Deubiquitination of CD36 by UCHL1 promotes foam cell formation.


Journal

Cell death & disease
ISSN: 2041-4889
Titre abrégé: Cell Death Dis
Pays: England
ID NLM: 101524092

Informations de publication

Date de publication:
15 08 2020
Historique:
received: 12 05 2020
accepted: 04 08 2020
revised: 03 08 2020
entrez: 18 8 2020
pubmed: 18 8 2020
medline: 13 4 2021
Statut: epublish

Résumé

Atherosclerosis-associated cardiovascular diseases are main causes leading to high mortality worldwide. Macrophage-derived foam cell formation via uptaking modified lipoproteins is the initial and core step in the process of atherosclerosis. Meanwhile, scavenger receptor is indispensable for the formation of foam cells. UCHL1, a deubiquitinase, has been widely studied in multiple cancers. UCHL1 could be an oncogene or a tumor suppressor in dependent of tumor types. It remains unknown whether UCHL1 influences cellular oxLDL uptake. Herein we show that UCHL1 deletion significantly inhibits lipid accumulation and foam cell formation. Subsequently, we found that UCHL1 inhibitor or siRNA downregulates the expression of CD36 protein whereas SR-A, ABCA1, ABCG1, Lox-1, and SR-B1 have no significant change. Furthermore, the treatment of UCHL1 inhibition increases the abundance of K48-polyubiquitin on CD36 and the suppression of lipid uptake induced by UCHL1 deficiency is attenuated by blocking CD36 activation. Our study concluded that UCHL1 deletion decreases foam cell formation by promoting the degradation of CD36 protein, indicating UCHL1 may be a potential target for atherosclerosis treatment.

Identifiants

pubmed: 32801299
doi: 10.1038/s41419-020-02888-x
pii: 10.1038/s41419-020-02888-x
pmc: PMC7429868
doi:

Substances chimiques

ATP Binding Cassette Transporter 1 0
ATP-Binding Cassette Transporters 0
CD36 Antigens 0
Lipids 0
Lipoproteins, LDL 0
Scavenger Receptors, Class A 0
oxidized low density lipoprotein 0
Cholesterol 97C5T2UQ7J
Deubiquitinating Enzymes EC 3.4.19.12
Ubiquitin Thiolesterase EC 3.4.19.12

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

636

Références

Vasan, R. S. & Benjamin, E. J. The future of cardiovascular epidemiology. Circulation 133, 2626–2633 (2016).
pubmed: 27324358 pmcid: 4974092
Writing Group, M. et al. Heart disease and stroke statistics-2016 update: a report from the American Heart Association. Circulation 133, e38–e360 (2016).
Go, A. S. et al. Executive summary: heart disease and stroke statistics-2013 update: a report from the American Heart Association. Circulation 127, 143–152 (2013).
Legein, B., Temmerman, L., Biessen, E. A. & Lutgens, E. Inflammation and immune system interactions in atherosclerosis. Cell. Mol. Life Sci. 70, 3847–3869 (2013).
pubmed: 23430000
Yuan, Y., Li, P. & Ye, J. Lipid homeostasis and the formation of macrophage-derived foam cells in atherosclerosis. Protein Cell 3, 173–181 (2012).
pubmed: 22447659 pmcid: 4875426
Moore, K. J. & Tabas, I. Macrophages in the pathogenesis of atherosclerosis. Cell 145, 341–355 (2011).
pubmed: 21529710 pmcid: 3111065
Chistiakov, D. A., Bobryshev, Y. V. & Orekhov, A. N. Macrophage-mediated cholesterol handling in atherosclerosis. J. Cell Mol. Med. 20, 17–28 (2016).
pubmed: 26493158
Kunjathoor, V. V. et al. Scavenger receptors class A-I/II and CD36 are the principal receptors responsible for the uptake of modified low density lipoprotein leading to lipid loading in macrophages. J. Biol. Chem. 277, 49982–49988 (2002).
pubmed: 12376530
Li, A. C. & Glass, C. K. The macrophage foam cell as a target for therapeutic intervention. Nat. Med. 8, 1235–1242 (2002).
pubmed: 12411950
Sporstol, M., Mousavi, S. A., Eskild, W., Roos, N. & Berg, T. ABCA1, ABCG1 and SR-BI: hormonal regulation in primary rat hepatocytes and human cell lines. BMC Mol. Biol. 8, 5 (2007).
pubmed: 17241464 pmcid: 1790708
Tall, A. R., Yvan-Charvet, L., Terasaka, N., Pagler, T. & Wang, N. HDL, ABC transporters, and cholesterol efflux: implications for the treatment of atherosclerosis. Cell Metab. 7, 365–375 (2008).
pubmed: 18460328
Yvan-Charvet, L., Wang, N. & Tall, A. R. Role of HDL, ABCA1, and ABCG1 transporters in cholesterol efflux and immune responses. Arterioscler. Thromb. Vasc. Biol. 30, 139–143 (2010).
pubmed: 19797709
Endemann, G. et al. CD36 is a receptor for oxidized low density lipoprotein. J. Biol. Chem. 268, 11811–11816 (1993).
pubmed: 7685021
Rahaman, S. O. et al. A CD36-dependent signaling cascade is necessary for macrophage foam cell formation. Cell Metab. 4, 211–221 (2006).
pubmed: 16950138 pmcid: 1855263
Nicholson, A. C., Frieda, S., Pearce, A. & Silverstein, R. L. Oxidized LDL binds to CD36 on human monocyte-derived macrophages and transfected cell lines. Evidence implicating the lipid moiety of the lipoprotein as the binding site. Arterioscler. Thromb. Vasc. Biol. 15, 269–275 (1995).
pubmed: 7538425
Nozaki, S. et al. Reduced uptake of oxidized low density lipoproteins in monocyte-derived macrophages from CD36-deficient subjects. J. Clin. Invest. 96, 1859–1865 (1995).
pubmed: 7560077 pmcid: 185822
Febbraio, M. et al. Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice. J. Clin. Invest. 105, 1049–1056 (2000).
pubmed: 10772649 pmcid: 300837
Han, J., Hajjar, D. P., Febbraio, M. & Nicholson, A. C. Native and modified low density lipoproteins increase the functional expression of the macrophage class B scavenger receptor, CD36. J. Biol. Chem. 272, 21654–21659 (1997).
pubmed: 9261189
Smith, J., Su, X., El-Maghrabi, R., Stahl, P. D. & Abumrad, N. A. Opposite regulation of CD36 ubiquitination by fatty acids and insulin: effects on fatty acid uptake. J. Biol. Chem. 283, 13578–13585 (2008).
pubmed: 18353783 pmcid: 2376227
Sun, S. et al. Ubiquitinated CD36 sustains insulin-stimulated Akt activation by stabilizing insulin receptor substrate 1 in myotubes. J. Biol. Chem. 293, 2383–2394 (2018).
pubmed: 29269414
Zhang, F. et al. Inhibition of USP14 suppresses the formation of foam cell by promoting CD36 degradation. J. Cell Mol. Med. 24, 3292–3302 (2020).
pubmed: 31970862 pmcid: 7131911
D’Arcy, P. & Linder, S. Molecular pathways: translational potential of deubiquitinases as drug targets. Clin. Cancer Res. 20, 3908–3914 (2014).
pubmed: 25085788
Tian, Z. et al. A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. Blood 123, 706–716 (2014).
pubmed: 24319254 pmcid: 3907756
Larsen, C. N., Price, J. S. & Wilkinson, K. D. Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry 35, 6735–6744 (1996).
pubmed: 8639624
Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z. & Lansbury, P. T. Jr. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility. Cell 111, 209–218 (2002).
pubmed: 12408865
Setsuie, R. & Wada, K. The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem. Int. 51, 105–111 (2007).
pubmed: 17586089
Goto, Y. et al. UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating effect on HIF-1alpha. Nat. Commun. 6, 6153 (2015).
pubmed: 25615526 pmcid: 4317501
Hussain, S. et al. The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling. Leukemia 24, 1641–1655 (2010).
pubmed: 20574456 pmcid: 3236611
Jin, C. et al. UCHL1 is a putative tumor suppressor in ovarian cancer cells and contributes to cisplatin resistance. J. Cancer 4, 662–670 (2013).
pubmed: 24155778 pmcid: 3805994
Li, L. et al. The tumor suppressor UCHL1 forms a complex with p53/MDM2/ARF to promote p53 signaling and is frequently silenced in nasopharyngeal carcinoma. Clin. Cancer Res. 16, 2949–2958 (2010).
pubmed: 20395212
Ummanni, R. et al. Ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) is a potential tumour suppressor in prostate cancer and is frequently silenced by promoter methylation. Mol. Cancer 10, 129 (2011).
pubmed: 21999842 pmcid: 3212821
Zhong, J. et al. UCHL1 acts as a colorectal cancer oncogene via activation of the beta-catenin/TCF pathway through its deubiquitinating activity. Int. J. Mol. Med. 30, 430–436 (2012).
pubmed: 22641175
Nicholson, A. C., Han, J., Febbraio, M., Silversterin, R. L. & Hajjar, D. P. Role of CD36, the macrophage class B scavenger receptor, in atherosclerosis. Ann. N. Y. Acad. Sci. 947, 224–228 (2001).
pubmed: 11795270
Febbraio, M. & Silverstein, R. L. CD36: implications in cardiovascular disease. Int. J. Biochem. Cell Biol. 39, 2012–2030 (2007).
pubmed: 17466567 pmcid: 2034445
Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405–439 (1996).
pubmed: 8982460
Miranda, M. & Sorkin, A. Regulation of receptors and transporters by ubiquitination: new insights into surprisingly similar mechanisms. Mol. Interv. 7, 157–167 (2007).
pubmed: 17609522
Hu, M. et al. The harsh microenvironment in infarcted heart accelerates transplanted bone marrow mesenchymal stem cells injury: the role of injured cardiomyocytes-derived exosomes. Cell Death Dis. 9, 357 (2018).
pubmed: 29500342 pmcid: 5834521
Liao, Y. et al. Targeting GRP78-dependent AR-V7 protein degradation overcomes castration-resistance in prostate cancer therapy. Theranostics 10, 3366–3381 (2020).
pubmed: 32206096 pmcid: 7069092
Xia, X. et al. Deubiquitination and stabilization of estrogen receptor alpha by ubiquitin-specific protease 7 promotes breast tumorigenesis. Cancer Lett. 465, 118–128 (2019).
pubmed: 31518603
Liao, Y. et al. Proteasome-associated deubiquitinase ubiquitin-specific protease 14 regulates prostate cancer proliferation by deubiquitinating and stabilizing androgen receptor. Cell Death Dis. 8, e2585 (2017).
pubmed: 28151478 pmcid: 5386460
Liao, Y. et al. Growth arrest and apoptosis induction in androgen receptor-positive human breast cancer cells by inhibition of USP14-mediated androgen receptor deubiquitination. Oncogene 37, 1896–1910 (2018).
pubmed: 29353883 pmcid: 5886989
Liu, N. et al. Auranofin lethality to prostate cancer includes inhibition of proteasomal deubiquitinases and disrupted androgen receptor signaling. Eur. J. Pharmacol. 846, 1–11 (2019).
pubmed: 30639309
Xia, X. et al. Targeting proteasome-associated deubiquitinases as a novel strategy for the treatment of estrogen receptor-positive breast cancer. Oncogenesis 7, 75 (2018).
pubmed: 30250021 pmcid: 30250021
Liao, Y. et al. USP10 modulates the SKP2/Bcr-Abl axis via stabilizing SKP2 in chronic myeloid leukemia. Cell Discov. 5, 24 (2019).
pubmed: 31044085 pmcid: 6488640
Xu, R. et al. Exosomes derived from pro-inflammatory bone marrow-derived mesenchymal stem cells reduce inflammation and myocardial injury via mediating macrophage polarization. J. Cell Mol. Med. 23, 7617–7631 (2019).
pubmed: 31557396 pmcid: 6815833

Auteurs

Xiaohong Xia (X)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China.
Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Affiliated Cancer Hospital & Institute of Guangzhou Medical University, 511436, Guangzhou, China.

Qiong Xu (Q)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China.

Mingke Liu (M)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China.

Xuke Chen (X)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China.

Xiaolin Liu (X)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China.

Jinchan He (J)

Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Affiliated Cancer Hospital & Institute of Guangzhou Medical University, 511436, Guangzhou, China.

Tumei Hu (T)

Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Affiliated Cancer Hospital & Institute of Guangzhou Medical University, 511436, Guangzhou, China.

Cuifu Yu (C)

Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Affiliated Cancer Hospital & Institute of Guangzhou Medical University, 511436, Guangzhou, China.

Hongbiao Huang (H)

Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Affiliated Cancer Hospital & Institute of Guangzhou Medical University, 511436, Guangzhou, China.

Shiming Liu (S)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China. liushiming@gzhmu.edu.cn.

Ningning Liu (N)

Guangzhou Institute of Cardiovascular Disease, Guangdong Key Laboratory of Vascular Diseases, State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 510260, Guangzhou, China. liuningning@gzhmu.edu.cn.

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