Related Experiment Video
Updated: May 29, 2026
10:16
In Vitro Enzyme Measurement to Test Pharmacological Chaperone Responsiveness in Fabry and Pompe Disease
Published on: December 20, 2017
[Fabry-Anderson disease: current state of knowledge]
Olynka Vega-Vega1, Angélica Pérez-Gutiérrez, Ricardo Correa-Rotter
1Departamento de Nefrología y Metabolismo Mineral, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Tlalpan, México, DF. olynkavega@hotmail.com
Summary
Fabry-Anderson disease, a lysosomal disorder from alpha-galactosidase deficiency, causes glycosphingolipid buildup. This review covers its epidemiology, genetics, clinical forms, and enzyme replacement therapy.
Area of Science:
- Biochemistry
- Genetics
- Medical Science
Context:
- Fabry-Anderson disease is a rare lysosomal storage disorder.
- It stems from a deficiency in the enzyme alpha-galactosidase.
- This leads to harmful glycosphingolipid accumulation in cells.
Purpose:
- To review the epidemiology of Fabry-Anderson disease.
- To detail the metabolic defect, molecular, and genetic basis.
- To discuss clinical presentations and enzyme replacement therapy.
Summary:
- The review examines Fabry-Anderson disease, a lysosomal storage disorder caused by alpha-galactosidase deficiency.
- This defect leads to glycosphingolipid accumulation, affecting organs like the heart, kidneys, and nervous system.
- It highlights the challenges in diagnosing partial enzyme deficits and the need for epidemiological data.
Impact:
- Provides a comprehensive overview of Fabry-Anderson disease.
- Aids in understanding the genetic and metabolic underpinnings.
- Informs diagnosis, management, and therapeutic strategies, including enzyme replacement therapy.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:22Lysosomal Hydrolases
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
01:21Smooth Endoplasmic Reticulum
Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
01:24Parkinson Disease ll: Pathophysiology
Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
01:24Cirrhosis II: Pathophysiology
Cirrhosis is a progressive chronic liver injury caused by prolonged inflammation, excessive fibrotic remodeling, and impaired regeneration. Over time, repeated hepatic insults disrupt the liver’s architecture and function, leading to reduced blood flow, impaired bile drainage, and diminished metabolic capacity.Pathophysiology of cirrhosisCirrhosis arises from three main responses to chronic liver damage: inflammation, immune activation, and hepatocyte death. These processes lead to structural...