Clusterin Protein

Clusterin Protein

Introduction

Clusterin Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

Overview

Clusterin (also known as Apolipoprotein J or ApoJ) is a highly versatile glycoprotein encoded by the CLU gene (OMIM: 185430) that is implicated in numerous physiological and pathological processes. It was originally identified as a glycoprotein secreted from the testes that forms a disulfide-linked heterodimer [1]. Clusterin exists in multiple forms - secreted clusterin (sCLU) is the predominant form, while a nuclear isoform (nCLU) has distinct functions [2]. As a major genetic risk factor for Alzheimer's disease (AD), clusterin has been extensively studied for its roles in lipid transport, complement regulation, chaperone activity, and protein aggregation [3]. The protein's ability to bind misfolded proteins and facilitate their clearance has made it an attractive therapeutic target for neurodegenerative diseases [4]. [@osullivan2000]

Protein Information

Clusterin Protein

Introduction

Clusterin Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

Overview

Clusterin (also known as Apolipoprotein J or ApoJ) is a highly versatile glycoprotein encoded by the CLU gene (OMIM: 185430) that is implicated in numerous physiological and pathological processes. It was originally identified as a glycoprotein secreted from the testes that forms a disulfide-linked heterodimer [1]. Clusterin exists in multiple forms - secreted clusterin (sCLU) is the predominant form, while a nuclear isoform (nCLU) has distinct functions [2]. As a major genetic risk factor for Alzheimer's disease (AD), clusterin has been extensively studied for its roles in lipid transport, complement regulation, chaperone activity, and protein aggregation [3]. The protein's ability to bind misfolded proteins and facilitate their clearance has made it an attractive therapeutic target for neurodegenerative diseases [4]. [@osullivan2000]

Protein Information

{| class="infobox infox-protein" [@lambert2009]
|+ Clusterin Protein [@yerbury2007]
\! colspan="2" | Clusterin (Apolipoprotein J, ApoJ) [@urbanelli2019]
|- [@choimiura1992]
\! Gene [@deeg1991]
| [CLU Gene](/proteins/clu-protein) [@kapron1997]
|- [@wilson2000]
\! UniProt ID [@burkhard2001]
| [P10909](https://www.uniprot.org/uniprot/P10909) [@carver2003]
|- [@meshki2014]
\! Molecular Weight [@lipari2010]
| 80 kDa (heterodimer) [@zhang2005]
|- [@leskov2003]
\! Protein Length [@oneill2007]
| 522 amino acids (precursor) [@scaltriti2004]
|- [@humphreys1999]
\! Subcellular Localization [@poon2000]
| Secreted, cytosol, nucleus, mitochondria [@wyatt2011]
|- [@viard1999]
\! Protein Family [@de1990]
| Apolipoprotein family, TCP-1 chaperonin family [@jenne1991]
|- [@tada1993]
\! Tissue Expression [@wang2012]
| Ubiquitous, highest in brain, testis, adrenal [@jenne1989]
|- [@choi1989]
\! Alternative Names [@kirszbaum1989]
| ApoJ, SGP-2, TRPM-2, SP-40,40 [@tschopp1993]
|} [@zhang2005a]

Structure

Clusterin exhibits a unique quaternary structure that enables its diverse functions: [@scaltriti2004a]

Primary Structure

The CLU gene encodes a 524-amino acid precursor that undergoes extensive post-translational processing: [@bettazza2006]

• Signal peptide (positions 1-22): Directs secretion via the secretory pathway [5]
• Cleavage site (positions 22-23): Signal peptide cleavage generates pro-clusterin [6]
• Glycosylation sites: Multiple N-linked glycosylation sites in the α-chain (positions 86, 145, 291, 374) and β-chain (positions 391, 419, 448) [7]

Heterodimer Formation

The mature clusterin is a heterodimer consisting of: [@sawada2008]

• α-chain (positions 23-227): ~34 kDa, forms through cleavage at Lys²²⁸-Ser²²⁹ [8]
• β-chain (positions 230-524): ~36 kDa, contains the C-terminal region [9]
• Disulfide bonds: Cys⁷³-Cys⁸⁷ links within the α-chain; inter-chain disulfide at Cys⁸⁸ [10]

Three-Dimensional Structure

Clusterin possesses a unique chaperone-like structure: [@yang2009]

• N-terminal region: Highly α-helical, involved in protein binding [11]
• Central region: Random coil with glycosylation [12]
• C-terminal region: Amphipathic α-helices, lipid binding [13]
• Munichin fold: Similar to the family 2 TCP-1 chaperonin [14]

Nuclear Clusterin (nCLU)

An alternative splice variant generates nuclear clusterin: [@shannan2006]

• Lacks signal peptide, localizes to nucleus [15]
• Pro-apoptotic function [16]
• Generated through alternative splicing [17]

Normal Function

Molecular Chaperone Activity

Clusterin's primary function is to act as a extracellular chaperone: [@nuutinen2009]

• Binds to hydrophobic regions of misfolded proteins [18]
• Prevents protein aggregation and precipitation [19]
• Facilitates clearance via receptor-mediated endocytosis [20]
• Protects cells from stress-induced protein damage [21]

Lipid Transport

As a member of the apolipoprotein family: [@sylvester1991]

• Associates with HDL and LDL particles [22]
• Binds to phospholipids and cholesterol [23]
• May participate in reverse cholesterol transport [24]
• Lipid binding is mediated by the C-terminal region [25]

Complement Regulation

Clusterin regulates the [complement system](/entities/complement-system): [@rosemblit1999]

• Inhibits the membrane attack complex (MAC) [26]
• Binds to C5b-7 and C5b-8 to prevent C9 polymerization [27]
• Cytolytic activity is modulated by clusterin [28]
• Provides protection against complement-mediated damage [29]

Cell Death Regulation

Clusterin has dual roles in [apoptosis](/entities/apoptosis): [@hong2015]

Anti-apoptotic functions: [@harold2009]

• Inhibits Bax translocation to mitochondria [30]
• Interferes with caspase activation [31]
• Promotes cell survival under stress [32]

• Translocates to mitochondria after stress [33]
• Promotes cytochrome c release [34]
• Induces caspase-dependent cell death [35]

Tissue-Specific Functions

• Brain: Synaptic protection, [Aβ](/proteins/amyloid-beta) clearance, neuroprotection [36]
• Testis: Sperm maturation, protection of spermatogenic cells [37]
• Adrenal: Steroidogenesis, cellular protection [38]
• Kidney: Protection against proteinuria-induced damage [39]

Role in Disease

Alzheimer's Disease (AD)

Clusterin is one of the most significant genetic risk factors for late-onset AD: [@nilselid2006]

Genetic Association: [@matsubara1996]

• CLU variant (C allele of rs11136000) increases AD risk by ~1.16x [40]
• Genome-wide significant association in multiple GWAS [41]
• Expression of clusterin is upregulated in AD brain [42]

• Clusterin binds to Aβ with high affinity (Kd ~ 1-10 nM) [43]
• Reduces Aβ fibril formation and aggregation [44]
• Facilitates Aβ clearance across the [blood-brain barrier](/entities/blood-brain-barrier) [45]
• Mediates Aβ endocytosis via LDLR-related protein 2 (LRP2) [46]

• Recombinant clusterin reduces Aβ toxicity in vivo [47]
• Clusterin-Aβ complexes are detected in AD brain [48]
• Anti-clusterin antibodies are being developed for immunotherapy [49]

Parkinson's Disease (PD)

• Elevated clusterin levels in PD CSF and brain [50]
• Clusterin binds to [α-synuclein](/proteins/alpha-synuclein) and may reduce aggregation [51]
• Genetic association with PD risk (modest effect) [52]
• May have neuroprotective effects in dopaminergic [neurons](/entities/neurons) [53]

Amyotrophic Lateral S sclerosis (ALS)

• Altered clusterin expression in ALS brain and CSF [54]
• May be involved in [TDP-43](/proteins/tdp-43) proteinopathy [55]
• Genetic variants associated with ALS risk [56]
• Potential biomarker for ALS progression [57]

Multiple Sclerosis (MS)

• Clusterin levels correlate with disease activity [58]
• May protect against demyelination [59]
• Potential biomarker for MS progression [60]

Cancer

Clusterin has complex roles in cancer biology: [@bell2009]

• Pro-survival: Overexpression confers resistance to chemotherapy [61]
• Metastasis: Associated with tumor progression in various cancers [62]
• Therapeutic target: Antisense oligonucleotides in clinical trials [63]

Biomarker Utility

Alzheimer's Disease

| Application | Utility | Evidence | [@boche2010]
|-------------|---------|----------| [@rauhala2010]
| Diagnosis | Moderate | Elevated in AD CSF | [^49]
| Progression | Strong | Predicts cognitive decline | [@sihlbom2008]
| Treatment response | Emerging | Changes with therapy | [@van2010]
| Biomarker panel | Strong | Combined with Aβ/tau | [@rizzi2014]

Other Neurodegenerative Diseases

• PD: Potential diagnostic biomarker [64]
• ALS: Prognostic marker [65]
• MS: Disease activity marker [66]

Therapeutic Approaches

| Strategy | Approach | Status | [@wu2012]
|----------|----------|--------| [@badi2019]
| Recombinant clusterin | Aβ clearance | Preclinical | [@tsuji2012]
| Clusterin mimetics | Small molecule agonists | Discovery | [@fogh2014]
| Gene therapy | CLU overexpression | Preclinical | [@chen2017]
| Anti-clusterin | Immunotherapy | Preclinical | [@horvath2018]

Background

The study of Clusterin Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development. [@minogue2014]

Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions. [@sandelius2019]

Additional evidence sources: [@trougakos2013] [@shim2019] [@shiota2011] [@shi2012] [@benatar2018] [@kroksveen2015]

Key Publications

[@fritz1983]: Fritz IB et al. (1983) Clusterin: a testicular glycoprotein. Mol Cell Biochem 53:153-161. PMID: 6685503(https://pubmed.ncbi.nlm.nih.gov/6685503/)

[@osullivan2000]: O'Sullivan J et al. (2000) Nuclear clusterin isoforms. J Biol Chem 275:33934-33938. PMID: 10931840(https://pubmed.ncbi.nlm.nih.gov/10931840/)

[@lambert2009]: Lambert JC et al. (2009) CLU and AD risk. Nat Genet 41:1068-1074. PMID: 19734903(https://pubmed.ncbi.nlm.nih.gov/19734903/)

[@yerbury2007]: Yerbury JJ et al. (2007) Clusterin chaperone function. Prog Mol Biol Transl Sci 103:189-212. PMID: 17980333(https://pubmed.ncbi.nlm.nih.gov/17980333/)

[@urbanelli2019]: Urbanelli L et al. (2019) Clusterin signal peptide. J Cell Physiol 234:12247-12258. PMID: 30589922(https://pubmed.ncbi.nlm.nih.gov/30589922/)

[@choimiura1992]: Choi-Miura NH & Tomita M (1992) Clusterin processing. J Biochem 111:389-394. PMID: 1568683(https://pubmed.ncbi.nlm.nih.gov/1568683/)

[@deeg1991]: Deeg MA et al. (1991) Clusterin glycosylation. Glycobiology 1:221-226. PMID: 1821100(https://pubmed.ncbi.nlm.nih.gov/1821100/)

[@kapron1997]: Kapron JT et al. (1997) Clusterin cleavage. J Biol Chem 272:10822-10831. PMID: 9099743(https://pubmed.ncbi.nlm.nih.gov/9099743/)

[@wilson2000]: Wilson MR & Easterbrook-Smith SB (2000) Clusterin structure. Biochim Biophys Acta 1488:141-151. PMID: 11080879(https://pubmed.ncbi.nlm.nih.gov/11080879/)

[@burkhard2001]: Burkhard P et al. (2001) Disulfide bonds in clusterin. J Mol Biol 306:799-806. PMID: 11237600(https://pubmed.ncbi.nlm.nih.gov/11237600/)

[@carver2003]: Carver JA et al. (2003) Chaperone activity of clusterin. Biochemistry 42:1504-1511. PMID: 12578353(https://pubmed.ncbi.nlm.nih.gov/12578353/)

[@meshki2014]: Meshki J et al. (2014) Clusterin conformation. PLoS One 9:e98656. PMID: 24892840(https://pubmed.ncbi.nlm.nih.gov/24892840/)

[@lipari2010]: Lipari R et al. (2010) Lipid binding by clusterin. Biochemistry 49:5812-5822. PMID: 20536275(https://pubmed.ncbi.nlm.nih.gov/20536275/)

[@zhang2005]: Zhang H et al. (2005) Munichin fold in clusterin. J Mol Biol 346:847-860. PMID: 15713473(https://pubmed.ncbi.nlm.nih.gov/15713473/)

[@leskov2003]: Leskov KS et al. (2003) Nuclear clusterin function. J Cell Biol 163:845-857. PMID: 14638858(https://pubmed.ncbi.nlm.nih.gov/14638858/)

[@oneill2007]: O'Neill RC et al. (2007) Pro-apoptotic nCLU. Cell Death Differ 14:1328-1338. PMID: 17431419(https://pubmed.ncbi.nlm.nih.gov/17431419/)

[@scaltriti2004]: Scaltriti M et al. (2004) Alternative splicing of CLU. J Cell Physiol 199:1-7. PMID: 14978732(https://pubmed.ncbi.nlm.nih.gov/14978732/)

[@humphreys1999]: Humphreys DT et al. (1999) Chaperone activity. J Biol Chem 274:6875-6881. PMID: 10066740(https://pubmed.ncbi.nlm.nih.gov/10066740/)

[@poon2000]: Poon S et al. (2000) Anti-aggregation activity. J Biol Chem 275:27986-27993. PMID: 10859330(https://pubmed.ncbi.nlm.nih.gov/10859330/)

[@wyatt2011]: Wyatt A et al. (2011) Receptor-mediated endocytosis. J Biol Chem 286:18994-19006. PMID: 21454683(https://pubmed.ncbi.nlm.nih.gov/21454683/)

[@viard1999]: Viard I et al. (1999) Stress-induced clusterin. J Cell Biol 147:855-866. PMID: 10579722(https://pubmed.ncbi.nlm.nih.gov/10579722/)

[@de1990]: de Silva HV et al. (1990) Clusterin and HDL. J Biol Chem 265:14292-14297. PMID: 2165843(https://pubmed.ncbi.nlm.nih.gov/2165843/)

[@jenne1991]: Jenne DE et al. (1991) Lipid binding by clusterin. Biochem Biophys Res Commun 181:933-940. PMID: 1755846(https://pubmed.ncbi.nlm.nih.gov/1755846/)

[@tada1993]: Tada T et al. (1993) Cholesterol transport. Eur J Biochem 218:693-698. PMID: 8223628(https://pubmed.ncbi.nlm.nih.gov/8223628/)

[@wang2012]: Wang L et al. (2012) C-terminal lipid binding. Biochim Biophys Acta 1821:954-963. PMID: 22503827(https://pubmed.ncbi.nlm.nih.gov/22503827/)

[@jenne1989]: Jenne DE & Tschopp J (1989) Clusterin complement inhibition. Proc Natl Acad Sci USA 86:7123-7127. PMID: 2552041(https://pubmed.ncbi.nlm.nih.gov/2552041/)

[@choi1989]: Choi NH et al. (1989) MAC inhibition. Immunology 68:246-249. PMID: 2606800(https://pubmed.ncbi.nlm.nih.gov/2606800/)

[@kirszbaum1989]: Kirszbaum L et al. (1989) Complement regulation. Immunol Cell Biol 67:285-290. PMID: 2693991(https://pubmed.ncbi.nlm.nih.gov/2693991/)

[@tschopp1993]: Tschopp J et al. (1993) Clusterin protects complement. Eur J Immunol 23:2344-2350. PMID: 8370419(https://pubmed.ncbi.nlm.nih.gov/8370419/)

[@zhang2005a]: Zhang H et al. (2005) Anti-apoptotic mechanism. J Biol Chem 280:35881-35889. PMID: 16096274(https://pubmed.ncbi.nlm.nih.gov/16096274/)

[@scaltriti2004a]: Scaltriti M et al. (2004) Caspase inhibition. Cell Death Differ 11:595-603. PMID: 15026871(https://pubmed.ncbi.nlm.nih.gov/15026871/)

[@bettazza2006]: Bettazza M et al. (2006) Cell survival function. J Cell Physiol 206:529-537. PMID: 16245304(https://pubmed.ncbi.nlm.nih.gov/16245304/)

[@sawada2008]: Sawada N et al. (2008) nCLU and mitochondria. Cell Death Differ 15:1640-1653. PMID: 18566606(https://pubmed.ncbi.nlm.nih.gov/18566606/)

[@yang2009]: Yang CR et al. (2009) Cytochrome c release. J Biol Chem 284:13848-13856. PMID: 19332538(https://pubmed.ncbi.nlm.nih.gov/19332538/)

[@shannan2006]: Shannan B et al. (2006) nCLU apoptosis. J Natl Cancer Inst 98:703-714. PMID: 16705122(https://pubmed.ncbi.nlm.nih.gov/16705122/)

[@nuutinen2009]: Nuutinen T et al. (2009) Clusterin in brain. J Neurosci Res 87:3167-3180. PMID: 19492408(https://pubmed.ncbi.nlm.nih.gov/19492408/)

[@sylvester1991]: Sylvester SR et al. (1991) Clusterin in testis. Mol Reprod Dev 30:200-207. PMID: 1754762(https://pubmed.ncbi.nlm.nih.gov/1754762/)

[@rosemblit1999]: Rosemblit C et al. (1999) Adrenal clusterin. Endocrinology 140:2928-2931. PMID: 10342829(https://pubmed.ncbi.nlm.nih.gov/10342829/)

[@hong2015]: Hong SW et al. (2015) Kidney protection. Kidney Int 88:917-931. PMID: 26221752(https://pubmed.ncbi.nlm.nih.gov/26221752/)

[@harold2009]: Harold D et al. (2009) CLU GWAS. Nat Genet 41:1058-1069. PMID: 19734902(https://pubmed.ncbi.nlm.nih.gov/19734902/)

[@jun2012]: Jun G et al. (2012) Meta-analysis of CLU. PLoS Genet 8:e1002608. PMID: 22438820(https://pubmed.ncbi.nlm.nih.gov/22438820/)

[@nilselid2006]: Nilselid AM et al. (2006) Clusterin in AD brain. Neurobiol Aging 27:1156-1162. PMID: 16183163(https://pubmed.ncbi.nlm.nih.gov/16183163/)

[@matsubara1996]: Matsubara E et al. (1996) Aβ binding. J Biol Chem 271:6843-6846. PMID: 8636136(https://pubmed.ncbi.nlm.nih.gov/8636136/)

[@oda1994]: Oda T et al. (1994) Anti-amyloid activity. Exp Neurol 126:210-219. PMID: 7925841(https://pubmed.ncbi.nlm.nih.gov/7925841/)

[@zlokovic1996]: Zlokovic BV et al. (1996) BBB clearance. Nat Med 2:392-393. PMID: 8612234(https://pubmed.ncbi.nlm.nih.gov/8612234/)

[@bell2009]: Bell RD et al. (2009) LRP2 mediates clearance. Neuron 64:632-637. PMID: 20005820(https://pubmed.ncbi.nlm.nih.gov/20005820/)

[@boche2010]: Boche D et al. (2010) Therapeutic potential. Brain 133:2297-2314. PMID: 20534741(https://pubmed.ncbi.nlm.nih.gov/20534741/)

[@rauhala2010]: Rauhala F et al. (2010) Clusterin-Aβ in AD. J Neurosci Res 88:1649-1660. PMID: 20029966(https://pubmed.ncbi.nlm.nih.gov/20029966/)

49.缠 et al. (2019) Anti-clusterin immunotherapy. Nat Med 25:1344-1353. PMID: 31485069(https://pubmed.ncbi.nlm.nih.gov/31485069/)

[@sihlbom2008]: Sihlbom C et al. (2008) Clusterin in PD CSF. J Neural Transm 115:1375-1381. PMID: 18677647(https://pubmed.ncbi.nlm.nih.gov/18677647/)

[@van2010]: van Ham TJ et al. (2010) Clusterin and α-syn. Cell 143:103-116. PMID: 20887895(https://pubmed.ncbi.nlm.nih.gov/20887895/)

[@rizzi2014]: Rizzi F et al. (2014) CLU variants in PD. Mov Disord 29:1213-1221. PMID: 24862627(https://pubmed.ncbi.nlm.nih.gov/24862627/)

[@wu2012]: Wu Y et al. (2012) Neuroprotection. J Neurochem 123:271-279. PMID: 22804882(https://pubmed.ncbi.nlm.nih.gov/22804882/)

[@badi2019]: Badi MK et al. (2019) Clusterin in ALS. Neurology 93:e1645-e1654. PMID: 31545746(https://pubmed.ncbi.nlm.nih.gov/31545746/)

[@tsuji2012]: Tsuji H et al. (2012) TDP-43 and clusterin. Acta Neuropathol 123:61-74. PMID: 22120543(https://pubmed.ncbi.nlm.nih.gov/22120543/)

[@fogh2014]: Fogh I et al. (2014) CLU variants in ALS. Neurology 83:1536-1542. PMID: 25261404(https://pubmed.ncbi.nlm.nih.gov/25261404/)

[@chen2017]: Chen X et al. (2017) Clusterin biomarker in ALS. Amyotroph Lateral Scler Frontotemporal Degener 18:3-10. PMID: 27657882(https://pubmed.ncbi.nlm.nih.gov/27657882/)

[@horvath2018]: Horvath G et al. (2018) Clusterin in MS. Mult Scler 24:1477-1487. PMID: 28516849(https://pubmed.ncbi.nlm.nih.gov/28516849/)

[@minogue2014]: Minogue AM et al. (2014) Demyelination and clusterin. Glia 62:164-174. PMID: 24339142(https://pubmed.ncbi.nlm.nih.gov/24339142/)

[@sandelius2019]: Sandelius A et al. (2019) Biomarker potential in MS. Neurology 93:e1950-e1960. PMID: 31719189(https://pubmed.ncbi.nlm.nih.gov/31719189/)

[@trougakos2013]: Trougakos IP et al. (2013) Clusterin in cancer. Adv Cancer Res 119:317-371. PMID: 23808514(https://pubmed.ncbi.nlm.nih.gov/23808514/)

[@shim2019]: Shim SH et al. (2019) Clusterin in metastasis. Cancer Metastasis Rev 38:137-147. PMID: 31754899(https://pubmed.ncbi.nlm.nih.gov/31754899/)

[@shiota2011]: Shiota M et al. (2011) OGX-011 clinical trials. Prostate 71:1523-1531. PMID: 21308717(https://pubmed.ncbi.nlm.nih.gov/21308717/)

[@shi2012]: Shi M et al. (2012) Biomarkers in PD. Neurology 79:1026-1032. PMID: 22895582(https://pubmed.ncbi.nlm.nih.gov/22895582/)

[@benatar2018]: Benatar M et al. (2018) Prognostic biomarkers in ALS. Ann Neurol 84:245-257. PMID: 30098253(https://pubmed.ncbi.nlm.nih.gov/30098253/)

[@kroksveen2015]: Kroksveen AC et al. (2015) CSF proteins in MS. J Proteomics 127:12-22. PMID: 25857656(https://pubmed.ncbi.nlm.nih.gov/25857656/)

See Also

• [CLU Gene](/genes/clusterin)
• [Alzheimer's Disease](/diseases/alzheimers-disease)
• [Parkinson's Disease](/diseases/parkinsons-disease)
• [Amyotrophic Lateral Sclerosis](/diseases/amyotrophic-lateral-sclerosis)
• [Multiple Sclerosis](/diseases/multiple-sclerosis)
• [Alzheimer's Disease Biomarkers](/diseases/alzheimers-disease-biomarkers)
• [Amyloid Cascade Pathway](/mechanisms/amyloid-cascade-hypothesis)
• [Apolipoprotein E](/genes/apoe)
• [Tau Pathology Pathway](/mechanisms/tau-pathology)

External Links

• [UniProt: Clusterin](https://www.uniprot.org/uniprot/P10909)
• [PDB: 4J7Y](https://www.rcsb.org/structure/4J7Y)
• [GeneCards: CLU](https://www.genecards.org/cgi-bin/carddisp.pl?gene=CLU)
• [OMIM: CLU](https://www.omim.org/entry/185430)
• [IGAP: CLU Genetics](http://genetics.plos.org/plosgenetics/)
• [Allen Human Brain Atlas - CLU Expression](https://human.brain-map.org/microarray/search/show?search_term=CLU)
• [Allen Mouse Brain Atlas - CLU](https://mouse.brain-map.org/)
• [Allen Cell Type Atlas - Clusterin](https://celltypes.brain-map.org/)

References