Defective Protein Folding and Aggregation as the Basis of Neurodegenerative Diseases: The Darker Aspect of Proteins

被引:59
作者
Naeem, Aabgeena [1 ]
Fazili, Naveed Ahmad [1 ]
机构
[1] Aligarh Muslim Univ, Fac Life Sci, Dept Biochem, Aligarh 202002, Uttar Pradesh, India
关键词
Aggregation; Conformational diseases; Protein misfolding; Molecular chaperones; AMYOTROPHIC-LATERAL-SCLEROSIS; AMYLOID FIBRIL FORMATION; HEAT-SHOCK PROTEINS; FRONTOTEMPORAL LOBAR DEGENERATION; PARTIALLY FOLDED INTERMEDIATE; PARKINSONS-DISEASE; ALPHA-SYNUCLEIN; CYSTIC-FIBROSIS; MOLECULAR CHAPERONES; ALZHEIMERS-DISEASE;
D O I
10.1007/s12013-011-9200-x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ability of a polypeptide to fold into a unique, functional, and three-dimensional structure depends on the intrinsic properties of the amino acid sequence, function of the molecular chaperones, proteins, and enzymes. Every polypeptide has a finite tendency to misfold and this forms the darker side of the protein world. Partially folded and misfolded proteins that escape the cellular quality control mechanism have the high tendency to form inter-molecular hydrogen bonding between the same protein molecules resulting in aggregation. This review summarizes the underlying and universal mechanism of protein folding. It also deals with the factors responsible for protein misfolding and aggregation. This article describes some of the consequences of such behavior particularly in the context of neurodegenerative conformational diseases such as Alzheimer's, Parkinson's, Huntington's, amyotrophic lateral sclerosis and other non-neurodegenerative conformational diseases such as cancer and cystic fibrosis etc. This will encourage a more proactive approach to the early diagnosis of conformational diseases and nutritional counseling for patients.
引用
收藏
页码:237 / 250
页数:14
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