Published in 2014, Protein Deimination in Human Health and Disease was the first book on this novel post-translational modification, in which selected positively-charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl-arginine deiminase (PAD) family of enzymes. This area of research continues to expand rapidly, necessitating the need for this second edition. Chronicling the latest inflammatory, epigenetic, neurodegenerative, and carcinogenic processes, Protein Deimination in Human Health and Disease, Second Edition, updates the latest advances in deimination research, including new information on PAD enzyme structure and activity, and how PAD knock-out animals are being used to study known and newly-discovered links to various human diseases.
The first edition outlined what was known about citrullinated proteins in normal tissues such as skin and hair, as well as in maladies such as rheumatoid arthritis (RA), multiple sclerosis (MS), Alzheimer’s disease (AD), glaucoma, peripheral nerve injury, neonatal hypoxic brain damage, and breast cancer. This second edition addresses numerous additional disorders such as diabetes, asthma, traumatic brain injury, inflammatory bowel disease, lupus, bone disease, heart failure, fronto-temporal dementia, and prostate and colon cancer. It also provides updates on the deimination research covering the three seminal diseases first linked to this process (RA, MS and AD), and details how auto-antibodies against citrullinated proteins contribute to disease. In addition, new hypotheses on the possible pathologic mechanisms of citrullinated myelin basic protein and glial fibrillary acidic protein are also proposed. This second edition also outlines the latest developments in therapeutic strategies, including the use of new PAD antagonists and innovative techniques such as micro-vescicles and stem cells as possible mechanisms to treat these conditions.
Edited by:
Anthony Nicholas,
Sanjoy K. Bhattacharya,
Paul R. Thompson
Imprint: Springer International Publishing AG
Country of Publication: Switzerland
Edition: 2nd ed. 2017
Dimensions:
Height: 235mm,
Width: 155mm,
Weight: 8.454kg
ISBN: 9783319582436
ISBN 10: 3319582437
Pages: 474
Publication Date: 28 September 2017
Audience:
College/higher education
,
Professional and scholarly
,
Further / Higher Education
,
Undergraduate
Format: Hardback
Publisher's Status: Active
Chapter 1: A History of Deimination Research in Japan. The Founding Fathers. Akihito Ishigami, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.- Chapter 2: Aspects of Peptidylarginine Deiminase Regulation That May Predispose to Autoreactivity Against Citrullinated Proteins. Indira Neeli and Marko Radic, University of Tennessee Health Science Center, Memphis, TN, USA.- Chapter 3: Structures and Functions of Peptidylarginine Deiminases. Masaki Unno, Kenji Kizawa, Hidenari Takahara, University of Ibaraki, Ibaraki, Japan.- Chapter 4: The Use PAD Knock-Out Mice in Deimination Research, Chinatsu Mukai, Brooke A. Marks and Scott A. Coonrod, Cornell University, Ithaca, NY, USA.- Chapter 5: PAD Activation in Arthritis. Dres Damgaard and Ger J.M. Pruijn, Radboud University, Nijmegen, The Netherlands and Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark.- Chapter 6: Rheumatoid Arthritis: Transition from Systemic Autoimmunity to Joint Inflammation and Bone Loss. Bence Rethi, Akilan Krishnamurthy and Anca I. Catrina, Karolinska University Hospital and Institute, Stockholm, Sweden.- Chapter 7: Porphyromonas Ginvivalis Peptidyl Arginine Deiminase: A Unique Bacterial PAD with Implications for Periodontal Disease and Rheumatoid Arthritis. Katarzyna Gawron, Anna Montgomery, Katarzyna Łazarz-Bartyzel, Grzegorz Bereta, Maria Chomyszyn-Gajewska, Patrick Venables, Jan Potempa, Jagiellonian University, Kraków, Poland and The Kennedy Institute of Rheumatology, Oxford, UK.- Chapter 8: Citrullination and Neutrophil Extracellular Traps. Nishant Dwivedi, Hui-Hsin Chang and I-Cheng Ho, Harvard Medical School, Boston, MA, USA.- Chapter 9: Citrullination and Autophagy. Guido Valesini, Cristiano Alesandri, Tania Colasanti and Fabrizio Conti, La Sapienza Università di Roma, Rome, Italy.- Chapter 10: Antigen Deimination in Human Type 1 Diabetes and Non-Obese Diabetic Mice. Hai Nguyen and Eddie A. James, Benaroya Research Institute, Seattle, Washington, USA.- Chapter 11: Citrullinated Autoantigen Targets as Risk Markers of Cardiovascular and Pulmonary Disease Phenotypes in Rheumatoid Arthritis. Vinitha Ganesan and Dana P. Ascherman, University of Miami, Miami, FL, USA.- Chapter 12: The Significance of Myofilament Protein Citrullination in Heart Failure. Citrullination in Cardiovascular Diseases, Justyna Fert-Bober, E. Crowgey, J. Sokolove, JT. Giles, J. Bathon and J. E. Van Eyk, Cedars Sinai Medical Center, Los Angeles, CA, Alfred I. duPont Hospital for Children, Wilmington, DE, AbbVie Pharmaceuticals, Redwood City, CA and Columbia University New York, NY, USA.- Chapter 13: Protein Deimination in Protein Misfolding Disorders - Modelled in Human induced Pluripotent Stem Cells (iPSCs). Sigrun Lange, Selina Wray, Mike Devine, Mar Matarin and John Hardy, University of Westminster and University College London School of Pharmacy and Institute of Neurology, London, UK.- Chapter 14: Protein Deimination in Aging and Age-Related Diseases with Ocular Manifestations. Di Ding, Mabel Enriquez-Algeciras, Sanjoy K. Bhattacharya and Vera L Bonilha. Bascom Palmer Eye Institute, University of Miami, Florida and Cole Eye Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.- Chapter 15: Chemical Modification and Mass Spectrometric Approaches for Detection of Brain Protein Deimination. Mabel Enriquez- Algeciras, Di Ding, Dana P. Ascherman and Sanjoy K. Bhattacharya, University of Miami, Miami, FL, USA.- Chapter 16: Citrullination Following Traumatic Brain Injury: A Mechanism for Ongoing Pathology Through Protein Modification. Rachel C. Lazarus John E. Buonora, Alaa Kamnaksh, Michael N. Flora, James G. Freedy, Gay R. Holstein, Giorgio P. Martinelli, David M. Jacobowitz, Denes Agoston and Gregory P Mueller, Uniformed Services University of the Health Sciences, Bethesda, MD, USA.- Chapter 17: Update on Deimination in Alzheimer's Disease. Yoshitaka Kondo, Eun-Kyoung Choi,Yong-Sun Kim and Akihito Ishigami, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan and Hallym University, Gyeonggi-do, Republic of Korea.- Chapter 18: Deimination in Multiple Sclerosis: The Bad, the Good and the Ugly. William R. Meador, John R. Rinker and Anthony P. Nicholas, University of Alabama at Birmingham and The Birmingham VA Medical Center, Birmingham, AL, USA.- Chapter 19: Turning White Matter “Inside‐Out” by Hyper‐Deimination of Myelin Basic Protein (MBP). George Harauz, University of Guelph, Guelph, ON, Canada.- Chapter 20: The Significance of Deiminated GFAP in Neurodegenerative Diseases with Special Emphasis on Alexander’s Disease. Michael Brenner and Anthony P. Nicholas, University of Alabama at Birmingham, Birmingham, AL, USA.- Chapter 21: Treatment of Prostate Cancer Using Deimination Antagonists and Microvescicle Technology. Sigrun Lange, Sharad Kholia, Uchini S Kosgodage and Jameel M. Inal, University College London School of Pharmacy, University of Westminster and London Metropolitan University, London, UK.- Chapter 22: Citrullination in Inflammatory-Driven Carcinogenesis of the Colon. Erin E. Witalison and Lorne J. Hofseth, University of South Carolina, Columbia, SC, USA.- Chapter 23: Development of the Protein Arginine Deiminase (PAD) Inhibitors. Aaron Muth and Paul R. Thompson, UMASS Medical School, Worcester, MA, USA.
Anthony Nicholas, University of Alabama - BirminghamSanjoy Bhattacharya, University of MiamiPaul R. Thompson, University of Massachusetts Medical School
