CLU（也稱為apoJ）是一種高度保守的糖蛋白，廣泛存在于多種細(xì)胞類型和組織中。CLU參與了多種生物學(xué)過程，包括細(xì)胞凋亡、炎癥、脂代謝和細(xì)胞遷移等。最近的研究表明，CLU與多種疾病的發(fā)生和發(fā)展有關(guān)，如癌癥、心血管疾病、神經(jīng)系統(tǒng)疾病和肝病等。此外，CLU還可能作為生物標(biāo)志物來評(píng)估某些疾病的診斷和預(yù)后。

Functions as extracellular chaperone that prevents aggregation of non native 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. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms 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. Following stress, promotes apoptosis. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury.

1. Real time RT-PCR and western blotting analysis indicated there was a greater abundance of clusterin in cryptorchid dog testes. Furthermore, clusterin was detected in extracellular regions of cryptorchid dog testes. PMID: 29678567
2. Clusterin may potentially serve as a marker for chronic spinal cord disease in the dog. PMID: 23990410
3. The chaperone action of clusterin targets prefibrillar species to inhibit amyloid formation PMID: 17412999
4. The extracellular chaperone clusterin appears in the cytosol during endoplasmic reticulum stress PMID: 17451556
5. The chaperone action of clusterin is important in quality control of extracellular protein folding PMID: 19878774
6. The chaperone clusterin mediates systemic clearance of extracellular misfolded proteins PMID: 21505792
7. Clusterin is an extracellular holdase-type chaperone PMID: 10066740
8. The chaperone action of clusterin is like that of the small heat shock proteins PMID: 10694874
9. The chaperone action of clusterin is independent of ATP PMID: 11123922
10. Clusterin expression may increase cardiac progenitor cell migration via increasing CXCR4 expression and SDF-1/chemokine receptor signaling in a PI3/Akt-dependent manner. PMID: 20813109

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Secreted. Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Mitochondrion. Mitochondrion membrane. Cytoplasm, perinuclear region. Cytoplasmic vesicle, secretory vesicle, chromaffin granule.

Clusterin family

KEGG: cfa:442971

STRING: 9615.ENSCAFP00000012350

UniGene: Cfa.1254