Association Between Progranulin and Gaucher Disease

EBioMedicine

Volumn 11, Issue , 2016, Pages 127-137

  Jian, Jinlong ^a   Zhao, Shuai ^a   Tian, Qing Yun ^a   Liu, Helen ^a   Zhao, Yunpeng ^a   Chen, Wen Chi ^a   Grunig, Gabriele ^a   Torres, Paola A ^a   Wang, Betty C ^a   Zeng, Bai ^a   Pastores, Gregory ^a   Tang, Wei ^b   Sun, Ying ^c   Grabowski, Gregory A ^c   Kong, Max Xiangtian ^d   Wang, Guilin ^e   Chen, Ying ^f   Liang, Fengxia ^a   Overkleeft, Herman S ^g   Saunders Pullman, Rachel ^h   Chan, Gerald L ⁱ   Liu, Chuan ju ^a   more..

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SHANDONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^c CINCINNATI CHILDREN'S HOSPITAL MEDICAL CENTER   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^e YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f NEW YORK STATE PSYCHIATRIC INSTITUTE   (United States)

^g LEIDEN UNIVERSITY   (Netherlands)

^h BETH ISRAEL MEDICAL CENTER   (United States)

ⁱ HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

Gaucher disease; Lysosomal storage diseases; Progranulin; Glucocerebrosidase

Indexed keywords

GENOMIC DNA; IMIGLUCERASE; PROGRANULIN; RECOMBINANT PROGRANULIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; GRN PROTEIN, HUMAN; SIGNAL PEPTIDE;

ADULT; AGED; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ASHKENAZI JEW; BONE MARROW; CONFOCAL MICROSCOPY; CONTROLLED STUDY; DISEASE ASSOCIATION; FEMALE; FLOW CYTOMETRY; GAUCHER DISEASE; GENE; GENE AMPLIFICATION; GENE EXPRESSION; GENE SEQUENCE; GENOTYPE; HUMAN; IMMUNOFLUORESCENCE TEST; IMMUNOHISTOCHEMISTRY; LUNG; LYSOSOME; MAJOR CLINICAL STUDY; MALE; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROGRANULIN GENE; PROTEIN BLOOD LEVEL; SINGLE NUCLEOTIDE POLYMORPHISM; SPLEEN; TRANSMISSION ELECTRON MICROSCOPY; ALLELE; ANIMAL; BLOOD; CASE CONTROL STUDY; DISEASE MODEL; ENZYME ACTIVATION; GENE FREQUENCY; GENETIC ASSOCIATION STUDY; GENETICS; KNOCKOUT MOUSE; METABOLISM; MIDDLE AGED; MUTATION; PHENOTYPE; PROTEIN TRANSPORT;

ADULT; AGED; ALLELES; ANIMALS; CASE-CONTROL STUDIES; DISEASE MODELS, ANIMAL; ENZYME ACTIVATION; FEMALE; GAUCHER DISEASE; GENE FREQUENCY; GENETIC ASSOCIATION STUDIES; GENOTYPE; HUMANS; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; LYSOSOMES; MALE; MICE; MICE, KNOCKOUT; MIDDLE AGED; MUTATION; PHENOTYPE; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN TRANSPORT;

EID: 84994832035     PISSN: None     EISSN: 23523964     Source Type: Journal    
DOI: 10.1016/j.ebiom.2016.08.004     Document Type: Article

References (32)

1. Aerts, J.M., Kallemeijn, W.W., Wegdam, W., Joa Oferraz, M., Van Breemen, M.J., Dekker, N., Kramer, G., Poorthuis, B.J., Groener, J.E., Cox-Brinkman, J., Rombach, S.M., Hollak, C.E., Linthorst, G.E., Witte, M.D., Gold, H., Van Der Marel, G.A., Overkleeft, H.S., Boot, R.G., Biomarkers in the diagnosis of lysosomal storage disorders: proteins, lipids, and inhibodies. J. Inherit. Metab. Dis. 34 (2011), 605–619.
2. Baker, M., Mackenzie, I.R., Pickering-Brown, S.M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A.D., Rollinson, S., Cannon, A., Dwosh, E., Neary, D., Melquist, S., Richardson, A., Dickson, D., Berger, Z., Eriksen, J., Robinson, T., Zehr, C., Dickey, C.A., Crook, R., Mcgowan, E., Mann, D., Boeve, B., Feldman, H., Hutton, M., Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature 442 (2006), 916–919.
3. Barnes, S., Xu, Y.H., Zhang, W., Liou, B., Setchell, K.D., Bao, L., Grabowski, G.A., Sun, Y., Ubiquitous transgene expression of the glucosylceramide-synthesizing enzyme accelerates glucosylceramide accumulation and storage cells in a Gaucher disease mouse model. PLoS One, 9, 2014, e116023.
4. Biegstraaten, M., Van Schaik, I.N., Aerts, J.M., Langeveld, M., Mannens, M.M., Bour, L.J., Sidransky, E., Tayebi, N., Fitzgibbon, E., Hollak, C.E., A monozygotic twin pair with highly discordant Gaucher phenotypes. Blood Cells Mol. Dis. 46 (2011), 39–41.
5. Cruts, M., Gijselinck, I., Van Der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.J., Van Duijn, C., Peeters, K., Sciot, R., Santens, P., De Pooter, T., Mattheijssens, M., Van Den Broeck, M., Cuijt, I., Vennekens, K., De Deyn, P.P., Kumar-Singh, S., Van Broeckhoven, C., Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature 442 (2006), 920–924.
6. Daley, E., Emson, C., Guignabert, C., De Waal Malefyt, R., Louten, J., Kurup, V.P., Hogaboam, C., Taraseviciene-Stewart, L., Voelkel, N.F., Rabinovitch, M., Grunig, E., Grunig, G., Pulmonary arterial remodeling induced by a Th2 immune response. J. Exp. Med. 205 (2008), 361–372.
7. Eid, J., Fehr, A., Gray, J., Luong, K., Lyle, J., Otto, G., Peluso, P., Rank, D., Baybayan, P., Bettman, B., Bibillo, A., Bjornson, K., Chaudhuri, B., Christians, F., Cicero, R., Clark, S., Dalal, R., Dewinter, A., Dixon, J., Foquet, M., Gaertner, A., Hardenbol, P., Heiner, C., Hester, K., Holden, D., Kearns, G., Kong, X., Kuse, R., Lacroix, Y., Lin, S., Lundquist, P., Ma, C., Marks, P., Maxham, M., Murphy, D., Park, I., Pham, T., Phillips, M., Roy, J., Sebra, R., Shen, G., Sorenson, J., Tomaney, A., Travers, K., Trulson, M., Vieceli, J., Wegener, J., Wu, D., Yang, A., Zaccarin, D., Zhao, P., Zhong, F., Korlach, J., Turner, S., Real-time DNA sequencing from single polymerase molecules. Science 323 (2009), 133–138.
8. Elstein, D., Gellman, A., Altarescu, G., Abrahamov, A., Hadas-Halpern, I., Phillips, M., Margalit, M., Lebel, E., Itzchaki, M., Zimran, A., Disease severity in sibling pairs with type 1 Gaucher disease. J. Inherit. Metab. Dis. 33 (2010), 79–83.
9. Fabrega, S., Durand, P., Codogno, P., Bauvy, C., Delomenie, C., Henrissat, B., Martin, B.M., Mckinney, C., Ginns, E.I., Mornon, J.P., Lehn, P., Human glucocerebrosidase: heterologous expression of active site mutants in murine null cells. Glycobiology 10 (2000), 1217–1224.
10. Farfel-Becker, T., Vitner, E.B., Futerman, A.H., Animal models for Gaucher disease research. Dis. Model. Mech. 4 (2011), 746–752.
11. Gaspar, P., Kallemeijn, W.W., Strijland, A., Scheij, S., Van Eijk, M., Aten, J., Overkleeft, H.S., Balreira, A., Zunke, F., Schwake, M., Sa Miranda, C., Aerts, J.M., Action myoclonus-renal failure syndrome: diagnostic applications of activity-based probes and lipid analysis. J. Lipid Res. 55 (2014), 138–145.
12. Ghidoni, R., Stoppani, E., Rossi, G., Piccoli, E., Albertini, V., Paterlini, A., Glionna, M., Pegoiani, E., Agnati, L.F., Fenoglio, C., Scarpini, E., Galimberti, D., Morbin, M., Tagliavini, F., Binetti, G., Benussi, L., Optimal plasma progranulin cutoff value for predicting null progranulin mutations in neurodegenerative diseases: a multicenter Italian study. Neurodegener. Dis. 9 (2012), 121–127.
13. Gotzl, J.K., Mori, K., Damme, M., Fellerer, K., Tahirovic, S., Kleinberger, G., Janssens, J., Van Der Zee, J., Lang, C.M., Kremmer, E., Martin, J.J., Engelborghs, S., Kretzschmar, H.A., Arzberger, T., Van Broeckhoven, C., Haass, C., Capell, A., Common pathobiochemical hallmarks of progranulin-associated frontotemporal lobar degeneration and neuronal ceroid lipofuscinosis. Acta Neuropathol. 127 (2014), 845–860.
14. Grabowski, G.A., Gaucher Disease and Other Storage Disorders. Hematology Am Soc Hematol Educ Program, 2012. 2012, 13–18.
15. He, Z., Bateman, A., Progranulin (granulin-epithelin precursor, PC-cell-derived growth factor, acrogranin) mediates tissue repair and tumorigenesis. J. Mol. Med. 81 (2003), 600–612.
16. He, Z., Ong, C.H., Halper, J., Bateman, A., Progranulin is a mediator of the wound response. Nat. Med. 9 (2003), 225–229.
17. Hu, X., Paik, P.K., Chen, J., Yarilina, A., Kockeritz, L., Lu, T.T., Woodgett, J.R., Ivashkiv, L.B., IFN-gamma suppresses IL-10 production and synergizes with TLR2 by regulating GSK3 and CREB/AP-1 proteins. Immunity 24 (2006), 563–574.
18. Jian, J., Konopka, J., Liu, C., Insights into the role of progranulin in immunity, infection, and inflammation. J. Leukoc. Biol. 93 (2013), 199–208.
19. Jian, J., Zhao, S., Tian, Q., Gonzalez-Gugel, E., Mundra, J.J., Uddin, S.M., Liu, B., Richbourgh, B., Brunetti, R., Liu, C.J., Progranulin directly binds to the CRD2 and CRD3 of TNFR extracellular domains. FEBS Lett. 587 (2013), 3428–3436.
20. Leverenz, J.B., Yu, C.E., Montine, T.J., Steinbart, E., Bekris, L.M., Zabetian, C., Kwong, L.K., Lee, V.M., Schellenberg, G.D., Bird, T.D., A novel progranulin mutation associated with variable clinical presentation and tau, TDP43 and alpha-synuclein pathology. Brain 130 (2007), 1360–1374.
21. Liou, B., Kazimierczuk, A., Zhang, M., Scott, C.R., Hegde, R.S., Grabowski, G.A., Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations. J. Biol. Chem. 281 (2006), 4242–4253.
22. Mateo, I., Gonzalez-Aramburu, I., Pozueta, A., Vazquez-Higuera, J.L., Rodriguez-Rodriguez, E., Sanchez-Juan, P., Calero, M., Dobato, J.L., Infante, J., Berciano, J., Combarros, O., Reduced serum progranulin level might be associated with Parkinson's disease risk. Eur. J. Neurol. 20 (2013), 1571–1573.
23. Mazzulli, J.R., Xu, Y.H., Sun, Y., Knight, A.L., Mclean, P.J., Caldwell, G.A., Sidransky, E., Grabowski, G.A., Krainc, D., Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 146 (2011), 37–52.
24. Migdalska-Richards, A., Schapira, A.H., The relationship between glucocerebrosidase mutations and Parkinson disease. J. Neurochem., 2016.
25. Park, B., Buti, L., Lee, S., Matsuwaki, T., Spooner, E., Brinkmann, M.M., Nishihara, M., Ploegh, H.L., Granulin is a soluble cofactor for toll-like receptor 9 signaling. Immunity 34 (2011), 505–513.
26. Perry, D.C., Lehmann, M., Yokoyama, J.S., Karydas, A., Lee, J.J., Coppola, G., Grinberg, L.T., Geschwind, D., Seeley, W.W., Miller, B.L., Rosen, H., Rabinovici, G., Progranulin mutations as risk factors for Alzheimer disease. JAMA Neurol. 70 (2013), 774–778.
27. Platt, F.M., Sphingolipid lysosomal storage disorders. Nature 510 (2014), 68–75.
28. Prabakaran, T., Nielsen, R., Satchell, S.C., Mathieson, P.W., Feldt-Rasmussen, U., Sorensen, S.S., Christensen, E.I., Mannose 6-phosphate receptor and sortilin mediated endocytosis of alpha-galactosidase A in kidney endothelial cells. PLoS One, 7, 2012, e39975.
29. Sidransky, E., Nalls, M.A., Aasly, J.O., Aharon-Peretz, J., Annesi, G., Barbosa, E.R., Bar-Shira, A., Berg, D., Bras, J., Brice, A., Chen, C.M., Clark, L.N., Condroyer, C., De Marco, E.V., Durr, A., Eblan, M.J., Fahn, S., Farrer, M.J., Fung, H.C., Gan-Or, Z., Gasser, T., Gershoni-Baruch, R., Giladi, N., Griffith, A., Gurevich, T., Januario, C., Kropp, P., Lang, A.E., Lee-Chen, G.J., Lesage, S., Marder, K., Mata, I.F., Mirelman, A., Mitsui, J., Mizuta, I., Nicoletti, G., Oliveira, C., Ottman, R., Orr-Urtreger, A., Pereira, L.V., Quattrone, A., Rogaeva, E., Rolfs, A., Rosenbaum, H., Rozenberg, R., Samii, A., Samaddar, T., Schulte, C., Sharma, M., Singleton, A., Spitz, M., Tan, E.K., Tayebi, N., Toda, T., Troiano, A.R., Tsuji, S., Wittstock, M., Wolfsberg, T.G., Wu, Y.R., Zabetian, C.P., Zhao, Y., Ziegler, S.G., Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease. N. Engl. J. Med. 361 (2009), 1651–1661.
30. Smith, K.R., Damiano, J., Franceschetti, S., Carpenter, S., Canafoglia, L., Morbin, M., Rossi, G., Pareyson, D., Mole, S.E., Staropoli, J.F., Sims, K.B., Lewis, J., Lin, W.L., Dickson, D.W., Dahl, H.H., Bahlo, M., Berkovic, S.F., Strikingly different clinicopathological phenotypes determined by progranulin-mutation dosage. Am. J. Hum. Genet. 90 (2012), 1102–1107.
31. Tang, W., Lu, Y., Tian, Q.Y., Zhang, Y., Guo, F.J., Liu, G.Y., Syed, N.M., Lai, Y., Lin, E.A., Kong, L., Su, J., Yin, F., Ding, A.H., Zanin-Zhorov, A., Dustin, M.L., Tao, J., Craft, J., Yin, Z., Feng, J.Q., Abramson, S.B., Yu, X.P., Liu, C.J., The growth factor progranulin binds to TNF receptors and is therapeutic against inflammatory arthritis in mice. Science 332 (2011), 478–484.
32. Witte, M.D., Kallemeijn, W.W., Aten, J., Li, K.Y., Strijland, A., Donker-Koopman, W.E., Van Den Nieuwendijk, A.M., Bleijlevens, B., Kramer, G., Florea, B.I., Hooibrink, B., Hollak, C.E., Ottenhoff, R., Boot, R.G., Van Der Marel, G.A., Overkleeft, H.S., Aerts, J.M., Ultrasensitive in situ visualization of active glucocerebrosidase molecules. Nat. Chem. Biol. 6 (2010), 907–913.