Role of glutamine deamidation in neurodegenerative diseases associated with triplet repeat expansions: a hypothesis.
The pathological expansion of unstable trinucleotide repeats is known to cause neurodegenerative diseases. Trinucleotide repeat expansions might prove to be pathological through a variety of mechanisms, including alteration of DNA structure, transcription, RNA-protein interaction, and altered protein conformations/interactions. Deamidation of human proteins have been shown to regulate some time-dependent biological processes such as development and aging. In this paper we hypothesize the possible role of glutamine deamidation as a signaling event in the pathogenesis of neurodegenerative diseases associated with triplet repeat expansion.
Hasan
Qurratulain
Q
Department of Genetics and Molecular Medicine, Kamineni Hospitals, LB Nagar, Hyderabad 500 068, India. qhasan2000@yahoo.com
Alluri
Ravindra Varma
RV
Rao
Pragna
P
Ahuja
Yog Raj
YR
D000577:Amides / Q000737:chemistry*; D003937:Diagnosis, Differential; D005973:Glutamine / Q000737:chemistry*; D006801:Humans; D019636:Neurodegenerative Diseases / Q000145:classification / Q000235:genetics / Q000378:metabolism / Q000503:physiopathology; D009474:Neurons / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D019680:Trinucleotide Repeat Expansion
D000577:Amides; D005973:Glutamine