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Update on Deimination in Alzheimer’s Disease

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Protein Deimination in Human Health and Disease

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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 the positive charges of native protein molecules, inevitably causing significant alterations in their structure and functions. Protein citrullination is important for the formation of the cornified layer of the skin that covers the human body. Despite this beneficial function, protein citrullination can also be detrimental as its accumulation in the brain is a possible cause of Alzheimer’s disease (AD). In this chapter, we introduce PADs and their protein citrullination function now considered critical for advancing research on aging and neurodegenerative disorders, especially AD.

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Abbreviations

AD:

Alzheimer’s disease

Anti-CCP:

Anti-cyclic citrullinated peptide

Anti-MVC:

Anti-mutated citrullinated vimentin

BAEE:

Benzoyl-l-arginine ethyl ester

Bz-l-Arg:

Benzoyl-l-arginine

Calbindin:

Calbindin-D-28K

cAMP:

Cyclic adenosine monophosphate

Cit-GFAP:

Citrullinated glial fibrillary acidic protein

Cit-hGFAP:

Citrullinated human glial fibrillary acidic protein

Cit-rhGFAP:

Citrullinated recombinant human glial fibrillary acidic protein

CNS:

Central nervous system

dbcAMP:

Dibutyryl cyclic adenosine monophosphate

GAPDH:

Glyceraldehyde-3-phosphate dehydrogenase

GFAP:

Glial fibrillary acidic protein

MALDI-TOF:

Matrix-associated laser desorption ionization-time of flight

MAP 2:

Microtubule-associated protein 2

MBP:

Myelin basic protein

Nef3:

Neurofilament 3

NFT:

Neurofibrillary tangles

PAD:

Peptidylarginine deiminase

PKA:

Protein kinase A

qPCR:

Quantitative real-time polymerase chain reaction

RA:

Rheumatoid arthritis

rhGFAP:

Recombinant human glial fibrillary acidic protein

rhPAD:

Recombinant human peptidylarginine deiminase

RT-PCR:

Reverse transcription polymerase chain reaction

SP:

Senile plaque

β2-MG:

β2-microglobulin

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Authors and Affiliations

  1. Molecular Regulation of Aging, Tokyo Metropolitan Institute of Gerontology (TMIG), Tokyo, Japan

    Yoshitaka Kondo & Akihito Ishigami

  2. Department of Biomedical Gerontology, Graduate School of Hallym University, Anyang, Republic of Korea

    Eun-Kyoung Choi & Yong-Sun Kim

Authors
  1. Yoshitaka Kondo
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  2. Eun-Kyoung Choi
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  3. Yong-Sun Kim
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  4. Akihito Ishigami
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Correspondence to Yoshitaka Kondo .

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Editors and Affiliations

  1. Department of Neurology, University of Alabama at Birmingham and The Birmingham Veterans Administration Medical Center, Birmingham, Alabama, USA

    Anthony P. Nicholas

  2. Bascom Palmer Eye Institute, University of Miami, Miami, Florida, USA

    Sanjoy K. Bhattacharya

  3. Department of Biochemistry and Molecular Pharmacology, UMASS Medical School, Worcester, Massachusetts, USA

    Paul R. Thompson

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Kondo, Y., Choi, EK., Kim, YS., Ishigami, A. (2017). Update on Deimination in Alzheimer’s Disease. In: Nicholas, A., Bhattacharya, S., Thompson, P. (eds) Protein Deimination in Human Health and Disease. Springer, Cham. https://doi.org/10.1007/978-3-319-58244-3_17

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