone marrow transplantation, and supportive care to manage symptoms and prevent complications. The prognosis for myeloid leukemia varies depending on the subtype of the disease and the patient's overall health. With current treatments, many patients with myeloid leukemia can achieve long-term remission or even be cured.
CCAAT-enhancer-binding proteins
Glutamate-rich protein 4
DNA damage-inducible transcript 3
CAAT box
CEBPA
CEBPB
CEBPD
CEBPG
CEBPE
WD Repeat and Coiled Coil Containing Protein
TRIB1
EHMT1
Myosatellite cell
Serum response factor
Liver X receptor alpha
CYP3A4
Estrogen receptor alpha
Dominance (genetics)
ACAT1
Jun dimerization protein
Transdifferentiation
PCK1
FOXI1
FOXA3
Antineoplastic resistance
Kaang Bong-kiun
Transcription elongation regulator 1
SUMO2
C8orf48
Adipogenesis
PANO1
Esta Sterneck
Glucocorticoid receptor
CUTL1
Embryonal fyn-associated substrate
Unfolded protein response
MicroRNA
C1orf112
ENO3
PIAS4
White adipose tissue
Haematopoiesis
Multiple Epidermal Growth Factor-like Domains 8
Transmembrane protein 251
CEBP
U7 small nuclear RNA
KMT2D
Transcription factor
DNA replication factor CDT1
IL18BP
Neutrophil-specific granule deficiency
DLX3
Down-regulation of the expression of CCAAT/enhancer binding protein α gene in cervical squamous cell carcinoma | BMC Cancer |...
CCAAT/enhancer binding protein β expression is increased in the brain during HIV-1-infection and contributes to regulation of...
Inhibited activities in CCAAT/enhancer-binding protein, activating protein-1 and cyclins after hepatectomy in rats with...
The VBP and a1/EBP leucine zipper factors bind overlapping subsets of avian retroviral long terminal repeat CCAAT/enhancer...
Biblio | Linus Pauling Institute | Oregon State University
CEBPA gene: MedlinePlus Genetics
RFA-DK-03-002: THE LIFE CYCLE OF THE ADIPOCYTE
Biomarkers Search
Another pedigree with familial acute myeloid leukemia and germline CEBPA mutation - PubMed
Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation - PubMed
Publication Detail
Go to Relief of cyclin A gene transcriptional inhibition during activation of human primary T lymphocytes via CD2 and CD28...
Frontiers | The Role of Decidual Subpopulations in Implantation, Menstruation and Miscarriage
The Heterogeneity of White Adipose Tissue | IntechOpen
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磷脂氫麩胱甘肽過氧化酵素PHGPx抑制砷
Genes4
- This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity (expression) of certain genes. (medlineplus.gov)
- This requires the activity of proteins called transcription factors that bind to DNA and switch on the expression of genes. (elifesciences.org)
- The canonical pathway of EZH2 (Enhancer of Zeste homolog 2) catalyzes the trimethylation of histone H3K27 to silence the transcription of target genes. (frontiersin.org)
- NF-κB acts as a transcription factor binding to an NF-κB response element located at the promoter of target genes, regulating TNF-α, IL-6 and IL-8 ( 11 , 12 ). (spandidos-publications.com)
Making a protein called1
- The CEBPA gene provides instructions for making a protein called CCAAT enhancer-binding protein alpha. (medlineplus.gov)
CHOP1
- Notably, Tan I upregulated CCAAT-enhancer-binding protein homologous protein (CHOP), inositol-requiring protein-1 (IRE1) and p-c-Jun N-terminal kinase (p-JNK), but silencing of IRE1 or p62 and JNK inhibitor SP600125 blocked the LC3II accumulation in Tan I-treated H28 cells. (oncotarget.com)
Factor5
- CCAAT enhancer binding protein β (C/EBP), a transcription factor, is detected in rodent brains in response to neuroinflammation, implicating it in Alzheimer's, Parkinson's and HIV-1-associated neurocognitive disorders (HAND). (nntc.org)
- Because levels of transcription factor CCAAT/enhancer binding protein-β, peroxisome proliferator-activated receptor-γ, and lipoprotein lipase are also increased, lipid transport into cells and fatty acid synthesis within cells is increased ( 8 - 15 ). (cdc.gov)
- Functional genomics data indicate that 2 of the suggestive SNPs (rs2446823 and rs2446824) are located within putative binding sites for the CCAAT/Enhancer Binding Protein (CEBP) and Hepatocyte Nuclear Factor 4, Alpha transcription factors (TFs), respectively. (cdc.gov)
- El FACTOR DE UNIÓN A CCAAT es estructuralmente un tipo distinto de proteína de unión aumentadora a CCAAT que consta de un trímero de tres subunidades diferentes. (bvsalud.org)
- CCAAT-BINDING FACTOR is structurally distinct type of CCAAT-enhancer binding protein consisting of a trimer of three different subunits. (bvsalud.org)
Receptors1
- Nuclear receptors that bind OXYSTEROLS and function as heterodimers with RETINOID X RECEPTORS. (ouhsc.edu)
Nuclear2
- Nuclear and cytoplasmic proteins were examined by western blot analysis. (spandidos-publications.com)
- Specific DNA-binding activity of C/EBPδ protein in nuclear extracts was examined by electromobility shift and antibody supershift assay. (utmb.edu)
Transcription Factors1
- The GR is an intracellular protein that is ubiquitously expressed in almost every cell of the organism and interacts with chromatin to modulate the activity of numerous transcription factors in a cell type-specific manner. (biomedcentral.com)
Mitochondrial1
- CCAAT/enhancer binding protein ß deletion increases mitochondrial function and protects mice from LXR-induced hepatic steatosis. (ouhsc.edu)
Gene expression3
- Impaired DNA binding interferes with the protein's ability to regulate gene expression and impairs its tumor suppressor function. (medlineplus.gov)
- If the amount of PPARγ bound to DNA is too low, then it is unable to activate gene expression. (elifesciences.org)
- Gene Expression of CCAAT/enhancer-binding Protein Mediated by Autoregulation Is Repressed by Related Gene Family Proteins. (elsevierpure.com)
Tumor3
- This shortened protein is produced from one copy of the CEBPA gene in each cell, and it is believed to interfere with the tumor suppressor function of the normal protein produced from the second copy of the gene. (medlineplus.gov)
- Absence of the tumor suppressor function of CCAAT enhancer-binding protein alpha is believed to disrupt the regulation of blood cell production, leading to the uncontrolled production of abnormal cells that occurs in acute myeloid leukemia. (medlineplus.gov)
- One type leads to production of an abnormally short protein that interferes with the tumor suppressor function of normal versions of CCAAT enhancer-binding protein alpha. (medlineplus.gov)
Adipocytes1
- In adipocytes, the sterol regulatory element binding protein pathway is increased, resulting in increases in levels of sterol regulatory element binding protein 1 and fatty acid synthase. (cdc.gov)
Metabolism1
- Adipose tissue not only stores energy, but also controls metabolism through secretion of hormones, cytokines, proteins, and microRNAs that affect the function of cells and tissues throughout the body. (intechopen.com)
Vitro1
- They bind in vitro respectively ATF-1 and NF-Y proteins. (cnrs.fr)
Increases2
- Overexpression of C/EBPβ increases TIMP-1 promoter activity, mRNA and protein levels in human astrocytes activated with IL-1β. (nntc.org)
- Histamine increases the permeability of capillaries to white blood cells and various proteins to allow them to engage pathogens in the infected tissue ( 6 ). (spandidos-publications.com)
Receptor3
- Histamine binds to the H1 receptor in target cells to contract gut and bronchus smooth muscle and to increase venular permeability and rheum ( 6 ). (spandidos-publications.com)
- Glucocorticoids exert their function by binding to the glucocorticoid receptor (GR). Physiological concentrations of glucocorticoids stimulate osteoblast proliferation and promote osteogenic differentiation of MSCs. (biomedcentral.com)
- Chronic and acute CB1 antagonism decreases NF-κB binding activity To further investigate the mechanisms involved in Slc2a4 upregulation by the CB1 receptor, an electrophoretic mobility shift assay ( EMSA ) was performed. (bioscientifica.com)
Specificity1
- OBJECTIVE: 18F-FP-CIT positron emission tomography (PET) is known for its high sensitivity and specificity for evaluating striatal dopamine transporter (DAT) binding. (bvsalud.org)
Differentiation2
- CCAAT enhancer-binding protein alpha is involved in the maturation (differentiation) of certain blood cells. (medlineplus.gov)
- TRIM23 knockdown caused a marked decrease in PPARγ protein abundance during preadipocyte differentiation, resulting in a severe defect in late adipogenic differentiation, whereas it did not affect the formation of early enhanceosomes. (elifesciences.org)
ALPHA4
- The mutations result in a shorter version of CCAAT enhancer-binding protein alpha. (medlineplus.gov)
- The somatic CEBPA gene mutations that have been identified in leukemia cells generally decrease the DNA-binding ability of CCAAT enhancer-binding protein alpha. (medlineplus.gov)
- The other type of mutation blocks the DNA-binding ability of CCAAT enhancer-binding protein alpha. (medlineplus.gov)
- CCAAT/enhancer binding protein alpha, beta and delta gene variants: associations with obesity related phenotypes in the Leeds Family Study. (cdc.gov)
MRNA2
Initiation1
- In vivo genomic DMS footprinting revealed upstream of the major transcription initiation sites, the presence of at least three protein binding sites, two of which were constitutively occupied. (cnrs.fr)
Motif1
- Here, we show that a novel ubiquitin E3 ligase, tripartite motif protein 23 (TRIM23), stabilizes PPARγ protein and mediates atypical polyubiquitin conjugation. (elifesciences.org)
Activation2
- Herein, Tan I exerted cytotoxicity with autophagic features of autophagy protein 5 (ATG5)/ microtubule-associated protein 1A/1B-light chain 3II (LC3 II) activation, p62/sequestosome 1 (SQSTM1) accumulation and increased number of LC3II punctae, acridine orange-stained cells and autophagic vacuoles. (oncotarget.com)
- The typical CCAAT-enhancer binding protein forms dimers and consists of an activation domain, a DNA-binding basic region, and a leucine-rich dimerization domain (LEUCINE ZIPPERS). (bvsalud.org)
Cells2
- To understand the mechanisms underlined in this regulation in normal human cells, we have analysed in vivo protein-DNA interactions at the Cyclin A locus in primary T lymphocytes. (cnrs.fr)
- analyzed this process in mouse cells and identified a protein called TRIM23 that is produced in precursor cells. (elifesciences.org)
Levels1
- TNF‑α, IL‑6 and IL‑8 secreted protein levels were measured using an ELISA assay. (spandidos-publications.com)
Shift1
- isoforms lacking KTS was associated with specific binding to cis -elements in the IGF-IR promoter region, as demonstrated using electrophoretic mobility shift assays ( EMSAs ) and DNaseI footprinting analysis. (bioscientifica.com)
Mice1
- 2014. Deficiency of CCAAT/enhancer binding protein-epsilon reduces atherosclerotic lesions in LDLR-/- mice. . (oregonstate.edu)
Suggests2
- this suggests that this protein is necessary for adipogenesis. (elifesciences.org)
- Overlap of 2 suggestive SNPs with likely TF binding sites suggests possible roles in disruption of gene regulation. (cdc.gov)
Regions1
- These enhancer regions are subsequently inherited by late enhanceosomes. (elifesciences.org)
Early1
- Our results suggest that TRIM23 plays a critical role in the switching from early to late adipogenic enhanceosomes by stabilizing PPARγ protein possibly via atypical polyubiquitin conjugation. (elifesciences.org)