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PubMed1998

CD36 is rapidly and transiently upregulated on phytohemagglutinin (PHA)-stimulated peripheral blood lymphocytes. Analysis by a new monoclonal antibody (UN7).

The monoclonal antibody (mAb) UN7, clustered as an anti-CD36 mAb, has been used to test the cell surface expression of CD36 on peripheral blood lymphocytes (PBL) following mitogenic stimulation. CD36, scarcely expressed on resting cell membranes, was rapidly upregulated on PBL after phytohemagglutinin (PHA) stimulation. The antigen was detected on the cell surface after 15 min of stimulation, increased rapidly by 60 min and peaked between 3 and 12 h, declining thereafter. The inhibition of protein synthesis by cycloheximide did not modify the PHA-induced expression of CD36. Neither the anti-CD3 OKT3 mAb nor the anti-CD2 BIL 2.29 and 9.1 mAbs induced any significant upregulation of the molecule. The addition of anti-CD28 15E8 mAb or IL-2 or IFN-gamma to PHA or anti-CD3 or anti-CD2 mAbs did not influence the pattern of CD36 expression. The phorbol-2-myristate-13-acetate (PMA), alone or in combination with ionomycin, was unable to activate the expression of CD36, while it inhibited the PHA-induced upregulation. The PHA-induced upregulation of CD36 was partially inhibited by the addition of LY294002 or wortmannin, while not affected by that of calphostin C. Thus, CD36 was found to be early and transiently upregulated by PHA stimulation on PBL. The rapid modulation of the molecule was not related to new protein synthesis, but was probably due to the insertion into the plasma membrane of a presynthetized protein pool.

Antibodies, Monoclonal↗
PubMed1991

Keratinocyte expression of CD36 antigen in benign and malignant epidermal cell-derived tumours.

Keratinocytes express the macrophage/monocyte antigen CD36 in a variety of inflammatory cutaneous diseases characterised by a T lymphocyte rich infiltrate. Since cell-mediated immune mechanisms also play a role in host responses to skin tumours, we investigated the presence of CD36 antigen on keratinocytes in a range of epidermal cell-derived benign and malignant tumours characterised by a peritumoural, dermal lymphocytic infiltrate. Frozen tissue sections of lesional tissue from a range of epidermally derived tumours were labelled with antibodies to CD1a, CD11b, CD36, and HLA-DR antigens. Benign and malignant squamoproliferative tumour cells exhibited a spectrum of CD36 expression, whereas those of basal cell origin were consistently CD36-. Suprabasal expression of CD36 was present in the normal perilesional epidermis of all tumours studied including basal cell carcinoma. Keratinocyte CD11b expression was not observed. The widespread presence of keratinocyte CD36 positivity in squamoproliferative, but not basal epidermal, tumours suggests its expression may be linked to the degree of keratinocyte differentiation. The stimulus for expression is unknown, but the fact that suprabasal perilesional epidermis expressed CD36 strongly in the absence of infiltrate suggests it may represent a non-specific response by keratinocytes to various stimuli.

Adult↗
PubMed2001

CD36, a member of class B scavenger receptor family, is a receptor for advanced glycation end products.

Interaction of advanced glycation end products (AGE) with AGE-receptors induces several cellular phenomena relating potentially to diabetic complications. Five AGE-receptors identified so far are RAGE (receptor for AGE), 80 K-H, OST-48, galectin-3, and SR-A (macrophage scavenger receptor type I and II). Since SR-A belongs to the class A scavenger receptor family and the scavenger receptor collectively represents a family of multiligand lipoprotein receptors, it is possible that CD36 belonging to the class B scavenger receptor family (SR-B) can recognize AGE-proteins as a ligand. This was tested in the present study at the cellular level using CHO (Chinese hamster ovary) cells overexpressing human CD36 (CHO-CD36 cells). 125I-AGE-BSA (bovine serum albumin) was endocytosed in a dose-dependent fashion and underwent lysosomal degradation by CHO-CD36 but not wild-type CHO cells. Endocytic uptake of 125I-AGE-BSA by these cells was inhibited 50% by oxidized LDL (Ox-LDL) and 60% by FA6-152, an anti-CD36 antibody inhibiting cellular binding of Ox-LDL. Our results indicate that CD36 expressed by these cells mediates endocytic uptake and subsequent intracellular degradation of AGE-proteins. Because CD36 is one of the major Ox-LDL receptors and is upregulated in macrophage- and smooth muscle cell-derived foam cells in human atherosclerotic lesions, the present results suggest that, like Ox-LDL, AGE-proteins generated in situ are recognized by CD36, which might contribute to the pathogenesis of diabetic macrovascular complications.

Animals↗
PubMed2005

CD36 deficiency impairs intestinal lipid secretion and clearance of chylomicrons from the blood.

CD36 mediates the transfer of fatty acids (FAs) across the plasma membranes of muscle and adipose cells, thus playing an important role in regulating peripheral FA metabolism in vivo. In the proximal intestine, CD36 is localized in abundant quantities on the apical surface of epithelial cells, a pattern similar to that of other proteins implicated in the uptake of dietary FAs. To define the role of CD36 in the intestine, we examined FA utilization and lipoprotein secretion by WT and CD36-null mice in response to acute and chronic fat feeding. CD36-null mice given a fat bolus by gavage or fed a high-fat diet accumulated neutral lipid in the proximal intestine, which indicated abnormal lipid processing. Using a model in which mice were equipped with lymph fistulae, we obtained evidence of defective lipoprotein secretion by directly measuring lipid output. The secretion defect appeared to reflect an impaired ability of CD36-null enterocytes to efficiently synthesize triacylglycerols from dietary FAs in the endoplasmic reticulum. In the plasma of intact mice, the reduced intestinal lipid secretion was masked by slow clearance of intestine-derived lipoproteins. The impaired clearance occurred despite normal lipoprotein lipase activity and likely reflected feedback inhibition of the lipase by FAs due to their defective removal from the plasma. We conclude that CD36 is important for both secretion and clearance of intestinal lipoproteins. CD36 deficiency results in hypertriglyceridemia both in the postprandial and fasting states and in humans may constitute a risk factor for diet-induced type 2 diabetes and cardiovascular disease.

Animals↗
PubMedDate not supplied

CD36(+)-dendritic epidermal cells: a putative actor in the cutaneous immune system.

UNLABELLED: In the present study we have investigated by indirect immunofluorescence staining and mixed lymphocyte reaction methods, the localization, distribution, percentage, and the immunological involvement of CD36(+)-dendritic epidermal cells (CD36(+)-DECs) in normal human skin. Human epidermal cell suspensions were obtained from skin specimen of healthy persons. First, an indirect immunofluorescent staining method was performed on frozen skin sections, freshly isolated cells, nonadherent and adherent cells and second, the allogeneic mixed epidermal cell-lymphocyte reaction (ELR) method was performed with human peripheral blood mononuclear cells and irradiated CD36(+)-DECs plus CD-1a+ (Langerhans cells) and/ConA (at 10 micrograms/mL). We found that CD36(+)-DECs were localized in the epidermis mainly in the basal layer. They were non adherent cells. The percentage of these CD36(+)-DECs was of about 2%. These CD36(+)-DECs were AE3 (which recognizes keratin normally expressed by keratinocytes) positive cells. Our immunoreactivity study using allogeneic mixed ELR, showed that CD36(+)-DECs stimulated allogeneic lymphocyte proliferation. Their stimulatory effects were important when Langerhans cells and ConA were added separately or together to the PBMCs culture. The above results suggest that CD36(+)-DECs may contribute to the immunological role of skin and could be involved in cutaneous allograft recognition and rejection. ABBREVIATIONS: DECs: dendritic epidermal cells; ConA: concanavalin A; DPM: disintegrations per minute; ELR: epidermal cell-lymphocyte reaction; LC: Langerhans cells; PBMCs: peripheral blood mononuclear cells.

Adult↗
PubMed2001

The nonexpression of CD36 on reticulocytes and mature red blood cells does not modify the clinical course of patients with sickle cell anemia.

It is thought that an increase in the adhesion of circulating reticulocytes to the vascular endothelium may initiate the vascular occlusion underlying the painful crises and organ failures typical of sickle cell disease (SCD). At least 2 receptors, usually present on reticulocytes, seem to be involved in this adhesion process: glycoprotein CD36 (glycoprotein IV) and integrin alpha(4)beta(1) (very late activation antigen--4). Recently, a high frequency of the platelet CD36--deficient phenotype was reported in black Africans. The frequency of this deficiency was similar in subjects with and without SCD. The role of CD36 in vaso-occlusion was then investigated by comparing the clinical course in 2 groups of black Africans homozygous for hemoglobin S, with and without CD36 deficiency, but similar in age, sex, geographical origin, number of alpha-globin genes, and beta-globin gene haplotype. Flow cytometry showed that CD36 was absent from the circulating red blood cells and reticulocytes of platelet CD36--deficient individuals but present on those from patients with normal platelet CD36 expression, and that alpha(4)beta(1) integrin levels were similar on the reticulocytes of the 2 groups. Neither clinical severity, as evaluated by the frequency and characteristics of vaso-occlusive events, nor biological data differed significantly in the 2 groups of patients. Finally, although CD36 has been suggested to play a critical role in the pathogenesis of vaso-occlusion, this study, despite including only a small number of patients, supports the idea that the modulation of expression of a single type of adhesion molecule is insufficient to counteract the pathological process leading to vaso-occlusion in SCD patients. (Blood. 2001;98:966-971)

Adolescent↗
PubMed2006

RUNX3 negatively regulates CD36 expression in myeloid cell lines.

CD36 is a member of the scavenger receptor type B family implicated in the binding of lipoproteins, phosphatidylserine, thrombospondin-1, and the uptake of long-chain fatty acids. On mononuclear phagocytes, recognition of apoptotic cells by CD36 contributes to peripheral tolerance and prevention of autoimmunity by impairing dendritic cell (DC) maturation. Besides, CD36 acts as a coreceptor with TLR2/6 for sensing microbial diacylglycerides, and its deficiency leads to increased susceptibility to Staphylococcus aureus infections. The RUNX3 transcription factor participates in reprogramming DC transcription after pathogen recognition, and its defective expression leads to abnormally accelerated DC maturation. We present evidence that CD36 expression is negatively regulated by the RUNX3 transcription factor during myeloid cell differentiation and activation. In molecular terms, RUNX3 impairs the activity of the proximal regulatory region of the CD36 gene in myeloid cells through in vitro recognition of two functional RUNX-binding elements. Moreover, RUNX3 occupies the CD36 gene proximal regulatory region in vivo, and its overexpression in myeloid cells results in drastically diminished CD36 expression. The down-regulation of CD36 expression by RUNX3 implies that this transcription factor could impair harmful autoimmune responses by contributing to the loss of pathogen- and apoptotic cell-recognition capabilities by mature DCs.

Animals↗
PubMed1999

CD36 antisense expression in 3T3-F442A preadipocytes.

An adipocyte membrane glycoprotein, FAT, homologous to CD36, has been implicated in the binding/transport of long-chain fatty acids. FAT/CD36 was identified by reaction with reactive long chain fatty acids derivatives under conditions where they inhibited FA uptake. Expression of CD36 in fibroblasts lacking the protein led to induction of a saturable high affinity, phloretin-sensitive component of oleate uptake. In this report, we have examined the effects of FAT/CD36 antisense expression in 3T3-F442A preadipocyte cells, on FA uptake and cell differentiation. Cells were transfected with pSG5-TAF vector obtained by insertion of antisense coding sequence of FAT/CD36 into the BamH 1 site of pSG5. Four clones were selected based on expression of antisense CD36 mRNA. Levels of CD36 protein were determined by flow cytometry and correlated with rates of oleate uptake. Three clones, TAF13, TAF25, and TAF38 exhibited low CD36 expression and one clone TAF 18 had expression comparable to that of F442A control cells. FA uptake rates in clones TAF13, TAF25 and TAF38 were lower than those observed in TAF18. At confluence, adipocyte differentiation could be promoted by addition of insulin and triiodothyronine only in TAF18 cells but not in TAF13, TAF25 or TAF38. Addition of fatty acids to clones TAF13, TAF25 and TAF38 lead to an induction of CD36 expression, an enhancement of FA uptake and better cell differentiation. The data support a role of CD36 in the membrane uptake of long chain FA. CD36 expression and FA uptake appear to be closely linked to preadipocyte differentiation.

3T3 Cells↗
PubMed2000

Nonopsonic monocyte/macrophage phagocytosis of Plasmodium falciparum-parasitized erythrocytes: a role for CD36 in malarial clearance.

Plasmodium falciparum is the most lethal form of malaria and is increasing both in incidence and in its resistance to antimalarial agents. An improved understanding of the mechanisms of malarial clearance may facilitate the development of new therapeutic interventions. We postulated that the scavenger receptor CD36, an important factor in cytoadherence of P falciparum-parasitized erythrocytes (PEs), might also play a role in monocyte- and macrophage-mediated malarial clearance. Exposure of nonopsonized PEs to Fc receptor-blocked monocytes resulted in significant PE phagocytosis, accompanied by intense clustering of CD36 around the PEs. Phagocytosis was blocked 60% to 70% by monocyte pretreatment with monoclonal anti-CD36 antibodies but not by antibodies to alpha(v)beta(3), thrombospondin, intercellular adhesion molecule-1, or platelet/endothelial cell adhesion molecule-1. Antibody-induced CD36 cross-linking did result in the early increase of surface CD11b expression, but there was no increase in, or priming for, tumor necrosis factor (TNF)-alpha secretion following either CD36 cross-linking or PE phagocytosis. CD36 clustering does support intracellular signaling: Antibody-induced cross-linking initiated intracellular tyrosine phosphorylation as well as extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein kinase (MAPK) phosphorylation. Both broad-spectrum tyrosine kinase inhibition (genistein) and selective ERK and p38 MAPK inhibition (PD98059 and SB203580, respectively) reduced PE uptake to almost the same extent as CD36 blockade. Thus, CD36-dependent binding and signaling appears to be crucial for the nonopsonic clearance of PEs and does not appear to contribute to the increase in TNF-alpha that is prognostic of poor outcome in clinical malaria.

Animals↗
PubMed2000

Methionine 156 in the immunodominant domain of CD36 contributes to define the epitope recognized by the NL07 MoAb.

CD36 is a membrane glycoprotein expressed by several cell types, and play a role as a receptor for different physiological and pathological ligands. An immunodominant domain of CD36 has been described in the amino acidic region 155-183, where many ligands and monoclonal antibodies (MoAbs) react. MoAbs against CD36 have proved useful in structural as well as functional studies. One of these antibodies, MoAb NL07, recognizes a conformational epitope that is acquired in the late steps of the CD36 maturation. The NL07 epitope appears to be functionally relevant and blocks CD36-mediated binding to red blood cells infected with the malaria parasite Plasmodium falciparum (IRBC). In this work a mutant COS-7 clone expressing NL07-negative CD36 molecules on the cell surface was investigated. In the mutant, the methionine in position 156 of the wild type CD36 sequence was replaced by a valine. It was determined that methionine 156 was essential for NL07 reactivity, mapping the NL07 epitope to the vicinity of the functionally important immunodominant domain (aa 155-183) of CD36. Although methionine 156 is located in this region, the CD36V156 mutated molecule was apparently functional and able to bind IRBC and oxidized LDL.

Amino Acid Sequence↗
PubMed2003

Thrombospondin-1 induces apoptosis in primary leukemia and cell lines mediated by CD36 and Caspase-3.

Thrombospondin-1 (TSP-1) is a naturally occurring anti-angiogenic compound that induces apoptosis of endothelial and cancer cells via its receptor CD36. The objectives of our study were to investigate the in vitro effects of TSP-1 on the apoptosis of primary human leukemia cells as well as leukemia cell lines and the possible mechanism involving CD36. Our results demonstrated that TSP-1 induced apoptosis in CD36 positive cell lines CHRF-288-11, Meg-01 and HL-60, but not CD36 negative K562, at a dose-dependent manner as demonstrated by DNA ladder formation, Annexin V and propidium iodide (PI) stainings. The addition of anti-CD36 antibody FA6-152 or thrombopoietin (TPO) significantly nullified the effects of TSP-1. TSP-1-mediated apoptosis was consistently associated with the up-regulation of active Caspase-3. Responses of 2 CD36 positive primary AML samples to TSP-1 and FA6-152 were similar with those of leukemia cell lines. TSP-1 significantly induced apoptosis in B-ALL but the counter-effects of FA6-152 were less apparent. CD36 negative AML cells appeared less susceptible to TSP-1 and FA6-152. Our data provided strong evidence that TSP-1 exerted direct apoptotic effects on leukemia cells and could be developed as an adjunct to conventional therapy, particularly for leukemia cells that express CD36 or other TSP-1 receptors.

Antineoplastic Agents↗
PubMed2006

[Scavenger receptor CD36: its expression, regulation, and role in the pathogenesis of atherosclerosis. Part I].

Atherosclerosis is a progressive pathological process based on endothelial dysfunction and chronic inflammation. Monocytes, macrophages, and modified lipoproteins, especially oxidized LDLs (oxLDLs), play a fundamental role in the pathogenesis of atherosclerosis. Monocytes evolve into macrophages in the vascular wall and then accumulate oxLDLs, forming foam cells. OxLDLs are toxic and activate foam cells, stimulate the replication of macrophages and their migration into atherosclerotic plaque, and increase the expression of metaloproteinases. Macrophages bind oxLDLs through many types of receptors, among them scavenger receptors. One of these is CD36, a membrane glycoprotein expressed by endothelial cells, adipocytes, smooth and skeletal muscle cells, cardiomiocytes, platelets, monocytes, and macrophages. CD36 recognizes and binds many ligands, such as oxLDLs, long-chain fatty acids, collagen, thrombospondin 1, apoptotic cells, anionic phospholipids, and Plasmodium falciparum-infected erythrocytes. CD36 is involved in many processes, e.g. inner immune system responses, removal of apoptotic cells and Plasmodium falciparum-infected erythrocytes, and the transport of long-chain fatty acids, and it also mediates collagen and thrombospondin action. Recent reports indicate that CD36 may play a role in the development of atherosclerosis. An animal model revealed that lack of CD36 expression restrains atheroslerosis. Increased expression of CD36 was shown in atheroslerotic plaque and damaged vascular tissue. Contradictory data about the effects of antiatherosclerotic drugs on CD36 expression indicate the necessity for further investigation of the role of CD36 in the development of atherosclerosis.

Animals↗
PubMed1997

The carboxyl-terminal cytoplasmic domain of CD36 is required for oxidized low-density lipoprotein modulation of NF-kappaB activity by tumor necrosis factor-alpha.

The binding of oxidized low-density lipoprotein (Ox LDL) by monocyte-macrophages causes pleiotropic effects, including changes in gene expression, and is thought to represent an early event in atherogenesis. The integral membrane glycoprotein CD36 appears to play a physiological role in binding and uptake of Ox LDL by monocyte-macrophages, although the molecular events associated with CD36-Ox LDL interaction are unknown. To approach this issue, we used CD36 transfected Chinese hampster ovary (CHO) cells, exposed them to Ox LDL, and determined changes in the activity of the transcription factor NF-kappaB. We report here that Ox LDL enhanced DNA binding activity of nuclear extracts to an NF-kappaB sequence following activation of CD36-producing CHO cells with the proinflammatory cytokine tumor necrosis factor-alpha (TNF-alpha). This enhanced DNA binding activity was inhibited by coincubation of CD36 transfected cells with the human CD36-specific antibody OKM5. We also determined that activation of NF-kappaB DNA binding activity required an intact carboxyl-terminal cytoplasmic segment on CD36. Our results support the idea that human CD36 mediates signal transduction events in response to Ox LDL.

Animals↗
PubMed1998

Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL.

Mouse and hamster SR-BI glycoproteins and their putative human counterpart CLA-I are so far the only scavenger receptors known to bind both native and modified lipoproteins. CD36, a multigland glycoprotein structurally related to SR-BI and CLA-1, has been reported to bind oxidized low density lipoprotein (OxLDL) and acetylated LDL (AcLDL). In this report, we have studied the ability of CD36 to bind native lipoproteins. By transient expression of human CD36 in mammalian and insect cells, we demonstrate that CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, VLDL, and, as previously reported, for OxLDL and AcLDL. The specificity of these interactions is supported by the dose-dependent inhibiton, effect of a monoclonal antibody against CD36. Furthermore, at least for HDL, binding to CD36 does not require the presence of apoE. These findings, together with preferential expression of CD36 in tissues performing very active fatty acid metabolism (skeletal muscle, heart, mammary epithelium, and adipose tissue) and its involvement in foam cell formation (macrophages), suggest that binding of lipoproteins to CD36 might contribute to the regulation of lipid metabolism, and to the pathogenesis of atherosclerosis.

Animals↗
PubMed1998

Absent myocardial iodine-123-BMIPP uptake and platelet/monocyte CD36 deficiency.

UNLABELLED: Global absence of myocardial 123I-15-(p-iodophenyl)-3-(R,S)-methyl pentadecanoic acid (BMIPP) uptake is occasionally noted, and it reflects myocardial long-chain fatty acid uptake abnormality. CD36, a membrane glycoprotein expressed on platelet, monocyte and endothelial cells, may contribute to myocardial fatty acid transport, and its deficiency has been reported in a small subset of the population. We hypothesized that CD36 deficiency may be related to absent myocardial BMIPP uptake. Thus, we investigated CD36 expression of platelet/monocyte in patients with absent myocardial BMIPP uptake. METHODS: Peripheral blood of 7 patients with global absence of myocardial BMIPP uptake (3 of 7 patients in one family) and 3 control subjects were examined in flow cytometric analysis. Platelet/monocyte surface CD36 was detected by using OKM5, an anti-CD36 mouse monoclonal antibody. RESULTS: There were no apparent relationships between specific clinical symptoms and absent myocardial BMIPP uptake. None of the blood samples of the 7 patients were stained with OKM5 on the platelet/monocyte cell surface, indicating that all of these patients were Type I CD36-deficient subjects. In contrast, all the control subjects showed normal staining. CONCLUSION: The fact that rare Type I CD36 deficiency was observed in all patients with absent myocardial BMIPP uptake suggests that CD36 plays a role in the myocardial long-chain fatty acid uptake process in humans.

Adult↗
PubMed1998

Thrombin-stimulated calcium mobilization is inhibited by thrombospondin via CD36.

Activation of the G-protein-linked thrombin receptor in endothelial cells normally leads to an increase in free intracellular calcium, [Ca2+]i, which is the proximate stimulus for many important cell functions. We present evidence showing that signals from CD36, the thrombospondin (TSP) receptor, can inhibit this thrombin-mediated calcium response. Human endothelial cells preloaded with Indo-1 exhibited rapid calcium mobilization in response to thrombin. The presence of TSP inhibited the thrombin-stimulated calcium response in CD36-positive microvascular endothelial cells but not in CD36-negative umbilical vein endothelial cells. This TSP effect was mimicked by anti-CD36 antibodies and a TSP peptide (CSVTCG), but not by an alternative CD36 ligand (collagen IV) or an antibody to an alternative TSP receptor (alphavbeta3). TSP also inhibited the calcium response to the thrombin receptor-tethered ligand peptide, SFLLRN. In addition, TSP and anti-CD36 antibodies inhibited the calcium response of a closely related receptor, the trypsin/SLIGKVD-activated receptor PAR-2. TSP did not indiscriminately inhibit all calcium release pathways, since histamine- or VEGF-stimulated calcium responses were not inhibited by TSP. We conclude that cross-talk from the CD36 receptor influences the responsive state of the endothelial thrombin receptor family and/or its signaling pathway.

CD36 Antigens↗
PubMed2005

Takotsubo-shaped cardiomyopathy with type I CD36 deficiency.

A transient left ventricular apical ballooning (so-called "ampulla" or "Takotsubo-shaped" cardiomyopathy) with type I CD36 deficiency is described in a 71-year-old woman. The patient was referred because of chest pain and worsening of dyspnea. Electrocardiogram showed T-wave inversions on the precordal leads, and acute coronary syndrome was suspected. Left ventricular apical ballooning was observed by echocardiogram and left ventriculography, and coronary arteriography did not reveal any significant stenosis. Left ventricular motion normalized at the follow-up period and there were no increases in specific markers for myocardial damage, such as myocardial band fraction of creatine kinase and troponin T, through out the admission. 123I-metaiodobengylguanidine myocardial single photon emission computed tomography (SPECT) revealed decreased accumulation areas at the apex, while 201Tl SPECT showed normal accumulation. An abnormal metabolism of cardiac free fatty acid was suggested by lack of accumulation of 123I beta-methyliodophenyl pentadecanoic acid (BMIPP) SPECT. No CD36 expression in either platelets or monocytes/macrophages was shown using flow cytometer analysis and type I CD36 deficiency was diagnosed. DNA sequencing showed that the patient had compound heterozygosity of the CD36 gene (a nucleotide change in C478T and an adenine insertion at nucleotide 1159 in exon 10). Although CD36 deficiency is thought to be involved with many cardiovascular disease and metabolic abnormalities, Takotsubo-shaped cardiomyopathy with CD36 deficiency had not been reported. Further studies of Takotsubo-shaped cardiomyopathy and CD36 deficiency may reveal an association between this cardiomyopathy and specific genetic profiles.

Aged↗
PubMed1998

Primary ex vivo culture of keratinocytes isolated from hypertrophic scars as a means of biochemical characterization of CD36.

The CD36 antigen is a molecule which is ectopically expressed on epidermal keratinocytes of hypertrophic scars and is a good candidate for a marker for a broad range of skin pathologies. Most marker studies have been performed using immunohistochemical techniques on fixed skin sections. Our aim was to investigate the biochemical features of the CD36 expressed in pathological keratinocytes and to find an in vitro model for the study of the regulation of its expression. Here we show how keratinocytes isolated from hypertrophic scars can be cultivated in vitro and employed as a model for the study of these cells. We demonstrated that the antigenic features of the CD36 expressed on keratinocytes of hypertrophic scars are identical to those described for the CD36 expressed by other cell types. The molecule was expressed on the surface of keratinocytes which were non-adherent in vitro. Adherent and proliferating keratinocytes, as well as normal keratinocytes, were CD36 negative both at the surface and intracellularly. The in vitro proliferating cells from hypertrophic scars, but not the normal keratinocytes, showed intracellular expression of CD36 after long-term culture and cell stratification, suggesting a regulated expression of CD36 in pathological keratinocyte differentiation.

Adult↗