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CD36

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CD36
Identifiers
AliasesCD36,BDPLT10, CHDS7, FAT, GP3B, GP4, GPIV, PASIV, SCARB3, CD36 molecule
External IDsOMIM:173510;MGI:107899;HomoloGene:73871;GeneCards:CD36;OMA:CD36 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

948

12491

Ensembl

ENSG00000135218

ENSMUSG00000002944

UniProt

P16671

Q08857

RefSeq (mRNA)

NM_001159555
NM_001159556
NM_001159557
NM_001159558
NM_007643

RefSeq (protein)

NP_001153027
NP_001153028
NP_001153029
NP_001153030
NP_031669

Location (UCSC)Chr 7: 80.37 – 80.68 MbChr 5: 17.99 – 18.09 Mb
PubMedsearch[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CD36(cluster of differentiation36), also known asplatelet glycoprotein 4,fatty acid translocase(FAT), scavenger receptor class B member 3 (SCARB3), and glycoproteins 88 (GP88), IIIb (GPIIIB), or IV (GPIV) is aproteinthat in humans is encoded by theCD36gene.The CD36 antigen is anintegral membrane proteinfound on the surface of many cell types in vertebrate animals. It imports fatty acids inside cells and is a member of the class Bscavenger receptorfamily ofcellsurface proteins. CD36 binds manyligandsincludingcollagen,[5]thrombospondin,[6]erythrocytesparasitized withPlasmodium falciparum,[7]oxidizedlow density lipoprotein,[8][9]nativelipoproteins,[10]oxidizedphospholipids,[11]and long-chainfatty acids.[12]

Work in genetically modified rodents suggest a role for CD36 infatty acidmetabolism,[13][14][15]heart disease,[16]taste,[17][18][19]and dietary fat processing in theintestine.[20]It may be involved in glucose intolerance,atherosclerosis,arterialhypertension,diabetes,cardiomyopathy,Alzheimer's diseaseand variouscancers,mostly ofepithelial origin(breast,prostate,ovary,andcolon) and also forhepatic carcinomaandgliomas.[21][22][23]

Structure

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Primary

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Inhumans,ratsandmice,CD36 consists of 472 amino acids with a predicted molecular weight of approximately 53,000Da.However, CD36 is extensively glycosylated and has an apparent molecular weight of 88,000Daas determined bySDS polyacrylamide gel electrophoresis.[24]

Tertiary

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UsingKyte–Doolittle analysis,[25]theamino acid sequenceof CD36 predicts ahydrophobicregion near each end of the protein large enough to spancellular membranes.Based on this notion and the observation that CD36 is found on the surface of cells, CD36 is thought to have a 'hairpin-like' structure withα-helicesat the C- and N- termini projecting through themembraneand a larger extracellular loop (Fig. 1). Thistopologyis supported by transfection experiments in cultured cells using deletion mutants of CD36.[26][27]

Based on the crystal structure of the homologousSCARB2,a model of the extracellular domain of CD36 has been produced.[28]Like SCARB2, CD36 is proposed to contain an antiparallel β-barrel core with many short α-helices adorning it. The structure is predicted to contain a hydrophobic transport tunnel. Disulfide linkages between 4 of the 6cysteineresidues in the extracellular loop are required for efficient intracellular processing and transport of CD36 to theplasma membrane.[29]It is not clear what role these linkages play on the function of the mature CD36 protein on the cell surface.

Posttranslational modification

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Besides glycosylation, additionalpost-translational modificationshave been reported for CD36. CD36 is modified with 4palmitoyl chains,2 on each of the two intracellular domains.[27]The function of these lipid modifications is currently unknown but they likely promote the association of CD36 with the membrane and possiblylipid raftswhich appear to be important for some CD36 functions.[30][31]CD36 could be also phosphorylated at Y62, T92, T323,[32]ubiquitinated at K56, K469, K472 and acetylated at K52, K56, K166, K231, K394, K398, K403.[33][34][35]

Protein-protein interactions

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In the absence of ligand, membrane bound CD36 exists primarily in a monomeric state. However exposure to thethrombospondinligand causes CD36 to dimerize. This dimerization has been proposed to play an important role in CD36signal transduction.[36]

Genetics

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In humans, thegeneis located on the long arm ofchromosome 7at band 11.2 (7q11.2[37]) and is encoded by 15exonsthat extend over more than 32kilobases.Both the 5' and the 3' untranslated regions containintrons:the 5' with two and the 3' one. Exons 1, 2 and first 89 nucleotides of exon 3 and as well as exon 15 are non-coding. Exon 3 contains encodes the N-terminal cytoplasmic and transmembrane domains. The C-terminal cytoplasmic and transmembrane regions is encoded by exon 14. The extracellular domain is encoded by the central 11 exons. Alternative splicing of the untranslated regions gives rise to at least twomRNAspecies.

Thetranscriptioninitiation site of the CD36 gene has been mapped to 289nucleotidesupstream from thetranslationalstartcodonand aTATA boxand several putative cis regulatory regions lie further 5'. A binding site for PEBP2/CBF factors has been identified between -158 and -90 and disruption of this site reduces expression. The gene is the transcriptional control of thenuclearreceptorPPAR/RXR heterodimer (Peroxisome proliferator-activated receptor–Retinoid X receptor) and gene expression can be up regulated using synthetic and natural ligands for PPAR and RXR, including thethiazolidinedioneclass of anti-diabeticdrugsand thevitamin Ametabolite 9-cis-retinoic acidrespectively.

Tissue distribution

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CD36 is found onplatelets,erythrocytes,monocytes,differentiatedadipocytes,skeletal muscle,mammary epithelial cells,spleencells and someskinmicrodermalendothelial cells.

Function

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The protein itself belongs to the class Bscavenger receptorfamily which includes receptors for selective cholesteryl ester uptake,scavenger receptor class B type I(SR-BI) andlysosomal integral membrane protein II(LIMP-II).

CD36 interacts with a number of ligands, includingcollagentypes I and IV,thrombospondin,erythrocytesparasitized withPlasmodium falciparum,platelet-agglutinating protein p37, oxidizedlow density lipoproteinandlong-chain fatty acids.[38]

OnmacrophagesCD36 forms part of anon-opsonic receptor(the scavenger receptor CD36/alpha-v beta-3complex) and is involved inphagocytosis.[39]

CD36 has also been implicated inhemostasis,thrombosis,malaria,inflammation,lipidmetabolismandatherogenesis.[40]

On binding a ligand the protein and ligand are internalized. This internalization is independent ofmacropinocytosisand occurs by an actin dependent mechanism requiring the activation Src-family kinases, JNK and Rho-family GTPases.[41]Unlike macropinocytosis this process is not affected byinhibitors of phosphatidylinositol 3-kinaseor Na+/H+exchange.

CD36 ligands have also been shown to promote sterile inflammation through assembly of aToll-like receptor4 and 6 heterodimer.[42]

Recently, CD36 was linked to store-operated calcium flux, phospholipase A2activation, and production of prostaglandin E2[43]

CD36 function in long-chain fatty acid uptake and signaling can be irreversibly inhibited bysulfo-N-succinimidyl oleate(SSO), which binds lysine 164 within a hydrophobic pocket shared by several CD36 ligands, e.g. fatty acid and oxLDL.[34]Recent research concluded that CD36 is involved in the fat taste transduction (oleogustus).

Clinical significance

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Malaria

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Infections with the human malaria parasitePlasmodium falciparumare characterized by sequestration of erythrocytes infected with mature forms of the parasite and CD36 has been shown to be a major sequestration receptor onmicrovascularendothelial cells. Parasitised erythrocytes adhere to endothelium at thetrophozoite/schizontsstage simultaneous with the appearance of thevargene product (erythrocyte membrane protein 1) on the erythrocyte surface. The appearance ofPlasmodium falciparumerythrocyte membrane protein 1(PfEMP1) on the erythrocyte surface is atemperaturedependent phenomenon which is due to increased protein trafficking to the erythrocyte surface at the raised temperature. PfEMP1 can bind other endothelial receptors -thrombospondin(TSP) and intercellular adhesion molecule 1 (ICAM-1) – in addition to CD36 - and genes other than PfEMP1 also bind to CD36:cytoadherence linked protein(clag) andsequestrin.The PfEMP1 binding site on CD36 is known to be located on exon 5.

CD36 on the surface of the platelets has been shown to be involved in adherence but direct adherence to the endothelium by the infected erythrocytes also occurs. Autoaggregation of infected erythrocytes by platelets has been shown to correlate with severe malaria and cerebral malaria in particular and antiplatelet antibodies may offer some protection.

Several lines of evidence suggest that mutations in CD36 are protective against malaria: mutations in thepromotersand within introns and in exon 5 reduce the risk of severe malaria. Gene diversity studies suggest there has been positive selection on this gene presumably due to malarial selection pressure. Dissenting reports are also known suggesting that CD36 is not the sole determinant of severe malaria. In addition a role for CD36 has been found in the clearance ofgametocytes(stages I and II).

CD36 has been shown to have a role in the innate immune response to malaria in mouse models.[44]Compared with wild type mice CD36 (-/-) mice the cytokine induction response and parasite clearance were impaired. Earlier peak parasitemias, higher parasite densities and higher mortality were noted. It is thought that CD36 is involved in thePlasmodium falciparumglycophosphatidylinositol(PfGPI) inducedMAPKactivation and proinflammatory cytokine secretion. When macrophages were exposed to PfGPI the proteins ERK1/2, JNK, p38, and c-Jun became phosphorylated. All these proteins are involved as secondary messengers in the immune response. These responses were blunted in the CD36 (-/-) mice. Also in the CD36 (-/-) macrophages secreted significantly less TNF-alpha on exposure to PfGPI. Work is ongoing to determine how these exactly how these responses provide protection against malaria.

CD36 deficiency and alloimmune thrombocytopenia

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CD36 is also known as glycoprotein IV (gpIV) or glycoprotein IIIb (gpIIIb) in platelets and gives rise to theNaka antigen.The Naka nullphenotypeis found in 0.3% of Caucasians and appears to be asymptomatic. The null phenotype is more common inAfrican(2.5%),Japanese,and otherAsianpopulations (5-11%).

Mutations in the human CD36 gene were first identified in a patient who, despite multipleplatelettransfusions,continued to exhibit low platelet levels.[45][46]This condition is known as refractoriness to platelet transfusion. Subsequent studies have shown that CD36 found on the surface of platelets. This antigen is recognized by themonoclonal antibodies(MAbs) OKM5 and OKM8. It is bound by thePlasmodium falciparumproteinsequestrin.[47]

Depending on the nature of the mutation in codon 90 CD36 may be absent either on both platelets and monocytes (type 1) or platelets alone (type 2). Type 2 has been divided into two subtypes - a and b. Deficiency restricted to the platelets alone is known as type 2a; if CD36 is also absent from the erythroblasts the phenotype is classified as type 2b.[48]The molecular basis is known for some cases: T1264G in bothKenyansandGambians;C478T (50%), 539 deletion of AC and 1159 insertion of an A, 1438-1449 deletion and a combined 839-841 deletion GAG and insertion of AAAAC in Japanese.

In a study of 827 apparently healthy Japanese volunteers, type I and II deficiencies were found in 8 (1.0%) and 48 (5.8%) respectively.[49]In 1127 healthy French blood donors (almost all of whom were white Europeans) no CD36 deficiency was found.[50]In a second group only 1 of 301 white test subjects was found to be CD36 deficient. 16 of the 206 sub-Saharan black Africans and 1 of 148 black Caribbeans were found to be CD36 -ve. Three of 13 CD36 -ve persons examined had anti CD36 antibodies. In a group of 250 black American blood donors 6 (2.4%) were found to be Naka antigen negative.[51]

CD36 deficiency may be a cause of post transfusionpurpura.[52]

Blood pressure

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Below normal levels of CD36 expression in the kidneys has been implicated as a genetic risk factor forhypertension(high blood pressure).[53]

Fatty acid uptake

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An association with myocardial fatty acid uptake in humans has been noted.[54]The data suggest a link betweenhypertrophic cardiomyopathyand CD36 but this needs to be confirmed.

Tuberculosis

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RNAiscreening in aDrosophilamodel has revealed that a member of the CD36 family is required forphagocytosisofMycobacterium tuberculosisinto macrophage phagosomes.[55]

Toxoplasmosis

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Avirulent strains ofToxoplasma gondiibind to CD36 but virulent parasites fail to engage CD36. In mice, CD36 is required for disease tolerance but not for the development of immunity or resistance.[56]

Obesity

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CD36's association with the ability totastefats has made it a target for various studies regardingobesityand alteration oflipidtasting.CD36 mRNA expression was found to be reduced intaste budcells (TBC) of obesesand rats(P. obesus) compared to lean controls, implicating an association between CD36 and obesity.[57]Although actual levels of CD36 protein were not different between the obese and control rat cells, Abdoul-Azize et al. hypothesize that the physical distribution of CD36 could differ in obese rat cells.[57]Changes in calcium mediation have been associated with CD36 and obesity as well. Taste bud cells (more specifically, cells from thecircumvallate papillae) containing CD36 that were isolated from obese mice exhibited a significantly smaller increase in calcium after fatty acid stimulation when compared to control mice:[58]CD36 associated calcium regulation is impaired when mice are made to be obese (but not in normal weight mice), and this could be a mechanism contributing to behavior changes in the obese mice, such as decreased lipid taste sensitivity and decreased attraction to fats.[58]

There has been some investigation into human CD36 as well. A study examined oral detection of fat in obese subjects with genetic bases for high, medium, and low expression of the CD36 receptor. Those subjects with high CD36 expression were eight times more sensitive to certain fats (oleic acidandtriolein) than the subjects with low CD36 expression.[18]Those subjects with an intermediate amount of CD36 expression were sensitive to fat at a level between the high and low groups.[18]This study demonstrates that there is a significant relationship between oral fat sensitivity and the amount of CD36 receptor expression, but further investigation into CD36 could be useful for learning more about lipid tasting in the context of obesity, as CD36 may be a target for therapies in the future.

Establishment of cellular senescence

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Reducing the burden of senescent cells, or reducing their inflammatory secretome through CD36 neutralization, accelerates regeneration in young and old mice.[59]

Cancer

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CD36 plays a role in the regulation ofangiogenesis,which may be a therapeutic strategy for controlling the spread of cancer.[60]Some data fromin vitroand animal studies suggested that fatty acid uptake through CD36 may promote cancer cell migration and proliferation in hepatocellular carcinoma,glioblastoma,and potentially other cancers; there was limited data from observational studies in people that low CD36 may correlate with a slightly better outcome in glioblastoma.[61]

Interactions

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CD36 has been shown tointeractwithFYN.[62][63]

[edit]
CD36 family
Structure of Limp-II. PDB entry4f7b
Identifiers
SymbolCD36
PfamPF01130
InterProIPR002159
Available protein structures:
Pfam structures/ECOD
PDBRCSB PDB;PDBe;PDBj
PDBsumstructure summary

Other humanscavenger receptorsrelated to CD36 areSCARB1andSCARB2proteins.

See also

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References

[edit]
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Further reading

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