Abstract
Peptidylarginine deiminases (PADs) are a group of posttranslational modification enzymes that citrullinate (deiminate) protein arginine residues in a calcium ion-dependent manner. Enzymatic citrullination abolishes positive charges of native protein molecules, inevitably causing significant alterations in their structure and functions. Deiminated protein provides the important physiological advantage of forming a cornified layer of skin that covers the human body (see Chap. 7 for more details). Despite this beneficial function, deimination also has a negative side, because the accumulation of these proteins in the brain is a possible cause of Alzheimer’s disease (AD). In this chapter, we introduce PADs and their protein citrullination function, which is now considered critical for advancing research on aging and neurodegenerative disorders, especially AD.
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Abbreviations
- anti-CCP:
-
Anti-cyclic citrullinated peptide
- anti-MVC:
-
Anti-mutated citrullinated vimentin,
- AD:
-
Alzheimer’s disease
- BAEE:
-
Benzoyl-l-arginine ethyl ester
- Bz-l-Arg:
-
Benzoyl-l-arginine
- Calbindin:
-
Calbindin-D-28K
- CNS:
-
Central nervous system
- DAB:
-
3,3′-Diaminobenzidine
- GAPDH:
-
Glyceraldehyde-3-phosphate dehydrogenase
- GFAP:
-
Glial fibrillary acidic protein
- NFT:
-
Neurofibrillary tangles
- MAP2:
-
Microtubule-associated protein 2
- MBP:
-
Myelin basic protein
- Nef3:
-
Neurofilament 3
- PAD:
-
Peptidylarginine deiminase
- RA:
-
Rheumatoid arthritis
- RT-PCR:
-
Reverse transcriptase-polymerase chain reaction
- SP:
-
Senile plaque
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The excellent editorial assistance of Ms. P. Minick is gratefully acknowledged.
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Ishigami, A., Choi, EK., Kim, YS., Maruyama, N. (2014). Deimination in Alzheimer’s Disease. In: Nicholas, A., Bhattacharya, S. (eds) Protein Deimination in Human Health and Disease. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-8317-5_13
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