Search results for CD36

Showing 24 results out of 44

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Species

Types

Compartments

Reaction types

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Protein (5 results from a total of 6)

Identifier: R-HSA-114687
Species: Homo sapiens
Compartment: platelet alpha granule membrane
Primary external reference: UniProt: CD36: P16671
Identifier: R-HSA-1236835
Species: Homo sapiens
Compartment: phagocytic vesicle
Primary external reference: UniProt: CD36: P16671
Identifier: R-HSA-51645
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CD36: P16671
Identifier: R-HSA-6806151
Species: Homo sapiens
Compartment: specific granule membrane
Primary external reference: UniProt: CD36: P16671
Identifier: R-HSA-2239449
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Primary external reference: UniProt: CD36: P16671

Reaction (5 results from a total of 15)

Identifier: R-HSA-6797267
Species: Homo sapiens
Compartment: plasma membrane, nucleoplasm
In human peripheral blood monocytes Interleukin-4 (IL4) and IL13 significantly upregulates the levels of proteins involved in inflammatory resolution including the cell surface protein CD36 (Berry et al. 2007).
Identifier: R-HSA-434381
Species: Homo sapiens
Compartment: plasma membrane
CD36 (FAT) located in the plasma membrane of pancreatic beta cells transports fatty acids such as palmitate into the cell (Noushmehr et al. 2005).
Identifier: R-HSA-560517
Species: Homo sapiens
Compartment: nucleoplasm, plasma membrane
The Platelet glycoprotein IV gene (CD36, PAS IV, GPIV) is transcribed to yield mRNA and the mRNA is translated to yield proteind.
Identifier: R-HSA-2559464
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Scavenger receptor CD36 has been reported to function as an essential co-receptor involved in recognition of LTA and certain diacylated lipoproteins and presenting them to the TLR2:TLR6 heterodimer at the cell surface. CD14, a GPI-anchored molecule found on the cell surface of human phagocytes, has been also implicated in TLR2:TLR6 signaling [Stuart L et al 2005; Hoebe KP et al 2005; Triantafilou M et al 2006; Nilsen NJ et al 2008]
Identifier: R-HSA-168950
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
TLR2 - in combination with TLR6 - plays a major role in recognizing lipoteichoic acid (LTA) and peptidoglycan wall products from Gram-positive bacteria, as well as Mycobacterial diacylated lipopeptides.

Set (5 results from a total of 7)

Identifier: R-HSA-2187232
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2247490
Species: Homo sapiens
Compartment: endocytic vesicle lumen
Identifier: R-NUL-9038450
Species: Neisseria gonorrhoeae, Homo sapiens
Compartment: extracellular region
Identifier: R-NUL-9038449
Species: Neisseria gonorrhoeae, Homo sapiens
Compartment: endocytic vesicle lumen
Identifier: R-HSA-2512795
Species: Homo sapiens
Compartment: extracellular region

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5640184
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000135218

Complex (5 results from a total of 12)

Identifier: R-HSA-2559461
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8869674
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-181410
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8869680
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-168949
Species: Homo sapiens
Compartment: plasma membrane

Pathway (3 results from a total of 3)

Identifier: R-HSA-434313
Species: Homo sapiens
Fatty acids augment the glucose triggered secretion of insulin through two mechanisms: activation of FFAR1 (GPR40) and intracellular metabolism of fatty acids. Fatty acids are transported into the cell by CD36 (FAT) (Noushmehr et al. 2005) and metabolized by ligation to coenzyme A (Ansari et al. 2017), transport into mitochondria, and beta oxidation which generates ATP. The ATP increases the intracellular ratio of ATP:ADP and thereby closes potassium channels (K(ATP) channels) at the plasma membrane (reviewed in Acosta-Montano and Garcia-Gonzalez 2018). The enzymes that metabolize glucose in beta cells also metabolize fatty acids in other tissues however their combinations and subcellular locations may differ.
Identifier: R-HSA-1989781
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane, extracellular region, lipid droplet, mitochondrial inner membrane, mitochondrial matrix, mitochondrial outer membrane, nucleoplasm, peroxisomal matrix, peroxisomal membrane, plasma membrane
The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include:
1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2);
2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2);
3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1);
4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5);
5) genes involved in triglyceride clearance ( Angptl4);
6) genes involved in glycerol metabolism (Gpd1 in mouse);
7) genes involved in glucose metabolism (Pdk4);
8) genes involved in peroxisome proliferation (Pex11a);
9) genes involved in lipid storage (Plin, Adfp).
Many other genes are known to be regulated by PPAR-alpha but whether their regulation is direct or indirect remains to be found. These genes include: ACACA, FAS, SREBP1, FADS1, DGAT1, ABCA1, PLTP, ABCB4, UGT2B4, SULT2A1, Pnpla2, Acsl1, Slc27a4, many Acot genes, and others (reviewed in Rakhshandehroo et al. 2010).
Identifier: R-HSA-381340
Species: Homo sapiens
Compartment: nucleoplasm, cytosol, plasma membrane
Adipogenesis is the process of cell differentiation by which preadipocytes become adipocytes. During this process the preadipocytes cease to proliferate, begin to accumulate lipid droplets and develop morphologic and biochemical characteristics of mature adipocytes such as hormone responsive lipogenenic and lipolytic programs. The most intensively studied model system for adipogenesis is differentiation of the mouse 3T3-L1 preadipocyte cell line by an induction cocktail of containing mitogens (insulin/IGF1), glucocorticoid (dexamethasone), an inducer of cAMP (IBMX), and fetal serum (Cao et al. 1991, reviewed in Farmer 2006). More recently additional cellular models have become available to study adipogenesis that involve almost all stages of development (reviewed in Rosen and MacDougald 2006). In vivo knockout mice lacking putative adipogenic factors have also been extensively studied. Human pathways are traditionally inferred from those discovered in mouse but are now beginning to be validated in cellular models derived from human adipose progenitors (Fischer-Posovszky et al. 2008, Wdziekonski et al. 2011).
Adipogenesis is controlled by a cascade of transcription factors (Yeh et al. 1995, reviewed in Farmer 2006, Gesta et al. 2007). One of the first observable events during adipocyte differentiation is a transient increase in expression of the CEBPB (CCAAT/Enhancer Binding Protein Beta, C/EBPB) and CEBPD (C/EBPD) transcription factors (Cao et al. 1991, reviewed in Lane et al. 1999). This occurs prior to the accumulation of lipid droplets. However, it is the subsequent inductions of CEBPA and PPARG that are critical for morphological, biochemical and functional adipocytes.
Ectopic expression of CEBPB alone is capable of inducing substantial adipocyte differentiation in fibroblasts while CEBPD has a minimal effect. CEBPB is upregulated in response to intracellular cAMP (possibly via pCREB) and serum mitogens (possibly via Krox20). CEBPD is upregulated in response to glucocorticoids. The exact mechanisms that upregulate the CEBPs are not fully known.
CEBPB and CEBPD act directly on the Peroxisome Proliferator-activated Receptor Gamma (PPARG) gene by binding its promoter and activating transcription. CEBPB and CEBPD also directly activate the EBF1 gene (and possibly other EBFs) and KLF5 (Jimenez et al. 2007, Oishi 2005). The EBF1 and KLF5 proteins, in turn bind, and activate the PPARG promoter. Other hormones, such as insulin, affect PPARG expression and other transcription factors, such as ADD1/SREBP1c, bind the PPARG promoter. This is an area of ongoing research.
During adipogenesis the PPARG gene is transcribed to yield 2 variants. The adipogenic variant 2 mRNA encodes 30 additional amino acids at the N-terminus compared to the widely expressed variant 1 mRNA.
PPARG encodes a type II nuclear hormone receptor (remains in the nucleus in the absence of ligand) that forms a heterodimer with the Retinoid X Receptor Alpha (RXRA). The heterodimer was initially identified as a complex regulating the aP2/FABP4 gene and named ARF6 (Tontonoz et al. 1994).
The PPARG:RXRA heterodimer binds a recognition sequence that consists of two hexanucleotide motifs (DR1 motifs) separated by 1 nucleotide. Binding occurs even in the absence of ligands, such as fatty acids, that activate PPARG. In the absence of activating ligands, the PPARG:RXRA complex recruits repressors of transcription such as SMRT/NCoR2, NCoR1, and HDAC3 (Tontonoz and Spiegelman 2008).
Each molecule of PPARG can bind 2 molecules of activating ligands. Although, the identity of the endogenous ligands of PPARG is unknown, exogenous activators include fatty acids and the thiazolidinedione class of antidiabetic drugs (reviewed in Berger et al. 2005, Heikkinen et al. 2007, Lemberger et al. 1996). The most potent activators of PPARG in vitro are oxidized derivatives of unsaturated fatty acids.. Upon binding activating ligands PPARG causes a rearrangement of adjacent factors: Corepressors such as SMRT/NCoR2 are lost and coactivators such as TIF2, PRIP, CBP, and p300 are recruited (Tontonoz and Spiegelman). PPARG also binds directly to the TRAP220 subunit of the TRAP/Mediator complex that recruits RNA polymerase II. Thus binding of activating ligand by PPARG causes transcription of PPARG target genes.
Targets of PPARG include genes involved in differentiation (PGAR/HFARP, Perilipin, aP2/FABP4, CEBPA), fatty acid transport (LPL, FAT/CD36), carbohydrate metabolism (PEPCK-C, AQP7, GK, GLUT4 (SLC2A4)), and energy homeostasis (LEPTIN and ADIPONECTIN) (Perera et al. 2006).
Within 10 days of differentiation CEBPB and CEBPD are no longer located at the PPARG promoter. Instead CEBPA is present. EBF1 and PPARG bind the CEBPA promoter and activate transcription of CEBPA, one of the key transcription factors in adipogenesis. A current hypothesis posits a self-reinforcing loop that maintains PPARG expression and the differentiated state: PPARG activates CEBPA and CEBPA activates PPARG. Additionally EBF1 (and possibly other EBFs) activates CEBPA, CEBPA activates EBF1, and EBF1 activates PPARG.
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