메뉴 건너뛰기




Volumn 12, Issue 1, 2017, Pages

Lysosomal processing of progranulin

Author keywords

Cathepsin; Frontotemporal lobar degeneration (FTLD); Lysosome; Neuronal ceroid lipofuscinosis (NCL); Progranulin (PGRN)

Indexed keywords

CATHEPSIN L; PROGRANULIN; PROSAPOSIN; CATHEPSIN; DNA BINDING PROTEIN; GRN PROTEIN, MOUSE; SIGNAL PEPTIDE;

EID: 85028351389     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/s13024-017-0205-9     Document Type: Article
Times cited : (60)

References (28)
  • 1
    • 33847654643 scopus 로고    scopus 로고
    • Progranulin in frontotemporal lobar degeneration and neuroinflammation
    • Ahmed Z, Mackenzie IR, Hutton ML, Dickson DW. Progranulin in frontotemporal lobar degeneration and neuroinflammation. J Neuroinflammation. 2007;4:7. https://doi.org/10.1186/1742-2094-4-7.
    • (2007) J Neuroinflammation , vol.4 , pp. 7
    • Ahmed, Z.1    Mackenzie, I.R.2    Hutton, M.L.3    Dickson, D.W.4
  • 2
    • 84866536050 scopus 로고    scopus 로고
    • Progranulin: A proteolytically processed protein at the crossroads of inflammation and neurodegeneration
    • Cenik B, Sephton CF, Kutluk Cenik B, Herz J, Yu G. Progranulin: a proteolytically processed protein at the crossroads of inflammation and neurodegeneration. J Biol Chem. 2012;287(39):32298-306. https://doi.org/10.1074/jbc.R112.399170.
    • (2012) J Biol Chem , vol.287 , Issue.39 , pp. 32298-32306
    • Cenik, B.1    Sephton, C.F.2    Kutluk Cenik, B.3    Herz, J.4    Yu, G.5
  • 3
    • 70549109118 scopus 로고    scopus 로고
    • The granulin gene family: From cancer to dementia
    • Bateman A, Bennett HP. The granulin gene family: from cancer to dementia. BioEssays. 2009;31(11):1245-54. https://doi.org/10.1002/bies.200900086.
    • (2009) BioEssays , vol.31 , Issue.11 , pp. 1245-1254
    • Bateman, A.1    Bennett, H.P.2
  • 4
    • 84855219552 scopus 로고    scopus 로고
    • Progranulin axis and recent developments in frontotemporal lobar degeneration
    • Nicholson AM, Gass J, Petrucelli L, Rademakers R. Progranulin axis and recent developments in frontotemporal lobar degeneration. Alzheimers Res Ther. 2012;4(1):4. doi:alzrt102 [pii]. https://doi.org/10.1186/alzrt102.
    • (2012) Alzheimers Res Ther , vol.4 , Issue.1 , pp. 4
    • Nicholson, A.M.1    Gass, J.2    Petrucelli, L.3    Rademakers, R.4
  • 5
    • 0031672540 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria
    • 1:STN:280:DyaK1M%2FntFWnsA%3D%3D 9855500
    • Neary D, Snowden JS, Gustafson L, Passant U, Stuss D, Black S, et al. Frontotemporal lobar degeneration: a consensus on clinical diagnostic criteria. Neurology. 1998;51(6):1546-54.
    • (1998) Neurology , vol.51 , Issue.6 , pp. 1546-1554
    • Neary, D.1    Snowden, J.S.2    Gustafson, L.3    Passant, U.4    Stuss, D.5    Black, S.6
  • 6
    • 84862134180 scopus 로고    scopus 로고
    • Strikingly different clinicopathological phenotypes determined by progranulin-mutation dosage
    • Smith KR, Damiano J, Franceschetti S, Carpenter S, Canafoglia L, Morbin M, et al. Strikingly different clinicopathological phenotypes determined by progranulin-mutation dosage. Am J Hum Genet. 2012;90(6):1102-7. https://doi.org/10.1016/j.ajhg.2012.04.021.
    • (2012) Am J Hum Genet , vol.90 , Issue.6 , pp. 1102-1107
    • Smith, K.R.1    Damiano, J.2    Franceschetti, S.3    Carpenter, S.4    Canafoglia, L.5    Morbin, M.6
  • 7
    • 84963540872 scopus 로고    scopus 로고
    • Portuguese family with the co-occurrence of frontotemporal lobar degeneration and neuronal ceroid lipofuscinosis phenotypes due to progranulin gene mutation
    • Almeida MR, Macario MC, Ramos L, Baldeiras I, Ribeiro MH, Santana I. Portuguese family with the co-occurrence of frontotemporal lobar degeneration and neuronal ceroid lipofuscinosis phenotypes due to progranulin gene mutation. Neurobiol Aging. 2016. doi: https://doi.org/10.1016/j.neurobiolaging.2016.02.019.
    • (2016) Neurobiol Aging
    • Almeida, M.R.1    Macario, M.C.2    Ramos, L.3    Baldeiras, I.4    Ribeiro, M.H.5    Santana, I.6
  • 8
    • 80455178749 scopus 로고    scopus 로고
    • Transcriptional gene network inference from a massive dataset elucidates transcriptome organization and gene function
    • Belcastro V, Siciliano V, Gregoretti F, Mithbaokar P, Dharmalingam G, Berlingieri S, et al. Transcriptional gene network inference from a massive dataset elucidates transcriptome organization and gene function. Nucleic Acids Res. 2011;39(20):8677-88. https://doi.org/10.1093/nar/gkr593.
    • (2011) Nucleic Acids Res , vol.39 , Issue.20 , pp. 8677-8688
    • Belcastro, V.1    Siciliano, V.2    Gregoretti, F.3    Mithbaokar, P.4    Dharmalingam, G.5    Berlingieri, S.6
  • 9
    • 78449286213 scopus 로고    scopus 로고
    • Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin
    • Hu F, Padukkavidana T, Vaegter CB, Brady OA, Zheng Y, Mackenzie IR, et al. Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin. Neuron. 2010;68(4):654-67. https://doi.org/10.1016/j.neuron.2010.09.034.
    • (2010) Neuron , vol.68 , Issue.4 , pp. 654-667
    • Hu, F.1    Padukkavidana, T.2    Vaegter, C.B.3    Brady, O.A.4    Zheng, Y.5    Mackenzie, I.R.6
  • 10
    • 84960380361 scopus 로고    scopus 로고
    • Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin
    • Zhou X, Sun L, Bastos de Oliveira F, Qi X, Brown WJ, Smolka MB, et al. Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin. J Cell Biol. 2015;210(6):991-1002. https://doi.org/10.1083/jcb.201502029.
    • (2015) J Cell Biol , vol.210 , Issue.6 , pp. 991-1002
    • Zhou, X.1    Sun, L.2    Bastos De Oliveira, F.3    Qi, X.4    Brown, W.J.5    Smolka, M.B.6
  • 11
    • 0025897376 scopus 로고
    • Saposin proteins: Structure, function, and role in human lysosomal storage disorders
    • 2001789
    • O'Brien JS, Kishimoto Y. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 1991;5(3):301-8.
    • (1991) FASEB J , vol.5 , Issue.3 , pp. 301-308
    • O'Brien, J.S.1    Kishimoto, Y.2
  • 12
    • 0035193420 scopus 로고    scopus 로고
    • Molecular and cell biology of acid beta-glucosidase and prosaposin
    • 1:STN:280:DC%2BD3crgsVanuw%3D%3D 11051765
    • Qi X, Grabowski GA. Molecular and cell biology of acid beta-glucosidase and prosaposin. Prog Nucleic Acid Res Mol Biol. 2001;66:203-39.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.66 , pp. 203-239
    • Qi, X.1    Grabowski, G.A.2
  • 13
    • 38449095568 scopus 로고    scopus 로고
    • The function of sphingolipids in the nervous system: Lessons learnt from mouse models of specific sphingolipid activator protein deficiencies
    • Matsuda J, Yoneshige A, Suzuki K. The function of sphingolipids in the nervous system: lessons learnt from mouse models of specific sphingolipid activator protein deficiencies. J Neurochem. 2007;103(Suppl 1):32-8. https://doi.org/10.1111/j.1471-4159.2007.04709.x.
    • (2007) J Neurochem , vol.103 , pp. 32-38
    • Matsuda, J.1    Yoneshige, A.2    Suzuki, K.3
  • 14
    • 0037074016 scopus 로고    scopus 로고
    • Conversion of proepithelin to epithelins: Roles of SLPI and elastase in host defense and wound repair
    • 1:CAS:528:DC%2BD3sXhtVyksw%3D%3D 12526812
    • Zhu J, Nathan C, Jin W, Sim D, Ashcroft GS, Wahl SM, et al. Conversion of proepithelin to epithelins: roles of SLPI and elastase in host defense and wound repair. Cell. 2002;111(6):867-78.
    • (2002) Cell , vol.111 , Issue.6 , pp. 867-878
    • Zhu, J.1    Nathan, C.2    Jin, W.3    Sim, D.4    Ashcroft, G.S.5    Wahl, S.M.6
  • 15
    • 84859590507 scopus 로고    scopus 로고
    • Regulation of progranulin expression in human microglia and proteolysis of progranulin by matrix metalloproteinase-12 (MMP-12)
    • e35115 10.1371/journal.pone.0035115 1:CAS:528:DC%2BC38XmtVOls7c%3D 22509390 3324426
    • Suh HS, Choi N, Tarassishin L, Lee SC. Regulation of progranulin expression in human microglia and proteolysis of progranulin by matrix metalloproteinase-12 (MMP-12). PLoS One. 2012;7(4):e35115. https://doi.org/10.1371/journal.pone.0035115.
    • (2012) PLoS One , vol.7 , Issue.4
    • Suh, H.S.1    Choi, N.2    Tarassishin, L.3    Lee, S.C.4
  • 16
    • 85026733581 scopus 로고    scopus 로고
    • The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C
    • Zhou X, Sullivan PM, Sun L, Hu F. The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C. J Neurochem. 2017; https://doi.org/10.1111/jnc.14110.
    • (2017) J Neurochem
    • Zhou, X.1    Sullivan, P.M.2    Sun, L.3    Hu, F.4
  • 17
    • 84965071473 scopus 로고    scopus 로고
    • Lysosomal cathepsins and their regulation in aging and neurodegeneration
    • Stoka V, Turk V, Turk B. Lysosomal cathepsins and their regulation in aging and neurodegeneration. Ageing Res Rev. 2016;32:22-37. https://doi.org/10.1016/j.arr.2016.04.010.
    • (2016) Ageing Res Rev , vol.32 , pp. 22-37
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 19
    • 33746255613 scopus 로고    scopus 로고
    • Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice
    • Sevenich L, Pennacchio LA, Peters C, Reinheckel T. Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. 2006;387(7):885-91. https://doi.org/10.1515/BC.2006.112.
    • (2006) Biol Chem , vol.387 , Issue.7 , pp. 885-891
    • Sevenich, L.1    Pennacchio, L.A.2    Peters, C.3    Reinheckel, T.4
  • 20
  • 21
  • 24
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • 1:CAS:528:DyaK2MXnsFGqtrk%3D 7641679 394433
    • Saftig P, Hetman M, Schmahl W, Weber K, Heine L, Mossmann H, et al. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 1995;14(15):3599-608.
    • (1995) EMBO J , vol.14 , Issue.15 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6
  • 25
    • 0033795691 scopus 로고    scopus 로고
    • Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis
    • Halangk W, Lerch MM, Brandt-Nedelev B, Roth W, Ruthenbuerger M, Reinheckel T, et al. Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. J Clin Invest. 2000;106(6):773-81. https://doi.org/10.1172/JCI9411.
    • (2000) J Clin Invest , vol.106 , Issue.6 , pp. 773-781
    • Halangk, W.1    Lerch, M.M.2    Brandt-Nedelev, B.3    Roth, W.4    Ruthenbuerger, M.5    Reinheckel, T.6
  • 26
    • 0033810653 scopus 로고    scopus 로고
    • Cathepsin L deficiency as molecular defect of furless: Hyperproliferation of keratinocytes and pertubation of hair follicle cycling
    • Roth W, Deussing J, Botchkarev VA, Pauly-Evers M, Saftig P, Hafner A, et al. Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling. FASEB J. 2000;14(13):2075-86. https://doi.org/10.1096/fj.99-0970com 14/13/2075 14/13/2075.
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 2075-2086
    • Roth, W.1    Deussing, J.2    Botchkarev, V.A.3    Pauly-Evers, M.4    Saftig, P.5    Hafner, A.6
  • 27
    • 0032506007 scopus 로고    scopus 로고
    • Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice
    • 1:CAS:528:DyaK1cXnsVGhtL4%3D 9811821 24840
    • Saftig P, Hunziker E, Wehmeyer O, Jones S, Boyde A, Rommerskirch W, et al. Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice. Proc Natl Acad Sci U S A. 1998;95(23):13453-8.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.23 , pp. 13453-13458
    • Saftig, P.1    Hunziker, E.2    Wehmeyer, O.3    Jones, S.4    Boyde, A.5    Rommerskirch, W.6
  • 28
    • 77249161680 scopus 로고    scopus 로고
    • Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice
    • Sevenich L, Schurigt U, Sachse K, Gajda M, Werner F, Muller S, et al. Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice. Proc Natl Acad Sci U S A. 2010;107(6):2497-502. https://doi.org/10.1073/pnas.0907240107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.6 , pp. 2497-2502
    • Sevenich, L.1    Schurigt, U.2    Sachse, K.3    Gajda, M.4    Werner, F.5    Muller, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.