Recombinant Human Lon protease homolog, mitochondrial (LONP1), partial

1. mitochondrial ATP-dependent Lon protease may serve as a potential biomarker for cancer diagnosis and novel target for the development of anticancer drugs and for predicting of the efficiency and effectiveness of chemotherapy of a variety of cancers. PMID: 29178076
2. We demonstrate that Lon plays a key role in glioma cell hypoxic survival and mitochondrial respiration, and propose Lon as a promising therapeutic target in the treatment of malignant gliomas. PMID: 27764809
3. Some features were not consistent with CODAS syndrome but overlapped with Marinesco-Sjogren syndrome, a multisystem disorder caused by a mutation in SIL1. An atypical mutation site may result in atypical presentation of the LONP1 mutation PMID: 28148925
4. LONP1 function and implication in human aging and disease was reviewed. PMID: 27387767
5. we observed that Lon protease downregulation is linked to a higher lipofuscinogenesis whereas the application of the mitochondrial-targeted antioxidant mitoTEMPO is able to prevent the accumulation of this protein aggregate. PMID: 28160744
6. Lon preferentially degrades the phosphorylated subunits of CcO and plays a role in the regulation of CcO activity in hypoxia and ischemia/reperfusion injury. PMID: 28442264
7. Lon protease (Lonp1), which is a key inductive of mitochondrial unfolded protein response (UPR(mt)) and is required to maintain the mitochondrial quality, was greatly induced in H. pylori infected gastric epithelial cells. PMID: 27108387
8. This analysis revealed that LONM specifically recognises and degrades unfolded, but not aggregated proteins. PMID: 26627475
9. Mutations of Lon, which likely impair its chaperone properties, are at the basis of a genetic inherited disease named the cerebral, ocular, dental, auricular, skeletal (CODAS) syndrome. (Review) PMID: 27033304
10. Inhibition of Lon protease by triterpenoids alters mitochondria and is associated to cell death in human cancer cells. PMID: 26314956
11. Lon downregulation attenuated hypoxia-induced cardiomyocyte apoptosis through a reduction of reactive oxygen species level. PMID: 25922169
12. LONP1 encodes an enzyme of bacterial ancestry that participates in protein turnover within the mitochondrial matrix, and mutations in its ATP-binding and proteolytic domains cause CODAS syndrome. PMID: 25808063
13. A review on the recent discoveries concerning Lon Protease functions. [review] PMID: 26363553
14. These results suggest that the mechanism underlying cell survival regulated by Lon is mediated by the maintenance of the protein stability of Hsp60-mtHsp70 complex. PMID: 25675302
15. Silencing of SIRT3 increased the levels of Lon protein and of its acetylation, suggesting that Lon is a target of SIRT3, likely at K917. PMID: 25128872
16. the structure of human mitochondrial Lon (hLon) protease, is reported. PMID: 25369343
17. We establish a link between LONP1 and CODAS syndrome in humans. PMID: 25574826
18. Lonp1 has a protective role against ochratoxin a induced cytotoxicity in kidney cells. PMID: 24565693
19. StAR proteolysis is executed by at least 2 mitochondrial proteases, the matrix LON protease and the inner membrane complexes of the metalloproteases AFG3L2 and AFG3L2:SPG7/paraplegin. PMID: 24422629
20. Lon protease deficiency led to an increase in ROS production and to an accumulation of carbonylated protein in the mitochondria. PMID: 24355201
21. Down-regulation of overexpressed human LON in cervical cancer suppresses cell proliferation and bioenergetics. PMID: 24260536
22. Data indicate that SDH5 is protected from mitochondrial LON protease (LONM)-mediated degradation in mitochondria by its stable interaction with SDHA, a state that is dysregulated in hereditary paraganglioma 2 (PGL2). PMID: 24414418
23. Lon is overexpressed specifically in various types of cancer tissue including oral cancer. PMID: 23788038
24. In cells with normal mitochondrial DNA levels, phosphorylated TFAM is degraded by Lon. PMID: 23201127
25. Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells. PMID: 21659532
26. Downregulation of mitochondrial lon protease impairs mitochondrial function and causes hepatic insulin resistance in human liver SK-HEP-1 cells. PMID: 21347624
27. The promoter of Lon is at least part responsible for the upregulation of this protein during oxidative stress. PMID: 20933102
28. Data show that Lon gene can be significantly downregulated by introduction of siRNA to result in enhanced sensitivity of MCF7 cells to UV, cisplatin and heat stress. PMID: 17584658
29. may prevent extensive oxidation, aggregation and accumulation of aconitase, which could otherwise compromise mitochondrial function and cellular viability PMID: 12198491
30. Lon participates directly in the metabolism of mtDNA. PMID: 14739292
31. results indicate that mitochondrial Lon is required for normal survival and proliferation; a clear impetus for Lon's evolutionary conservation PMID: 15683722
32. Results demonstrate that mitochondrial DNA binding is a physiological function of Lon and that cellular levels of Lon influence sensitivity to mtDNA damage. PMID: 17420247
33. A review of the current knowledge on both catalytic mechanisms and inhibitors of Lon protease. PMID: 18021745
34. Electrophoretic mobility shift assay and circular dichroism show that ssDNAs with a propensity for forming parallel G-quartets are specifically bound by hLon. PMID: 18174225

Show More

Hide All

HGNC: 9479

OMIM: 600373

KEGG: hsa:9361

STRING: 9606.ENSP00000353826

UniGene: Hs.350265