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A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis
Neuronal Ceroid Lipofuscinosis (NCL), also known as Batten disease, is an incurable childhood brain disease. The thirteen forms of NCL are caused by mutations in thirteen CLN genes. Mutations in one CLN gene, CLN5, cause variant late-infantile NCL, with an age of onset between 4 and 7 years. The CLN...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8195759/ https://www.ncbi.nlm.nih.gov/pubmed/33792748 http://dx.doi.org/10.1007/s00018-021-03813-x |
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author | Basak, I. Wicky, H. E. McDonald, K. O. Xu, J. B. Palmer, J. E. Best, H. L. Lefrancois, S. Lee, S. Y. Schoderboeck, L. Hughes, S. M. |
author_facet | Basak, I. Wicky, H. E. McDonald, K. O. Xu, J. B. Palmer, J. E. Best, H. L. Lefrancois, S. Lee, S. Y. Schoderboeck, L. Hughes, S. M. |
author_sort | Basak, I. |
collection | PubMed |
description | Neuronal Ceroid Lipofuscinosis (NCL), also known as Batten disease, is an incurable childhood brain disease. The thirteen forms of NCL are caused by mutations in thirteen CLN genes. Mutations in one CLN gene, CLN5, cause variant late-infantile NCL, with an age of onset between 4 and 7 years. The CLN5 protein is ubiquitously expressed in the majority of tissues studied and in the brain, CLN5 shows both neuronal and glial cell expression. Mutations in CLN5 are associated with the accumulation of autofluorescent storage material in lysosomes, the recycling units of the cell, in the brain and peripheral tissues. CLN5 resides in the lysosome and its function is still elusive. Initial studies suggested CLN5 was a transmembrane protein, which was later revealed to be processed into a soluble form. Multiple glycosylation sites have been reported, which may dictate its localisation and function. CLN5 interacts with several CLN proteins, and other lysosomal proteins, making it an important candidate to understand lysosomal biology. The existing knowledge on CLN5 biology stems from studies using several model organisms, including mice, sheep, cattle, dogs, social amoeba and cell cultures. Each model organism has its advantages and limitations, making it crucial to adopt a combinatorial approach, using both human cells and model organisms, to understand CLN5 pathologies and design drug therapies. In this comprehensive review, we have summarised and critiqued existing literature on CLN5 and have discussed the missing pieces of the puzzle that need to be addressed to develop an efficient therapy for CLN5 Batten disease. |
format | Online Article Text |
id | pubmed-8195759 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-81957592021-06-28 A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis Basak, I. Wicky, H. E. McDonald, K. O. Xu, J. B. Palmer, J. E. Best, H. L. Lefrancois, S. Lee, S. Y. Schoderboeck, L. Hughes, S. M. Cell Mol Life Sci Review Neuronal Ceroid Lipofuscinosis (NCL), also known as Batten disease, is an incurable childhood brain disease. The thirteen forms of NCL are caused by mutations in thirteen CLN genes. Mutations in one CLN gene, CLN5, cause variant late-infantile NCL, with an age of onset between 4 and 7 years. The CLN5 protein is ubiquitously expressed in the majority of tissues studied and in the brain, CLN5 shows both neuronal and glial cell expression. Mutations in CLN5 are associated with the accumulation of autofluorescent storage material in lysosomes, the recycling units of the cell, in the brain and peripheral tissues. CLN5 resides in the lysosome and its function is still elusive. Initial studies suggested CLN5 was a transmembrane protein, which was later revealed to be processed into a soluble form. Multiple glycosylation sites have been reported, which may dictate its localisation and function. CLN5 interacts with several CLN proteins, and other lysosomal proteins, making it an important candidate to understand lysosomal biology. The existing knowledge on CLN5 biology stems from studies using several model organisms, including mice, sheep, cattle, dogs, social amoeba and cell cultures. Each model organism has its advantages and limitations, making it crucial to adopt a combinatorial approach, using both human cells and model organisms, to understand CLN5 pathologies and design drug therapies. In this comprehensive review, we have summarised and critiqued existing literature on CLN5 and have discussed the missing pieces of the puzzle that need to be addressed to develop an efficient therapy for CLN5 Batten disease. Springer International Publishing 2021-04-01 2021 /pmc/articles/PMC8195759/ /pubmed/33792748 http://dx.doi.org/10.1007/s00018-021-03813-x Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Basak, I. Wicky, H. E. McDonald, K. O. Xu, J. B. Palmer, J. E. Best, H. L. Lefrancois, S. Lee, S. Y. Schoderboeck, L. Hughes, S. M. A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title | A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title_full | A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title_fullStr | A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title_full_unstemmed | A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title_short | A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis |
title_sort | lysosomal enigma cln5 and its significance in understanding neuronal ceroid lipofuscinosis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8195759/ https://www.ncbi.nlm.nih.gov/pubmed/33792748 http://dx.doi.org/10.1007/s00018-021-03813-x |
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