| The Batten disease gene product CLN5 is the lysosomal bis(monoacylglycero)phosphate synthase. | The Batten disease gene product CLN5 is the lysosomal bis(monoacylglycero)phosphate synthase.
Medoh UN, Hims A, Chen JY, Ghoochani A, Nyame K, Dong W, Abu-Remaileh M. | 09/18/2023 |
| Lysosomal dysfunction, autophagic defects, and CLN5 accumulation underlie the pathogenesis of KCTD7-mutated neuronal ceroid lipofuscinoses. | Lysosomal dysfunction, autophagic defects, and CLN5 accumulation underlie the pathogenesis of KCTD7-mutated neuronal ceroid lipofuscinoses.
Wang Y, Wang H, Wang C., Free PMC Article | 06/14/2023 |
| Cln5 represents a new type of cysteine-based S-depalmitoylase linked to neurodegeneration. | Cln5 represents a new type of cysteine-based S-depalmitoylase linked to neurodegeneration.
Luebben AV, Bender D, Becker S, Crowther LM, Erven I, Hofmann K, Söding J, Klemp H, Bellotti C, Stäuble A, Qiu T, Kathayat RS, Dickinson BC, Gärtner J, Sheldrick GM, Krätzner R, Steinfeld R., Free PMC Article | 05/7/2022 |
| Deficiency of the Lysosomal Protein CLN5 Alters Lysosomal Function and Movement. | Deficiency of the Lysosomal Protein CLN5 Alters Lysosomal Function and Movement.
Basak I, Hansen RA, Ward ME, Hughes SM., Free PMC Article | 01/22/2022 |
| CLN5 in heterozygosis may protect against the development of tumors in a VHL patient. | CLN5 in heterozygosis may protect against the development of tumors in a VHL patient.
de Rojas-P I, Albiñana V, Recio-Poveda L, Rodriguez-Rufián A, Cuesta ÁM, Botella LM., Free PMC Article | 07/31/2021 |
| Association of the Recurrent Rare Variant c.415T>C p.Phe139Leu in CLN5 With a Recessively Inherited Macular Dystrophy. | Association of the Recurrent Rare Variant c.415T>C p.Phe139Leu in CLN5 With a Recessively Inherited Macular Dystrophy.
Magliyah MS, Geuer S, Alsalamah AK, Lenzner S, Drasdo M, Schatz P., Free PMC Article | 07/3/2021 |
| Novel likely disease-causing CLN5 variants identified in Pakistani patients with neuronal ceroid lipofuscinosis. | Novel likely disease-causing CLN5 variants identified in Pakistani patients with neuronal ceroid lipofuscinosis.
Azad B, Efthymiou S, Sultan T, Scala M, Alvi JR, Neuray C, Dominik N, SYNaPS Study Group, Gul A, Houlden H., Free PMC Article | 05/15/2021 |
| The Neuronal Ceroid Lipofuscinoses-Linked Loss of Function CLN5 and CLN8 Variants Disrupt Normal Lysosomal Function. | The Neuronal Ceroid Lipofuscinoses-Linked Loss of Function CLN5 and CLN8 Variants Disrupt Normal Lysosomal Function.
Parvin S, Rezazadeh M, Hosseinzadeh H, Moradi M, Shiva S, Gharesouran J. | 02/6/2021 |
| This is the first report of whole gene deletion in combination with a novel pathogenic sequence variant in a CLN5 patient. The two mutations detected with whole exome sequencing simultaneously proved the advantage of the sequencing technology for genetic diagnostics | A novel pathogenic frameshift variant unmasked by a large de novo deletion at 13q21.33-q31.1 in a Chinese patient with neuronal ceroid lipofuscinosis type 5.
Li W, Fan X, Zhang Y, Huang L, Jiang T, Qin Z, Su J, Luo J, Yi S, Zhang S, Shen Y., Free PMC Article | 07/18/2020 |
| This study demonstrated that Novel Mutations in CLN5 of Chinese Patients With Neuronal Ceroid Lipofuscinosis. | Novel Mutations in CLN5 of Chinese Patients With Neuronal Ceroid Lipofuscinosis.
Ge L, Li HY, Hai Y, Min L, Xing L, Min J, Shu HX, Mei OY, Hua L. | 10/5/2019 |
| The onset of visual deficits was much delayed. Computed tomography and MRI showed that brain structures and volumes remained stable. Because gene therapy in humans is more likely to begin after clinical diagnosis, self-complementary AAV9-CLN5 was injected into the brain ventricles of four 7-month-old affected sheep already showing early clinical signs in a second trial. | Longitudinal In Vivo Monitoring of the CNS Demonstrates the Efficacy of Gene Therapy in a Sheep Model of CLN5 Batten Disease.
Mitchell NL, Russell KN, Wellby MP, Wicky HE, Schoderboeck L, Barrell GK, Melzer TR, Gray SJ, Hughes SM, Palmer DN., Free PMC Article | 08/17/2019 |
| We identified a missense variant in CLN5 c.A959G (p.Asn320Ser) that segregated with Alzheimer's disease. We find that this variant causes glycosylation defects in the expressed protein, which causes it to be retained in the endoplasmic reticulum with reduced delivery to the endolysosomal compartment, CLN5's normal cellular location. | An Alzheimer's Disease-Linked Loss-of-Function CLN5 Variant Impairs Cathepsin D Maturation, Consistent with a Retromer Trafficking Defect.
Qureshi YH, Patel VM, Berman DE, Kothiya MJ, Neufeld JL, Vardarajan B, Tang M, Reyes-Dumeyer D, Lantigua R, Medrano M, Jiménez-Velázquez IJ, Small SA, Reitz C., Free PMC Article | 06/29/2019 |
| Genotype-phenotype correlation between CNL5 gene mutations and CNL5 disease symptoms. | Phenotype and natural history of variant late infantile ceroid-lipofuscinosis 5.
Simonati A, Williams RE, Nardocci N, Laine M, Battini R, Schulz A, Garavaglia B, Moro F, Pezzini F, Santorelli FM. | 07/22/2017 |
| We conclude that, whereas sleep homeostasis is present in CLN5(-/-) sheep, underlying CLN5(-/-) disease processes prevent its full expression, even at early stages. | An EEG Investigation of Sleep Homeostasis in Healthy and CLN5 Batten Disease Affected Sheep.
Perentos N, Martins AQ, Cumming RJ, Mitchell NL, Palmer DN, Sawiak SJ, Morton AJ., Free PMC Article | 07/15/2017 |
| findings support CLN5 hypomorphic mutations cause autosomal recessive cerebellar ataxia, confirming other reports showing CLN mutations are associated with adult-onset neurodegenerative disorders | Adult-onset autosomal recessive ataxia associated with neuronal ceroid lipofuscinosis type 5 gene (CLN5) mutations.
Mancini C, Nassani S, Guo Y, Chen Y, Giorgio E, Brussino A, Di Gregorio E, Cavalieri S, Lo Buono N, Funaro A, Pizio NR, Nmezi B, Kyttala A, Santorelli FM, Padiath QS, Hakonarson H, Zhang H, Brusco A. | 04/9/2016 |
| Two forms of CLN5, derived from the C-terminal proteolytic processing, are present in most cells and tissues. | Proteolytic processing of the neuronal ceroid lipofuscinosis related lysosomal protein CLN5.
De Silva B, Adams J, Lee SY., Free PMC Article | 01/2/2016 |
| There are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5. | The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
Moharir A, Peck SH, Budden T, Lee SY., Free PMC Article | 06/21/2014 |
| a role for CLN5 in controlling the itinerary of the lysosomal sorting receptors by regulating retromer recruitment at the endosome | The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting.
Mamo A, Jules F, Dumaresq-Doiron K, Costantino S, Lefrancois S., Free PMC Article | 07/6/2013 |
| This study highlights a close interaction between CLN5/CLN8 proteins, and their role in sphingolipid metabolism. Our findings suggest that CLN5p/CLN8p most likely are positive modulators of CerS1 and/or CerS2. | CLN5 and CLN8 protein association with ceramide synthase: biochemical and proteomic approaches.
Haddad SE, Khoury M, Daoud M, Kantar R, Harati H, Mousallem T, Alzate O, Meyer B, Boustany RM. | 05/4/2013 |
| analysis of mutations in neuronal ceroid lipofuscinosis protein CLN5 | The neuronal ceroid lipofuscinosis protein CLN5: new insights into cellular maturation, transport, and consequences of mutations.
Schmiedt ML, Bessa C, Heine C, Ribeiro MG, Jalanko A, Kyttälä A. | 10/30/2010 |
| CLN5 mutations are 1) more common in patients with neuronal ceroid lipofuscinosis (NCL) than previously reported, 2) found in patients of broad ethnic diversity, and 3) can be identified in patients with disease onset in adult and juvenile epochs | CLN5 mutations are frequent in juvenile and late-onset non-Finnish patients with NCL.
Xin W, Mullen TE, Kiely R, Min J, Feng X, Cao Y, O'Malley L, Shen Y, Chu-Shore C, Mole SE, Goebel HH, Sims K, Xin W, Mullen TE, Kiely R, Min J, Feng X, Cao Y, O'Malley L, Shen Y, Chu-Shore C, Mole SE, Goebel HH, Sims K. | 03/15/2010 |
| Study found that CLN5 interacts with several other NCL proteins namely, CLN1/PPT1, CLN2/TPP1, CLN3, CLN6 and CLN8. | Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins.
Lyly A, von Schantz C, Heine C, Schmiedt ML, Sipilä T, Jalanko A, Kyttälä A., Free PMC Article | 01/21/2010 |
| Double immunofluorescence microscopy showed that while the wild-type CLN5 protein is localized in lysosomes, both mutant CLN5 proteins are retained in the endoplasmic reticulum rather than reaching the lysosome. | Retention of lysosomal protein CLN5 in the endoplasmic reticulum causes neuronal ceroid lipofuscinosis in Asian sibship.
Lebrun AH, Storch S, Rüschendorf F, Schmiedt ML, Kyttälä A, Mole SE, Kitzmüller C, Saar K, Mewasingh LD, Boda V, Kohlschütter A, Ullrich K, Braulke T, Schulz A. | 01/21/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (2) articlesCLN5 mutations are frequent in juvenile and late-onset non-Finnish patients with NCL.
Xin W, Mullen TE, Kiely R, Min J, Feng X, Cao Y, O'Malley L, Shen Y, Chu-Shore C, Mole SE, Goebel HH, Sims K, Xin W, Mullen TE, Kiely R, Min J, Feng X, Cao Y, O'Malley L, Shen Y, Chu-Shore C, Mole SE, Goebel HH, Sims K. Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis.
Kousi M, Siintola E, Dvorakova L, Vlaskova H, Turnbull J, Topcu M, Yuksel D, Gokben S, Minassian BA, Elleder M, Mole SE, Lehesjoki AE. | 03/25/2009 |
| In cultures of brain microvascular endothelial cells, VEGF-A specifically down-regulated CLN-5 and OCLN protein and mRNA | VEGF-mediated disruption of endothelial CLN-5 promotes blood-brain barrier breakdown.
Argaw AT, Gurfein BT, Zhang Y, Zameer A, John GR., Free PMC Article | 01/21/2010 |