Дисертації з теми "Lysosomal storage disorder (LSD)"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-15 дисертацій для дослідження на тему "Lysosomal storage disorder (LSD)".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте дисертації для різних дисциплін та оформлюйте правильно вашу бібліографію.
Roy, Elise. "Cell disorders in lysosomal storage diseases." Phd thesis, Université René Descartes - Paris V, 2012. http://tel.archives-ouvertes.fr/tel-00683248.
Повний текст джерелаMason, Lyndel Ann. "Expression variation in lysosomal storage disorder genes." Thesis, Queensland University of Technology, 2006. https://eprints.qut.edu.au/16240/1/Lyndel_Mason_Thesis.pdf.
Повний текст джерелаMason, Lyndel Ann. "Expression variation in lysosomal storage disorder genes." Queensland University of Technology, 2006. http://eprints.qut.edu.au/16240/.
Повний текст джерелаLangford-Smith, Alexander William Walker. "Lentiviral vector mediated haematopoietic stem cell gene therapy for mucopolysaccharidosis type IIIA." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/lentiviral-vector-mediated-haematopoietic-stem-cell-gene-therapy-for-mucopolysaccharidosis-type-iiia(89f8e108-58f3-42bb-8b80-0e0a1fe45fd7).html.
Повний текст джерелаMauri, Victor [Verfasser]. "Trehalose mediated enhancement of glycosaminoglycan degradation in the lysosomal storage disorder Mucopolysaccharidosis III / Victor Mauri." Köln : Deutsche Zentralbibliothek für Medizin, 2014. http://d-nb.info/1047324342/34.
Повний текст джерелаHuynh, Julie. "ESCRT-Dependent Cell Death in a Caenorhabditis elegans Model of the Lysosomal Storage Disorder Mucolipidosis Type IV." Thesis, The University of Arizona, 2015. http://hdl.handle.net/10150/595811.
Повний текст джерелаDe, Silva Weerakonda Arachchige Bhagya Nilukshi. "A study of neuronal ceroid lipofuscinosis proteins CLN5 and CLN8." Thesis, Kansas State University, 2015. http://hdl.handle.net/2097/35749.
Повний текст джерелаBiochemistry and Molecular Biophysics Interdepartmental Program
Stella Yu-Chien Lee
Neuronal ceroid lipofuscinoses (NCLs) are a group of neurodegenerative lysosomal storage disorders which is the most frequent group of inherited neurodegenerative disorders that affect children leading to severe pathological conditions such as progressive loss of motor neuron functions, loss of vision, mental retardation, epilepsy, ataxia and atrophy in cerebral, cerebella cortex and retina and eventually premature death. Among the many genes that cause NCL, mutations in CLN5 leads to different forms of NCL (infantile, late infantile, juvenile and adult) and mutations in CLN8 leads to progressive epilepsy with mental retardation (EPMR) and a variant late infantile form of NCL. The function(s) of both CLN5 and CLN8 proteins remain elusive. CLN5 is a glycosylated soluble protein that resides in the lysosome. We observed that endogenous CLN5 protein exist in two forms and identified a previously unknown C-terminal proteolytic processing event of CLN5. Using a cycloheximide chase experiment we demonstrated that the proteolytic processing of CLN5 is a post-translational modification. Furthermore treatment with chloroquine showed the processing occurs in low pH cellular compartments. After treatment with different protease inhibitors our results suggested the protease involved in the processing of CLN5 could be a cysteine protease. Using two glycosylation mutants of CLN5, retained in the endoplasmic reticulum (ER) or the Golgi we showed the proteolytic processing occurs in an organelle beyond the ER. This study contributes to understanding the characteristics of the CLN5 protein. CLN8 is an ER resident transmembrane protein that shuttles between the ER and the ER-Golgi intermediate compartment (ERGIC). In our study we identified a potential interaction between CLN8 and a PP2A holoenzyme complex consisting regulatory subunit A α isoform and regulatory subunit B α isoform. Using two CLN8 patient derived fibroblast cell lines we were able to show that the phosphorylated levels of PP2A target kinase Akt was reduced at both of its regulatory sites Ser473 and Thr308 and the activity of PP2A was increased. A delay of ceramide transport from ER to Golgi in CLN8 deficient patient cell lines was observed using BODIPY FL C5-Ceramide staining. Our results provide evidence for CLN8 protein being involved in the regulation of PP2A activity and trafficking of ceramide from ER to Golgi.
Di, Malta Chiara. "The analysis of a mouse model of Lysosomal Storage Disorder uncovers a role for astrocyte dysfunction in neurodegeneration." Thesis, Open University, 2012. http://oro.open.ac.uk/54503/.
Повний текст джерелаHersh, Bradley Michael 1973. "C. elegans apoptosis : CED-4 translocation and involvement in a model of mucolipidosis type IV human lysosomal storage disorder." Thesis, Massachusetts Institute of Technology, 2001. http://hdl.handle.net/1721.1/8305.
Повний текст джерелаIncludes bibliographical references.
The process of programmed cell death is important in the development and homeostasis of multicellular organisms. The conserved morphological events of this process have been termed apoptosis. The molecular mechanisms of apoptosis execution are also conserved. We have investigated the behavior of these shared components during programmed cell death in the nematode Caenorhabditis elegans. We have found that the CED-9 protein, an anti-apoptotic member of the Bcl-2 family of apoptotic regulators, is required for the sequestering of the CED-4 cell-death activator to mitochondria. In the absence of CED-9 in C. elegans embryos, we found that CED-4 protein translocates to the nuclear membrane. In addition, inducing excess programmed cell death by expression of the EGL-1 cell-death activator triggers the translocation of CED-4 from mitochondria to the nuclear membrane. We performed a genetic screen for mutations that trigger programmed cell death in ced-9 gain-of-function animals where cell death is blocked. We identified a mutation in cup-5, the C. elegans homolog of the human mucolipidosis type IV gene, which is mutated in a lysosomal storage disorder. We found that cup-5 is required for viability and that excess lysosomes accumulate in cup-5 mutants. In addition, cup--5 mutants contain excess programmed cell deaths, suggesting that apoptosis may play a role in the pathology of mucolipidosis type IV.
by Bradley Michael Hersh.
Ph.D.
Budden, Theodore. "CLN5 deficiency results in alterations in the activation of autophagy." Thesis, Kansas State University, 2014. http://hdl.handle.net/2097/20473.
Повний текст джерелаDepartment of Biology
Stella Y. Lee
CLN5 is one of several proteins that when mutated result in the lysosomal storage disorder (LSD) Neuronal Ceroid Lipofuscinosis (NCL). CLN5 is a soluble lysosomal protein that has no known function at this time. Previously we showed that eight asparagine residues in CLN5 are N-glycosylated, and that this modification is important for the protein’s transport and function. Now, we have identified a link between the activation of autophagy and CLN5 deficiency. The autophagy-lysosomal protein degradation system is one of the major pathways the cell uses to degrade intracellular material and recycle cellular building blocks. It was recently shown that other CLN proteins affect the relative level of autophagy, indicating a potential link between the autophagy pathway and the NCLs. By knocking down endogenous CLN5 in HeLa we showed that, upon stress induction, cells responded with higher levels of autophagy activation. Consistent with these knockdown experiments, there is a higher level of the autophagy marker protein, LC3-II, in CLN5 patient cells that are naturally deficient for the CLN5 protein. Pharmaceutical induction of autophagy through different means also showed higher LC3-II levels compared to control, though patterns differed in the type of autophagy induced. In summary, we discovered that the autophagy pathway is altered in CLN5 deficient cells, indicating a potential role for CLN5 in autophagy. Further analyses of the autophagy pathway will shed light on where CLN5 is acting and the mechanism by which defective CLN5 causes NCL.
OulaÏdi, Farah. "Conception et synthèse d'iminoglycolipides comme inhibiteurs d'enzymes lysosomales à effet chaperon pharmacologique." Thesis, Orléans, 2011. http://www.theses.fr/2011ORLE2001/document.
Повний текст джерелаChaperone Mediated Therapy represents an innovative and strategic approach to treat lysosomal storage disorders which a class of rare genetic diseases. Competitive inhibitors for some of these lysosomal enzymes can, at sub inhibitory concentrations, act as chaperones and rescue the mutant proteins. In fact, enzymes carrying some mutations are still catalytically active. α-1-C-alkyl iminoxylitols represent a class of iminosugars which mimic the “gluco” configuration of the substrate and give powerful inhibitors of β-glucocerebrosidase, the enzyme involved in Gaucher disease. Moreover, this class of iminosugars, synthesized by our group, act as pharmacological chaperones and are able to double the residual activity of the N370S mutant. In order to synthesize more efficiently these iminosugars, the synthetic strategy was improved and optimized. Moreover, we focused our investigations on structural variations on our lead compound (α-1-C9 iminoxylitol) and draw important conclusions on structure-activity relationship. Then, we extended our expertise on iminosugars as pharmacological chaperones to another lysosomal glycosidase. In paricular, we targeted β-galactocerebrosidase, the enzyme responsible for Krabbe disease, and synthesized a series of iminosugars which mimic the “galacto” configuration. Biological assays were performed on our compounds to determine their activity as inhibitors and for some of them, their chaperone effects
Kongmanas, Kessiri. "Roles of Seminolipid and Its Associated Membrane Domain in Male Fertility." Thesis, Université d'Ottawa / University of Ottawa, 2015. http://hdl.handle.net/10393/32509.
Повний текст джерелаCamps, Bres Flora. "Synthèse d'aminocyclitols, inhibiteurs potentiels de glycosidases lysosomales, via des aldolases." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2010. http://tel.archives-ouvertes.fr/tel-00629666.
Повний текст джерелаWhyte, Lauren Sue. "The role of heterozygous lysosomal storage disorder alleles as risk factors for dementia." Thesis, 2019. http://hdl.handle.net/2440/123399.
Повний текст джерелаThesis (Ph.D.) -- University of Adelaide, Adelaide Medical School, 2020
Martinho, Sara Isabel da Silva. "Doença de Gaucher e seu tratamento: uma revisão narrativa." Master's thesis, 2021. http://hdl.handle.net/10284/10857.
Повний текст джерелаGaucher disease is a rare, autosomal recessive disease that results from an abnormal accumulation of a lipid substance known as glucocerebroside or glucosylceramide. Normally, glucoderebroside is metabolized by the enzyme glucocerebrosidase (or acid β-glucosidase). The mutations in the glucocerebrosidase 1 gene, are the most prevalent cause of all forms of Gaucher disease. This genetic alteration means that the enzyme does not work properly or is completely absent. This, in turn, leads to the accumulation of glucocerebroside in cells. It is because of this clumping that Gaucher disease is called a storage disorder and, as the accumulation occurs in the lysosome, it is a lysosomal storage disorder (also know as lysosomal storage disease, or sphingolipidosis) in which this excess of lipids happens in macrophages. The accumulation of lipids in cells in Gaucher disease is different for each person, resulting in unequal symptomatology that varies considerably from patient to patient. Some people have severe symptoms in childhood, while others have no symptoms or only mild symptoms and are diagnosed later in life. Gaucher disease patients may manifest neurological damage, three main types of Gaucher disease have been described over time, based on the absence (type 1), presence (type 2 and type 3) or the severity of neurological characteristics. A complex multisystem phenomenon arises involving the liver, spleen, bone marrow and, occasionally, the lungs, with cases of progressive neurodegenerative disease still occurring. Enzyme replacement treatment became the standard of therapy in 1991, transforming the natural history of Gaucher disease. Currently, treatments for Gaucher disease, clinically used for the systemic type of disease, include enzyme replacement therapy, substrate reduction therapy, and hematopoietic stem cell transplantation, although the latter is the only successful option for patients with the neuronopathic types of Gaucher disease. This work aims to make a narrative review of Gaucher disease, considering, in particular, the treatment used.