Analysis of F2 and backcross animals has confirmed the X-chromosome linkage of Ags, the structural locus for mouse alpha-galactosidase. The position of Ags has been located in the X chromosome, 9 centimorgans from Mo, and the gene order is centromere-Hq-Bn-Ta-Mo-Ags. A variation in the developmental expression of alpha-galactosidase activity, inherited as an autosomal trait, has been characterized using recombinant inbred lines of mice. Among certain recombinant inbred lines, the variation appears to segregate as a single major locus.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1213804 | PMC |
| http://dx.doi.org/10.1093/genetics/88.2.327 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The interaction of tPA with NMDAR1 drives neuroinflammation and neurodegeneration in α-synuclein-mediated neurotoxicity.
J Neuroinflammation
January 2025
Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI, USA.
The thrombolytic protease tissue plasminogen activator (tPA) is expressed in the CNS, where it regulates diverse functions including neuronal plasticity, neuroinflammation, and blood-brain-barrier integrity. However, its role in different brain regions such as the substantia nigra (SN) is largely unexplored. In this study, we characterize tPA expression, activity, and localization in the SN using a combination of retrograde tracing and β-galactosidase tPA reporter mice.
View Article and Find Full Text PDFTargeting p97/Valosin-Containing Protein Promotes Hepatic Stellate Cell Senescence and Mitigates Liver Fibrosis.
DNA Cell Biol
January 2025
Research Center of Integrated Traditional Chinese and Western Medicine, The Affiliated Traditional Chinese Medicine Hospital, Southwest Medical University, Luzhou 646000, China.
Liver fibrosis, one of the main histological determinants of various chronic liver diseases, currently lacks effective treatment. Hepatic stellate cells (HSCs) are pivotal in the production of extracellular matrix and amplify the fibrogenic response. Inhibiting the activation of HSCs or promoting the senescence of activated HSCs is crucial for the regression of liver fibrosis.
View Article and Find Full Text PDFUse of a mouse-human chimeric anti-α-galactosidase A monoclonal antibody as a reference for measuring serum antidrug antibody titers in patients with Fabry disease.
Mol Genet Metab
January 2025
Department of Clinical Genetics, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204-8588, Japan. Electronic address:
The detection of antidrug antibodies (ADAs) is important for monitoring patients with Fabry disease who are undergoing enzyme replacement therapy (ERT) with recombinant α-galactosidase A (GLA) drugs, as ADAs can cause allergic reactions and reduce therapeutic efficacy. Various immunological methods, particularly enzyme-linked immunosorbent assay (ELISA), are widely used to measure serum ADA titers in patients with Fabry disease. However, estimating and comparing results of ELISA is challenging because of the absence of a reference antibody.
View Article and Find Full Text PDFPreclinical efficacy and safety of adeno-associated virus 5 alpha-galactosidase: A gene therapy for Fabry disease.
Mol Ther Methods Clin Dev
December 2024
uniQure biopharma B.V., Amsterdam 1105 BP, the Netherlands.
We developed a novel adeno-associated virus 5 gene therapy (AAV5-GLA) expressing human alpha-galactosidase A (GLA) under the control of a novel, small and strong, liver-restricted promoter. We assessed the preclinical potential of AAV5-GLA for treating Fabry disease, an X-linked hereditary metabolic disorder resulting from mutations in the gene encoding GLA that lead to accumulation of the substrates globotriaosylceramide and globotriaosylsphingosine, causing heart, kidney, and central nervous system dysfunction. Effects of intravenously administered AAV5-GLA were evaluated in (1) GLA-knockout mice aged 7-8 weeks (early in disease) and 20 weeks (nociception phenotype manifestation) and (2) cynomolgus macaques during an 8-week period.
View Article and Find Full Text PDFTargeted nanoliposomes to improve enzyme replacement therapy of Fabry disease.
Sci Adv
December 2024
Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina, Instituto de Salud Carlos III, Madrid, Spain.
The central nervous system represents a major target tissue for therapeutic approach of numerous lysosomal storage disorders. Fabry disease arises from the lack or dysfunction of the lysosomal alpha-galactosidase A (GLA) enzyme, resulting in substrate accumulation and multisystemic clinical manifestations. Current enzyme replacement therapies (ERTs) face limited effectiveness due to poor enzyme biodistribution in target tissues and inability to reach the brain.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!