Progress on the function and mechanism of pigment epithelium derived factor receptors in the occurrence and development of diabetic retinopathy_Chinese Journal of Ocular Fundus Diseases

Authors：

Xu Manhong , Chen Xin ,  Li Xiaorong

Tianjin Medical University Eye Hospital, Eye Institute and School of Optometry, Tianjin Key Laboratory of Retinal Functions and Diseases, Tianjin Branch of National Clinical Research Center for Ocular Disease, Tianjin 300384, China;

Corresponding author：

Li Xiaorong, Email: xiaorli@163.com

Keywords：

Diabetic retinopathy; Pigment epithelium-derived factor receptor; Review

DOI：

10.3760/cma.j.cn511434-20210803-00417

Video：

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Abstract Full text Figures/Tables Video References Cited by

Endogenous pigment epithelium derived factor (PEDF) shows great potential as a drug target for the treatment of diabetes retinopathy (DR) due to its anti-angiogenesis, anti-inflammatory, neuroprotective and neurotrophic effects. PEDF plays a biological role by combining with receptor proteins on cell membrane surface and regulating a variety of signaling pathways. Low density lipoprotein receptor related protein 6 plays a role in inhibiting oxidative stress reaction, inflammatory reaction, and neovascularization of DR. Adipose triglyceride lipase, laminin receptor, plexin domain containing 1 (PLXDC) 1, PLXDC2 and F₁-adenosine triphosphate synthase have the effect of promoting endothelial cell apoptosis, among which PLXDC1 also has neuroprotective effect. By clarifying the receptor that PEDF acts on, exploring the affinity between the receptor and PEDF, the difference in the expression level of each receptor in the process of disease, and the specific function that PEDF plays after binding with specific receptors, we can develop fusion protein drugs for the active domain of high affinity of receptors, have a clearer understanding of the pathogenesis of DR, and take PEDF or PEDF receptor as the target to consolidate the theoretical basis for the development of new therapeutic drugs and strategies for DR.

Citation： Xu Manhong, Chen Xin, Li Xiaorong. Progress on the function and mechanism of pigment epithelium derived factor receptors in the occurrence and development of diabetic retinopathy. Chinese Journal of Ocular Fundus Diseases, 2023, 39(3): 265-270. doi: 10.3760/cma.j.cn511434-20210803-00417 Copy

1.	Tombran-Tink J, Johnson LV. Neuronal differentiation of retinoblastoma cells induced by medium conditioned by human RPE cells[J]. Invest Ophthalmol Vis Sci, 1989, 30(8): 1700-1707.
2.	Steele FR, Chader GJ, Johnson LV, et al. Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family[J]. Proc Natl Acad Sci USA, 1993, 90(4): 1526-1530. DOI: 10.1073/pnas.90.4.1526.
3.	Dawson DW, Volpert OV, Gillis P, et al. Pigment epithelium-derived factor: a potent inhibitor of angiogenesis[J]. Science, 1999, 285(5425): 245-248. DOI: 10.1126/science.285.5425.245.
4.	Zhang SX, Wang JJ, Gao G, et al. Pigment epithelium-derived factor (PEDF) is an endogenous antiinflammatory factor[J]. FASEB J, 2006, 20(2): 323-325. DOI: 10.1096/fj.05-4313fje.
5.	Brown SD, Twells RC, Hey PJ, et al. Isolation and characterization of LRP6, a novel member of the low density lipoprotein receptor gene family[J]. Biochem Biophys Res Commun, 1998, 248(3): 879-888. DOI: 10.1006/bbrc.1998.9061.
6.	Hey PJ, Twells RC, Phillips MS, et al. Cloning of a novel member of the low-density lipoprotein receptor family[J]. Gene, 1998, 216(1): 103-111. DOI: 10.1016/s0378-1119(98)00311-4.
7.	Wang ZM, Luo JQ, Xu LY, et al. Harnessing low-density lipoprotein receptor protein 6 (LRP6) genetic variation and Wnt signaling for innovative diagnostics in complex diseases[J]. Pharmacogenomics J, 2018, 18(3): 351-358. DOI: 10.1038/tpj.2017.28.
8.	Nie X, Wei X, Ma H, et al. The complex role of Wnt ligands in type 2 diabetes mellitus and related complications[J]. J Cell Mol Med, 2021, 25(14): 6479-6495. DOI: 10.1111/jcmm.16663.
9.	Kang S. Low-density lipoprotein receptor-related protein 6-mediated signaling pathways and associated cardiovascular diseases: diagnostic and therapeutic opportunities[J]. Hum Genet, 2020, 139(4): 447-459. DOI: 10.1007/s00439-020-02124-8.
10.	Park K, Lee K, Zhang B, et al. Identification of a novel inhibitor of the canonical Wnt pathway[J]. Mol Cell Biol, 2011, 31(14): 3038-3051. DOI: 10.1128/MCB.01211-10.
11.	Chen Y, Hu Y, Zhou T, et al. Activation of the Wnt pathway plays a pathogenic role in diabetic retinopathy in humans and animal models[J]. Am J Pathol, 2009, 175(6): 2676-2685. DOI: 10.2353/ajpath.2009.080945.
12.	Zhou T, Hu Y, Chen Y, et al. The pathogenic role of the canonical Wnt pathway in age-related macular degeneration[J]. Invest Ophthalmol Vis Sci, 2010, 51(9): 4371-4379. DOI: 10.1167/iovs.09-4278.
13.	Lee K, Hu Y, Ding L, et al. Therapeutic potential of a monoclonal antibody blocking the Wnt pathway in diabetic retinopathy[J]. Diabetes, 2012, 61(11): 2948-2957. DOI: 10.2337/db11-0300.
14.	Zhang B, Zhou KK, Ma JX. Inhibition of connective tissue growth factor overexpression in diabetic retinopathy by SERPINA3K via blocking the WNT/beta-catenin pathway[J]. Diabetes, 2010, 59(7): 1809-1816. DOI: 10.2337/db09-1056.
15.	Zuercher J, Fritzsche M, Feil S, et al. Norrin stimulates cell proliferation in the superficial retinal vascular plexus and is pivotal for the recruitment of mural cells[J]. Hum Mol Genet, 2012, 21(12): 2619-2630. DOI: 10.1093/hmg/dds087.
16.	Chen J, Stahl A, Krah NM, et al. Wnt signaling mediates pathological vascular growth in proliferative retinopathy[J]. Circulation, 2011, 124(17): 1871-1881. DOI: 10.1161/CIRCULATIONAHA.111.040337.
17.	Zimmermann R, Strauss JG, Haemmerle G, et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase[J]. Science, 2004, 306(5700): 1383-1386. DOI: 10.1126/science.1100747.
18.	Jenkins CM, Mancuso DJ, Yan W, et al. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities[J]. J Biol Chem, 2004, 279(47): 48968-48975. DOI: 10.1074/jbc.M407841200.
19.	Villena JA, Roy S, Sarkadi-Nagy E, et al. Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis[J]. J Biol Chem, 2004, 279(45): 47066-47075. DOI: 10.1074/jbc.M403855200.
20.	Al-Zoughbi W, Pichler M, Gorkiewicz G, et al. Loss of adipose triglyceride lipase is associated with human cancer and induces mouse pulmonary neoplasia[J]. Oncotarget, 2016, 7(23): 33832-33840. DOI: 10.18632/oncotarget.9418.
21.	Notari L, Baladron V, Aroca-Aguilar JD, et al. Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor[J]. J Biol Chem, 2006, 281(49): 38022-38037. DOI: 10.1074/jbc.M600353200.
22.	Alberdi E, Aymerich MS, Becerra SP. Binding of pigment epithelium-derived factor (PEDF) to retinoblastoma cells and cerebellar granule neurons. Evidence for a PEDF receptor[J]. J Biol Chem, 1999, 274(44): 31605-31612. DOI: 10.1074/jbc.274.44.31605.
23.	Desjardin JT, Becerra SP, Subramanian P. Searching for alternatively spliced variants of phospholipase domain-containing 2 (Pnpla2), a novel gene in the retina[J]. J Clin Exp Ophthalmol, 2013, 4(5): 295. DOI: 10.4172/2155-9570.1000295.
24.	Subramanian P, Notario PM, Becerra SP. Pigment epithelium-derived factor receptor (PEDF-R): a plasma membrane-linked phospholipase with PEDF binding affinity[J]. Adv Exp Med Biol, 2010, 664: 29-37. DOI: 10.1007/978-1-4419-1399-9_4.
25.	Schreiber R, Xie H, Schweiger M. Of mice and men: the physiological role of adipose triglyceride lipase (ATGL)[J]. Biochim Biophys Acta Mol Cell Biol Lipids, 2019, 1864(6): 880-899. DOI: 10.1016/j.bbalip.2018.10.008.
26.	Schreiber R, Hofer P, Taschler U, et al. Hypophagia and metabolic adaptations in mice with defective ATGL-mediated lipolysis cause resistance to HFD-induced obesity[J]. Proc Natl Acad Sci USA, 2015, 112(45): 13850-13855. DOI: 10.1073/pnas.1516004112.
27.	Pesapane A, Di Giovanni C, Rossi FW, et al. Discovery of new small molecules inhibiting 67 kDa laminin receptor interaction with laminin and cancer cell invasion[J]. Oncotarget, 2015, 6(20): 18116-18133. DOI: 10.18632/oncotarget.4016.
28.	Chung C, Doll JA, Gattu AK, et al. Anti-angiogenic pigment epithelium-derived factor regulates hepatocyte triglyceride content through adipose triglyceride lipase (ATGL)[J]. J Hepatol, 2008, 48(3): 471-478. DOI: 10.1016/j.jhep.2007.10.012.
29.	Borg ML, Andrews ZB, Duh EJ, et al. Pigment epithelium-derived factor regulates lipid metabolism via adipose triglyceride lipase[J]. Diabetes, 2011, 60(5): 1458-1466. DOI: 10.2337/db10-0845.
30.	Niyogi S, Ghosh M, Adak M, et al. PEDF promotes nuclear degradation of ATGL through COP1[J]. Biochem Biophys Res Commun, 2019, 512(4): 806-811. DOI: 10.1016/j.bbrc.2019.03.111.
31.	Yang Z, Sun J, Ji H, et al. Pigment epithelium-derived factor improves TNFα-induced hepatic steatosis in grass carp (Ctenopharyngodon idella)[J]. Dev Comp Immunol, 2017, 71: 8-17. DOI: 10.1016/j.dci.2017.01.016.
32.	Zhang H, Sun T, Jiang X, et al. PEDF and PEDF-derived peptide 44mer stimulate cardiac triglyceride degradation via ATGL[J]. J Transl Med, 2015, 13: 68. DOI: 10.1186/s12967-015-0432-1.
33.	Hirsch J, Johnson CL, Nelius T, et al. PEDF inhibits IL8 production in prostate cancer cells through PEDF receptor/phospholipase A2 and regulation of NFκB and PPARγ[J]. Cytokine, 2011, 55(2): 202-210. DOI: 10.1016/j.cyto.2011.04.010.
34.	Aurora AB, Biyashev D, Mirochnik Y, et al. NF-kappaB balances vascular regression and angiogenesis via chromatin remodeling and NFAT displacement[J]. Blood, 2010, 116(3): 475-484. DOI: 10.1182/blood-2009-07-232132.
35.	DiGiacomo V, Meruelo D. Looking into laminin receptor: critical discussion regarding the non-integrin 37/67-kDa laminin receptor/RPSA protein[J]. Biol Rev Camb Philos Soc, 2016, 91(2): 288-310. DOI: 10.1111/brv.12170.
36.	Pesapane A, Ragno P, Selleri C, et al. Recent advances in the function of the 67 kDa laminin receptor and its targeting for personalized therapy in cancer[J]. Curr Pharm Des, 2017, 23(32): 4745-4757. DOI: 10.2174/1381612823666170710125332.
37.	Sheibani N, Wang S, Darjatmoko SR, et al. Novel anti-angiogenic PEDF-derived small peptides mitigate choroidal neovascularization[J/OL]. Exp Eye Res, 2019, 188: 107798[2019-09-11]. https://pubmed.ncbi.nlm.nih.gov/31520600/. DOI: 10.1016/j.exer.2019.107798.
38.	Sheibani N, Zaitoun IS, Wang S, et al. Inhibition of retinal neovascularization by a PEDF-derived nonapeptide in newborn mice subjected to oxygen-induced ischemic retinopathy[J/OL]. Exp Eye Res, 2020, 195: 108030[2020-04-06]. https://pubmed.ncbi.nlm.nih.gov/32272114/. DOI: 10.1016/j.exer.2020.108030.
39.	Bernard A, Gao-Li J, Franco CA, et al. Laminin receptor involvement in the anti-angiogenic activity of pigment epithelium-derived factor[J]. J Biol Chem, 2009, 284(16): 10480-10490. DOI: 10.1074/jbc.M809259200.
40.	Gong Q, Qiu S, Li S, et al. Proapoptotic PEDF functional peptides inhibit prostate tumor growth-a mechanistic study[J]. Biochem Pharmacol, 2014, 92(3): 425-437. DOI: 10.1016/j.bcp.2014.09.012.
41.	Carson-Walter EB, Watkins DN, Nanda A, et al. Cell surface tumor endothelial markers are conserved in mice and humans[J]. Cancer Res, 2001, 61(18): 6649-6655.
42.	Lee HK, Seo IA, Park HK, et al. Identification of the basement membrane protein nidogen as a candidate ligand for tumor endothelial marker 7 in vitro and in vivo[J]. FEBS Lett, 2006, 580(9): 2253-2257. DOI: 10.1016/j.febslet.2006.03.033.
43.	Nanda A, Buckhaults P, Seaman S, et al. Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R[J]. Cancer Res, 2004, 64(23): 8507-8511. DOI: 10.1158/0008-5472.CAN-04-2716.
44.	Beaty RM, Edwards JB, Boon K, et al. PLXDC1 (TEM7) is identified in a genome-wide expression screen of glioblastoma endothelium[J]. J Neurooncol, 2007, 81(3): 241-248. DOI: 10.1007/s11060-006-9227-9.
45.	Cheng G, Zhong M, Kawaguchi R, et al. Identification of PLXDC1 and PLXDC2 as the transmembrane receptors for the multifunctional factor PEDF[J/OL]. Elife, 2014, 3: e05401[2014-12-23]. https://pubmed.ncbi.nlm.nih.gov/25535841/. DOI: 10.7554/eLife.05401.
46.	Nirody JA, Budin I, Rangamani P. ATP synthase: evolution, energetics, and membrane interactions[J/OL]. J Gen Physiol, 2020, 152(11): e201912475[2020-11-02]. https://pubmed.ncbi.nlm.nih.gov/32966553/. DOI: 10.1085/jgp.201912475.
47.	Champagne E, Martinez LO, Collet X, et al. Ecto-F1Fo ATP synthase/F1 ATPase: metabolic and immunological functions[J]. Curr Opin Lipidol, 2006, 17(3): 279-284. DOI: 10.1097/01.mol.0000226120.27931.76.
48.	Notari L, Arakaki N, Mueller D, et al. Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase[J]. FEBS J, 2010, 277(9): 2192-2205. DOI: 10.1111/j.1742-4658.2010.07641.x.
49.	Qiu F, Zhang H, Yuan Y, et al. A decrease of ATP production steered by PEDF in cardiomyocytes with oxygen-glucose deprivation is associated with an AMPK-dependent degradation pathway[J]. Int J Cardiol, 2018, 257: 262-271. DOI: 10.1016/j.ijcard.2018.01.034.

1. Tombran-Tink J, Johnson LV. Neuronal differentiation of retinoblastoma cells induced by medium conditioned by human RPE cells[J]. Invest Ophthalmol Vis Sci, 1989, 30(8): 1700-1707.
2. Steele FR, Chader GJ, Johnson LV, et al. Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family[J]. Proc Natl Acad Sci USA, 1993, 90(4): 1526-1530. DOI: 10.1073/pnas.90.4.1526.
3. Dawson DW, Volpert OV, Gillis P, et al. Pigment epithelium-derived factor: a potent inhibitor of angiogenesis[J]. Science, 1999, 285(5425): 245-248. DOI: 10.1126/science.285.5425.245.
4. Zhang SX, Wang JJ, Gao G, et al. Pigment epithelium-derived factor (PEDF) is an endogenous antiinflammatory factor[J]. FASEB J, 2006, 20(2): 323-325. DOI: 10.1096/fj.05-4313fje.
5. Brown SD, Twells RC, Hey PJ, et al. Isolation and characterization of LRP6, a novel member of the low density lipoprotein receptor gene family[J]. Biochem Biophys Res Commun, 1998, 248(3): 879-888. DOI: 10.1006/bbrc.1998.9061.
6. Hey PJ, Twells RC, Phillips MS, et al. Cloning of a novel member of the low-density lipoprotein receptor family[J]. Gene, 1998, 216(1): 103-111. DOI: 10.1016/s0378-1119(98)00311-4.
7. Wang ZM, Luo JQ, Xu LY, et al. Harnessing low-density lipoprotein receptor protein 6 (LRP6) genetic variation and Wnt signaling for innovative diagnostics in complex diseases[J]. Pharmacogenomics J, 2018, 18(3): 351-358. DOI: 10.1038/tpj.2017.28.
8. Nie X, Wei X, Ma H, et al. The complex role of Wnt ligands in type 2 diabetes mellitus and related complications[J]. J Cell Mol Med, 2021, 25(14): 6479-6495. DOI: 10.1111/jcmm.16663.
9. Kang S. Low-density lipoprotein receptor-related protein 6-mediated signaling pathways and associated cardiovascular diseases: diagnostic and therapeutic opportunities[J]. Hum Genet, 2020, 139(4): 447-459. DOI: 10.1007/s00439-020-02124-8.
10. Park K, Lee K, Zhang B, et al. Identification of a novel inhibitor of the canonical Wnt pathway[J]. Mol Cell Biol, 2011, 31(14): 3038-3051. DOI: 10.1128/MCB.01211-10.
11. Chen Y, Hu Y, Zhou T, et al. Activation of the Wnt pathway plays a pathogenic role in diabetic retinopathy in humans and animal models[J]. Am J Pathol, 2009, 175(6): 2676-2685. DOI: 10.2353/ajpath.2009.080945.
12. Zhou T, Hu Y, Chen Y, et al. The pathogenic role of the canonical Wnt pathway in age-related macular degeneration[J]. Invest Ophthalmol Vis Sci, 2010, 51(9): 4371-4379. DOI: 10.1167/iovs.09-4278.
13. Lee K, Hu Y, Ding L, et al. Therapeutic potential of a monoclonal antibody blocking the Wnt pathway in diabetic retinopathy[J]. Diabetes, 2012, 61(11): 2948-2957. DOI: 10.2337/db11-0300.
14. Zhang B, Zhou KK, Ma JX. Inhibition of connective tissue growth factor overexpression in diabetic retinopathy by SERPINA3K via blocking the WNT/beta-catenin pathway[J]. Diabetes, 2010, 59(7): 1809-1816. DOI: 10.2337/db09-1056.
15. Zuercher J, Fritzsche M, Feil S, et al. Norrin stimulates cell proliferation in the superficial retinal vascular plexus and is pivotal for the recruitment of mural cells[J]. Hum Mol Genet, 2012, 21(12): 2619-2630. DOI: 10.1093/hmg/dds087.
16. Chen J, Stahl A, Krah NM, et al. Wnt signaling mediates pathological vascular growth in proliferative retinopathy[J]. Circulation, 2011, 124(17): 1871-1881. DOI: 10.1161/CIRCULATIONAHA.111.040337.
17. Zimmermann R, Strauss JG, Haemmerle G, et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase[J]. Science, 2004, 306(5700): 1383-1386. DOI: 10.1126/science.1100747.
18. Jenkins CM, Mancuso DJ, Yan W, et al. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities[J]. J Biol Chem, 2004, 279(47): 48968-48975. DOI: 10.1074/jbc.M407841200.
19. Villena JA, Roy S, Sarkadi-Nagy E, et al. Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis[J]. J Biol Chem, 2004, 279(45): 47066-47075. DOI: 10.1074/jbc.M403855200.
20. Al-Zoughbi W, Pichler M, Gorkiewicz G, et al. Loss of adipose triglyceride lipase is associated with human cancer and induces mouse pulmonary neoplasia[J]. Oncotarget, 2016, 7(23): 33832-33840. DOI: 10.18632/oncotarget.9418.
21. Notari L, Baladron V, Aroca-Aguilar JD, et al. Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor[J]. J Biol Chem, 2006, 281(49): 38022-38037. DOI: 10.1074/jbc.M600353200.
22. Alberdi E, Aymerich MS, Becerra SP. Binding of pigment epithelium-derived factor (PEDF) to retinoblastoma cells and cerebellar granule neurons. Evidence for a PEDF receptor[J]. J Biol Chem, 1999, 274(44): 31605-31612. DOI: 10.1074/jbc.274.44.31605.
23. Desjardin JT, Becerra SP, Subramanian P. Searching for alternatively spliced variants of phospholipase domain-containing 2 (Pnpla2), a novel gene in the retina[J]. J Clin Exp Ophthalmol, 2013, 4(5): 295. DOI: 10.4172/2155-9570.1000295.
24. Subramanian P, Notario PM, Becerra SP. Pigment epithelium-derived factor receptor (PEDF-R): a plasma membrane-linked phospholipase with PEDF binding affinity[J]. Adv Exp Med Biol, 2010, 664: 29-37. DOI: 10.1007/978-1-4419-1399-9_4.
25. Schreiber R, Xie H, Schweiger M. Of mice and men: the physiological role of adipose triglyceride lipase (ATGL)[J]. Biochim Biophys Acta Mol Cell Biol Lipids, 2019, 1864(6): 880-899. DOI: 10.1016/j.bbalip.2018.10.008.
26. Schreiber R, Hofer P, Taschler U, et al. Hypophagia and metabolic adaptations in mice with defective ATGL-mediated lipolysis cause resistance to HFD-induced obesity[J]. Proc Natl Acad Sci USA, 2015, 112(45): 13850-13855. DOI: 10.1073/pnas.1516004112.
27. Pesapane A, Di Giovanni C, Rossi FW, et al. Discovery of new small molecules inhibiting 67 kDa laminin receptor interaction with laminin and cancer cell invasion[J]. Oncotarget, 2015, 6(20): 18116-18133. DOI: 10.18632/oncotarget.4016.
28. Chung C, Doll JA, Gattu AK, et al. Anti-angiogenic pigment epithelium-derived factor regulates hepatocyte triglyceride content through adipose triglyceride lipase (ATGL)[J]. J Hepatol, 2008, 48(3): 471-478. DOI: 10.1016/j.jhep.2007.10.012.
29. Borg ML, Andrews ZB, Duh EJ, et al. Pigment epithelium-derived factor regulates lipid metabolism via adipose triglyceride lipase[J]. Diabetes, 2011, 60(5): 1458-1466. DOI: 10.2337/db10-0845.
30. Niyogi S, Ghosh M, Adak M, et al. PEDF promotes nuclear degradation of ATGL through COP1[J]. Biochem Biophys Res Commun, 2019, 512(4): 806-811. DOI: 10.1016/j.bbrc.2019.03.111.
31. Yang Z, Sun J, Ji H, et al. Pigment epithelium-derived factor improves TNFα-induced hepatic steatosis in grass carp (Ctenopharyngodon idella)[J]. Dev Comp Immunol, 2017, 71: 8-17. DOI: 10.1016/j.dci.2017.01.016.
32. Zhang H, Sun T, Jiang X, et al. PEDF and PEDF-derived peptide 44mer stimulate cardiac triglyceride degradation via ATGL[J]. J Transl Med, 2015, 13: 68. DOI: 10.1186/s12967-015-0432-1.
33. Hirsch J, Johnson CL, Nelius T, et al. PEDF inhibits IL8 production in prostate cancer cells through PEDF receptor/phospholipase A2 and regulation of NFκB and PPARγ[J]. Cytokine, 2011, 55(2): 202-210. DOI: 10.1016/j.cyto.2011.04.010.
34. Aurora AB, Biyashev D, Mirochnik Y, et al. NF-kappaB balances vascular regression and angiogenesis via chromatin remodeling and NFAT displacement[J]. Blood, 2010, 116(3): 475-484. DOI: 10.1182/blood-2009-07-232132.
35. DiGiacomo V, Meruelo D. Looking into laminin receptor: critical discussion regarding the non-integrin 37/67-kDa laminin receptor/RPSA protein[J]. Biol Rev Camb Philos Soc, 2016, 91(2): 288-310. DOI: 10.1111/brv.12170.
36. Pesapane A, Ragno P, Selleri C, et al. Recent advances in the function of the 67 kDa laminin receptor and its targeting for personalized therapy in cancer[J]. Curr Pharm Des, 2017, 23(32): 4745-4757. DOI: 10.2174/1381612823666170710125332.
37. Sheibani N, Wang S, Darjatmoko SR, et al. Novel anti-angiogenic PEDF-derived small peptides mitigate choroidal neovascularization[J/OL]. Exp Eye Res, 2019, 188: 107798[2019-09-11]. https://pubmed.ncbi.nlm.nih.gov/31520600/. DOI: 10.1016/j.exer.2019.107798.
38. Sheibani N, Zaitoun IS, Wang S, et al. Inhibition of retinal neovascularization by a PEDF-derived nonapeptide in newborn mice subjected to oxygen-induced ischemic retinopathy[J/OL]. Exp Eye Res, 2020, 195: 108030[2020-04-06]. https://pubmed.ncbi.nlm.nih.gov/32272114/. DOI: 10.1016/j.exer.2020.108030.
39. Bernard A, Gao-Li J, Franco CA, et al. Laminin receptor involvement in the anti-angiogenic activity of pigment epithelium-derived factor[J]. J Biol Chem, 2009, 284(16): 10480-10490. DOI: 10.1074/jbc.M809259200.
40. Gong Q, Qiu S, Li S, et al. Proapoptotic PEDF functional peptides inhibit prostate tumor growth-a mechanistic study[J]. Biochem Pharmacol, 2014, 92(3): 425-437. DOI: 10.1016/j.bcp.2014.09.012.
41. Carson-Walter EB, Watkins DN, Nanda A, et al. Cell surface tumor endothelial markers are conserved in mice and humans[J]. Cancer Res, 2001, 61(18): 6649-6655.
42. Lee HK, Seo IA, Park HK, et al. Identification of the basement membrane protein nidogen as a candidate ligand for tumor endothelial marker 7 in vitro and in vivo[J]. FEBS Lett, 2006, 580(9): 2253-2257. DOI: 10.1016/j.febslet.2006.03.033.
43. Nanda A, Buckhaults P, Seaman S, et al. Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R[J]. Cancer Res, 2004, 64(23): 8507-8511. DOI: 10.1158/0008-5472.CAN-04-2716.
44. Beaty RM, Edwards JB, Boon K, et al. PLXDC1 (TEM7) is identified in a genome-wide expression screen of glioblastoma endothelium[J]. J Neurooncol, 2007, 81(3): 241-248. DOI: 10.1007/s11060-006-9227-9.
45. Cheng G, Zhong M, Kawaguchi R, et al. Identification of PLXDC1 and PLXDC2 as the transmembrane receptors for the multifunctional factor PEDF[J/OL]. Elife, 2014, 3: e05401[2014-12-23]. https://pubmed.ncbi.nlm.nih.gov/25535841/. DOI: 10.7554/eLife.05401.
46. Nirody JA, Budin I, Rangamani P. ATP synthase: evolution, energetics, and membrane interactions[J/OL]. J Gen Physiol, 2020, 152(11): e201912475[2020-11-02]. https://pubmed.ncbi.nlm.nih.gov/32966553/. DOI: 10.1085/jgp.201912475.
47. Champagne E, Martinez LO, Collet X, et al. Ecto-F1Fo ATP synthase/F1 ATPase: metabolic and immunological functions[J]. Curr Opin Lipidol, 2006, 17(3): 279-284. DOI: 10.1097/01.mol.0000226120.27931.76.
48. Notari L, Arakaki N, Mueller D, et al. Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase[J]. FEBS J, 2010, 277(9): 2192-2205. DOI: 10.1111/j.1742-4658.2010.07641.x.
49. Qiu F, Zhang H, Yuan Y, et al. A decrease of ATP production steered by PEDF in cardiomyocytes with oxygen-glucose deprivation is associated with an AMPK-dependent degradation pathway[J]. Int J Cardiol, 2018, 257: 262-271. DOI: 10.1016/j.ijcard.2018.01.034.

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