>Neurodegeneration and Neurodegenerative Disease
Neurodegeneration and Neurodegenerative Disease
Sino Biological offers a comprehensive set of tools for research on neurodegeneration and neurodegenerative diseases, including recombinant proteins, antibodies, ELISA kits, and cDNA clones.
Neurodegeneration and Neurodegenerative Disease Related Products Index
Neurodegeneration and Neurodegenerative Disease Background
Neurodegeneration is referred to as the progressive loss of structure and function of neurons. Neurodegenerative diseases constitute one of the major challenges of modern medicine, including Alzheimer's disease, amyotrophic lateral sclerosis, Huntington's disease, Lyme disease, Parkinson's disease, and so on. These diseases are relatively common and often highly debilitating. However, the mechanisms responsible for their pathologies are poorly understood, and there are currently no effective preventative therapies. Advances in our understanding of the molecular mechanisms underlying nervous system dysfunction are critical for the development of effective treatments. Recent research on the genetic pathways leading to pathology with animal models (mice and Drosophila) begun to identify molecular mechanisms underlying neurodegenerative disorders.
In many of the neurodegenerative diseases, a common feature of genetic mutation is a repeat of the CAG nucleotide triplet within the mutated gene. CAG encodes for the amino acid glutamine. A repeat of CAG results in a polyglutamine (polyQ) tract. Research on the neurodegenerative disease, spinocerebellar ataxia type 1 (SCA1), found out that polyglutamine expansion contributes to disease by both a gain-of-function mechanism and partial loss of function of the SCA1 encoded protein ATXN1. Another important pathological mechanism is alpha-synuclein aggregation. Alpha-synuclein is the primary structural component of Lewy body fibrils. Normally an unstructured soluble protein, alpha-synuclein can aggregate to form insoluble fibrils in pathological conditions characterized by Lewy bodies, such as Parkinson's disease, dementia with Lewy bodiesand multiple system atrophy. Alpha-synuclein pathology is also found in both sporadic and familial cases with Alzheimer's disease.
Strong evidence underscores the tight link between oxidative stress and neurodegenerative disease pathogenesis, including in four of the well known diseases Alzheimer's, Parkinson's, Amyotrophic lateral sclerosis, and Huntington's. Studies suggest that oxidative modification of K+ channels might be a general principle underlying aging and neurodegeneration. The formation of intracellular aggregates by toxic proteins is also a cause of many late-onset neurodegenerative diseases, including Parkinson's disease and Huntington's disease. The degradation pathways acting on such aggregate-prone cytosolic proteins include the ubiquitin-proteasome system and macroautophagy. Dysfunction of the ubiquitin-proteasome or macroautophagy pathways might contribute to the pathology of various neurodegenerative conditions. In addition, current research indicates that cell death in neurodegeneration is generally due to apoptosis and most commonly through the intrinsic mitochondrial pathway.
Neurodegeneration and Neurodegenerative Disease Related Studies
- Arima K, et al. (1998) Immunoelectron-microscopic demonstration of NACP/alpha-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies. Brain Res. 808(1):93-100.
- Yokota O, et al. (2002) NACP/alpha-synuclein, NAC, and beta-amyloid pathology of familial Alzheimer's disease with the E184D presenilin-1 mutation: a clinicopathological study of two autopsy cases. Acta Neuropathol. 104(6):637-48.
- Rubinsztein DC. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature. 443(7113):780-6.
- Bredesen DE, et al. (2006) Cell death in the nervous system. Nature. 443(7113):796-802.
- Thompson LM. (2008) Neurodegeneration: a question of balance. Nature. 452(7188):707-8.
- Marsh JL, et al. (2009) Animal models of polyglutamine diseases and therapeutic approaches. J Biol Chem. 284(12):7431-5.