Clusterin

Details

Name
Clusterin
Synonyms
  • Aging-associated gene 4 protein
  • Apo-J
  • APOJ
  • Apolipoprotein J
  • CLI
  • Complement cytolysis inhibitor
  • Complement-associated protein SP-40,40
  • Ku70-binding protein 1
  • KUB1
  • NA1/NA2
  • Testosterone-repressed prostate message 2
  • TRPM-2
Gene Name
CLU
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049822|Clusterin
MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLI
EKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQT
CMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHF
SRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNF
HAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKD
QCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLE
QLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVP
VEVSRKNPKFMETVAEKALQEYRKKHREE
Number of residues
449
Molecular Weight
52494.22
Theoretical pI
Not Available
GO Classification
Functions
chaperone binding / misfolded protein binding / ubiquitin protein ligase binding
Processes
antimicrobial humoral response / cell morphogenesis / central nervous system myelin maintenance / chaperone-mediated protein complex assembly / chaperone-mediated protein folding / complement activation / complement activation, classical pathway / innate immune response / intrinsic apoptotic signaling pathway / lipid metabolic process / microglial cell activation / microglial cell proliferation / negative regulation of amyloid fibril formation / negative regulation of beta-amyloid formation / negative regulation of cell death / negative regulation of cellular response to thapsigargin / negative regulation of cellular response to tunicamycin / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / negative regulation of protein homooligomerization / negative regulation of release of cytochrome c from mitochondria / negative regulation of response to endoplasmic reticulum stress / platelet degranulation / positive regulation of apoptotic process / positive regulation of beta-amyloid formation / positive regulation of intrinsic apoptotic signaling pathway / positive regulation of neurofibrillary tangle assembly / positive regulation of neuron death / positive regulation of NF-kappaB transcription factor activity / positive regulation of nitric oxide biosynthetic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of protein homooligomerization / positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process / positive regulation of tau-protein kinase activity / positive regulation of tumor necrosis factor production / protein import / protein stabilization / regulation of beta-amyloid clearance / regulation of neuron death / regulation of neuronal signal transduction / release of cytochrome c from mitochondria / response to misfolded protein / response to virus / reverse cholesterol transport
Components
apical dendrite / blood microparticle / cell surface / chromaffin granule / cytoplasm / cytosol / endoplasmic reticulum / extracellular exosome / extracellular matrix / extracellular region / extracellular space / Golgi apparatus / intracellular / mitochondrial membrane / mitochondrion / neurofibrillary tangle / nucleus / perinuclear region of cytoplasm / platelet alpha granule lumen / protein complex / spherical high-density lipoprotein particle
General Function
Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation.
Specific Function
Chaperone binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0049823|Clusterin (CLU)
ATGATGAAGACTCTGCTGCTGTTTGTGGGGCTGCTGCTGACCTGGGAGAGTGGGCAGGTC
CTGGGGGACCAGACGGTCTCAGACAATGAGCTCCAGGAAATGTCCAATCAGGGAAGTAAG
TACGTCAATAAGGAAATTCAAAATGCTGTCAACGGGGTGAAACAGATAAAGACTCTCATA
GAAAAAACAAACGAAGAGCGCAAGACACTGCTCAGCAACCTAGAAGAAGCCAAGAAGAAG
AAAGAGGATGCCCTAAATGAGACCAGGGAATCAGAGACAAAGCTGAAGGAGCTCCCAGGA
GTGTGCAATGAGACCATGATGGCCCTCTGGGAAGAGTGTAAGCCCTGCCTGAAACAGACC
TGCATGAAGTTCTACGCACGCGTCTGCAGAAGTGGCTCAGGCCTGGTTGGCCGCCAGCTT
GAGGAGTTCCTGAACCAGAGCTCGCCCTTCTACTTCTGGATGAATGGTGACCGCATCGAC
TCCCTGCTGGAGAACGACCGGCAGCAGACGCACATGCTGGATGTCATGCAGGACCACTTC
AGCCGCGCGTCCAGCATCATAGACGAGCTCTTCCAGGACAGGTTCTTCACCCGGGAGCCC
CAGGATACCTACCACTACCTGCCCTTCAGCCTGCCCCACCGGAGGCCTCACTTCTTCTTT
CCCAAGTCCCGCATCGTCCGCAGCTTGATGCCCTTCTCTCCGTACGAGCCCCTGAACTTC
CACGCCATGTTCCAGCCCTTCCTTGAGATGATACACGAGGCTCAGCAGGCCATGGACATC
CACTTCCATAGCCCGGCCTTCCAGCACCCGCCAACAGAATTCATACGAGAAGGCGACGAT
GACCGGACTGTGTGCCGGGAGATCCGCCACAACTCCACGGGCTGCCTGCGGATGAAGGAC
CAGTGTGACAAGTGCCGGGAGATCTTGTCTGTGGACTGTTCCACCAACAACCCCTCCCAG
GCTAAGCTGCGGCGGGAGCTCGACGAATCCCTCCAGGTCGCTGAGAGGTTGACCAGGAAA
TACAACGAGCTGCTAAAGTCCTACCAGTGGAAGATGCTCAACACCTCCTCCTTGCTGGAG
CAGCTGAACGAGCAGTTTAACTGGGTGTCCCGGCTGGCAAACCTCACGCAAGGCGAAGAC
CAGTACTATCTGCGGGTCACCACGGTGGCTTCCCACACTTCTGACTCGGACGTTCCTTCC
GGTGTCACTGAGGTGGTCGTGAAGCTCTTTGACTCTGATCCCATCACTGTGACGGTCCCT
GTAGAAGTCTCCAGGAAGAACCCTAAATTTATGGAGACCGTGGCGGAGAAAGCGCTGCAG
GAATACCGCAAAAAGCACCGGGAGGAGTGA
Chromosome Location
8
Locus
8p21.1
External Identifiers
ResourceLink
UniProtKB IDP10909
UniProtKB Entry NameCLUS_HUMAN
HGNC IDHGNC:2095
General References
  1. Jenne DE, Tschopp J: Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7123-7. [PubMed:2780565]
  2. Wong P, Taillefer D, Lakins J, Pineault J, Chader G, Tenniswood M: Molecular characterization of human TRPM-2/clusterin, a gene associated with sperm maturation, apoptosis and neurodegeneration. Eur J Biochem. 1994 May 1;221(3):917-25. [PubMed:8181474]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005]
  5. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed:16421571]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  7. James RW, Hochstrasser AC, Borghini I, Martin B, Pometta D, Hochstrasser D: Characterization of a human high density lipoprotein-associated protein, NA1/NA2. Identity with SP-40,40, an inhibitor of complement-mediated cytolysis. Arterioscler Thromb. 1991 May-Jun;11(3):645-52. [PubMed:1903064]
  8. de Silva HV, Stuart WD, Park YB, Mao SJ, Gil CM, Wetterau JR, Busch SJ, Harmony JA: Purification and characterization of apolipoprotein J. J Biol Chem. 1990 Aug 25;265(24):14292-7. [PubMed:2387851]
  9. Ghiso J, Matsubara E, Koudinov A, Choi-Miura NH, Tomita M, Wisniewski T, Frangione B: The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem J. 1993 Jul 1;293 ( Pt 1):27-30. [PubMed:8328966]
  10. Choi NH, Mazda T, Tomita M: A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes. Mol Immunol. 1989 Sep;26(9):835-40. [PubMed:2601725]
  11. Hochstrasser AC, James RW, Martin BM, Harrington M, Hochstrasser D, Pometta D, Merril CR: HDL particle associated proteins in plasma and cerebrospinal fluid: identification and partial sequencing. Appl Theor Electrophor. 1988;1(1):73-6. [PubMed:3154963]
  12. de Silva HV, Harmony JA, Stuart WD, Gil CM, Robbins J: Apolipoprotein J: structure and tissue distribution. Biochemistry. 1990 Jun 5;29(22):5380-9. [PubMed:1974459]
  13. Danik M, Chabot JG, Mercier C, Benabid AL, Chauvin C, Quirion R, Suh M: Human gliomas and epileptic foci express high levels of a mRNA related to rat testicular sulfated glycoprotein 2, a purported marker of cell death. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8577-81. [PubMed:1924317]
  14. Kirszbaum L, Sharpe JA, Murphy B, d'Apice AJ, Classon B, Hudson P, Walker ID: Molecular cloning and characterization of the novel, human complement-associated protein, SP-40,40: a link between the complement and reproductive systems. EMBO J. 1989 Mar;8(3):711-8. [PubMed:2721499]
  15. Kirszbaum L, Bozas SE, Walker ID: SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges. FEBS Lett. 1992 Feb 3;297(1-2):70-6. [PubMed:1551440]
  16. Ehnholm C, Bozas SE, Tenkanen H, Kirszbaum L, Metso J, Murphy B, Walker ID: The apolipoprotein A-I binding protein of placenta and the SP-40,40 protein of human blood are different proteins which both bind to apolipoprotein A-I. Biochim Biophys Acta. 1991 Nov 27;1086(3):255-60. [PubMed:1742316]
  17. Choi-Miura NH, Takahashi Y, Nakano Y, Tobe T, Tomita M: Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J). J Biochem. 1992 Oct;112(4):557-61. [PubMed:1491011]
  18. Kelso GJ, Stuart WD, Richter RJ, Furlong CE, Jordan-Starck TC, Harmony JA: Apolipoprotein J is associated with paraoxonase in human plasma. Biochemistry. 1994 Jan 25;33(3):832-9. [PubMed:8292612]
  19. Kapron JT, Hilliard GM, Lakins JN, Tenniswood MP, West KA, Carr SA, Crabb JW: Identification and characterization of glycosylation sites in human serum clusterin. Protein Sci. 1997 Oct;6(10):2120-33. [PubMed:9336835]
  20. Poon S, Easterbrook-Smith SB, Rybchyn MS, Carver JA, Wilson MR: Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry. 2000 Dec 26;39(51):15953-60. [PubMed:11123922]
  21. Hatters DM, Wilson MR, Easterbrook-Smith SB, Howlett GJ: Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin. Eur J Biochem. 2002 Jun;269(11):2789-94. [PubMed:12047389]
  22. Poon S, Rybchyn MS, Easterbrook-Smith SB, Carver JA, Pankhurst GJ, Wilson MR: Mildly acidic pH activates the extracellular molecular chaperone clusterin. J Biol Chem. 2002 Oct 18;277(42):39532-40. Epub 2002 Aug 9. [PubMed:12176985]
  23. Leskov KS, Klokov DY, Li J, Kinsella TJ, Boothman DA: Synthesis and functional analyses of nuclear clusterin, a cell death protein. J Biol Chem. 2003 Mar 28;278(13):11590-600. Epub 2003 Jan 24. [PubMed:12551933]
  24. Santilli G, Aronow BJ, Sala A: Essential requirement of apolipoprotein J (clusterin) signaling for IkappaB expression and regulation of NF-kappaB activity. J Biol Chem. 2003 Oct 3;278(40):38214-9. Epub 2003 Jul 25. [PubMed:12882985]
  25. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed:12754519]
  26. Takahashi M, Lin YM, Nakamura Y, Furukawa Y: Isolation and characterization of a novel gene CLUAP1 whose expression is frequently upregulated in colon cancer. Oncogene. 2004 Dec 9;23(57):9289-94. [PubMed:15480429]
  27. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718]
  28. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952]
  29. Zhang H, Kim JK, Edwards CA, Xu Z, Taichman R, Wang CY: Clusterin inhibits apoptosis by interacting with activated Bax. Nat Cell Biol. 2005 Sep;7(9):909-15. Epub 2005 Aug 21. [PubMed:16113678]
  30. Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [PubMed:16548883]
  31. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed:16740002]
  32. Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [PubMed:16263699]
  33. Stewart EM, Aquilina JA, Easterbrook-Smith SB, Murphy-Durland D, Jacobsen C, Moestrup S, Wilson MR: Effects of glycosylation on the structure and function of the extracellular chaperone clusterin. Biochemistry. 2007 Feb 6;46(5):1412-22. [PubMed:17260971]
  34. Ranney MK, Ahmed IS, Potts KR, Craven RJ: Multiple pathways regulating the anti-apoptotic protein clusterin in breast cancer. Biochim Biophys Acta. 2007 Sep;1772(9):1103-11. Epub 2007 Jul 4. [PubMed:17689225]
  35. Wang Z, Widgren EE, Richardson RT, O'Rand MG: Characterization of an eppin protein complex from human semen and spermatozoa. Biol Reprod. 2007 Sep;77(3):476-84. Epub 2007 Jun 13. [PubMed:17567961]
  36. Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR: The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 2007 Aug;21(10):2312-22. Epub 2007 Apr 5. [PubMed:17412999]
  37. Cochrane DR, Wang Z, Muramaki M, Gleave ME, Nelson CC: Differential regulation of clusterin and its isoforms by androgens in prostate cells. J Biol Chem. 2007 Jan 26;282(4):2278-87. Epub 2006 Dec 4. [PubMed:17148459]
  38. Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM: The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. J Mol Biol. 2007 May 25;369(1):157-67. Epub 2007 Mar 7. [PubMed:17407782]
  39. Andersen CL, Schepeler T, Thorsen K, Birkenkamp-Demtroder K, Mansilla F, Aaltonen LA, Laurberg S, Orntoft TF: Clusterin expression in normal mucosa and colorectal cancer. Mol Cell Proteomics. 2007 Jun;6(6):1039-48. Epub 2007 Feb 23. [PubMed:17322305]
  40. Nizard P, Tetley S, Le Drean Y, Watrin T, Le Goff P, Wilson MR, Michel D: Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol. Traffic. 2007 May;8(5):554-65. [PubMed:17451556]
  41. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. doi: 10.1002/pmic.200701057. [PubMed:18780401]
  42. Wyatt AR, Yerbury JJ, Wilson MR: Structural characterization of clusterin-chaperone client protein complexes. J Biol Chem. 2009 Aug 14;284(33):21920-7. doi: 10.1074/jbc.M109.033688. Epub 2009 Jun 17. [PubMed:19535339]
  43. Rizzi F, Caccamo AE, Belloni L, Bettuzzi S: Clusterin is a short half-life, poly-ubiquitinated protein, which controls the fate of prostate cancer cells. J Cell Physiol. 2009 May;219(2):314-23. doi: 10.1002/jcp.21671. [PubMed:19137541]
  44. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218]
  45. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [PubMed:19139490]
  46. Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18. [PubMed:19838169]
  47. Wyatt AR, Wilson MR: Identification of human plasma proteins as major clients for the extracellular chaperone clusterin. J Biol Chem. 2010 Feb 5;285(6):3532-9. doi: 10.1074/jbc.M109.079566. Epub 2009 Dec 7. [PubMed:19996109]
  48. Zoubeidi A, Ettinger S, Beraldi E, Hadaschik B, Zardan A, Klomp LW, Nelson CC, Rennie PS, Gleave ME: Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells. Mol Cancer Res. 2010 Jan;8(1):119-30. doi: 10.1158/1541-7786.MCR-09-0277. Epub 2010 Jan 12. [PubMed:20068069]
  49. Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR: Clusterin facilitates in vivo clearance of extracellular misfolded proteins. Cell Mol Life Sci. 2011 Dec;68(23):3919-31. doi: 10.1007/s00018-011-0684-8). Epub 2011 Apr 20. [PubMed:21505792]
  50. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails