Protein Deimination In Human Health And Disease Pdf

protein deimination in human health and disease pdf

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It seems that you're in Germany. We have a dedicated site for Germany. Deimination is a relatively new post-translational modification of proteins, whose recognition is ever-increasing.

Protein Deimination in Human Health and Disease

Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline. Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code. Instead, it is the result of a post-translational modification. Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family.

Arginine is positively charged at a neutral pH, whereas citrulline has no net charge. This increases the hydrophobicity of the protein, which can lead to changes in protein folding , affecting the structure and function.

The immune system can attack citrullinated proteins, leading to autoimmune diseases such as rheumatoid arthritis RA and multiple sclerosis MS. Fibrin and fibrinogen may be favored sites for arginine deimination within rheumatoid joints.

Citrullinated vimentin may be an autoantigen in RA and other autoimmune diseases, and is used to study RA. Moreover, antibodies against mutated citrullinated vimentin MCV may be useful for monitoring effects of RA therapy. In the reaction from arginine to citrulline, one of the terminal nitrogen atoms of the arginine side chain is replaced by an oxygen.

Thus, arginine's positive charge at physiological pH is removed, altering the protein's tertiary structure. The reaction uses one water molecule and yields ammonia as a side-product:.

PADs are found in chordates but not in lower animals. PAD1 expression has been detected in epidermis and the uterus, and it acts in citrullination of keratin and filaggrin , key components of keratinocytes.

PAD2 is expressed at a high level in the central nervous system CNS , including the eye and brain, as well as skeletal muscle and the spleen. One of PAD2's target substrates is myelin basic protein. In the normal retina , deimination is found in nearly all the retinal layers, including the photoreceptors.

Deimination has been also reported in neuronal cells, such as astrocytes , microglia and oligodendrocytes , Schwann cells and neurons. In adults, MBP deimination is found in demyelination diseases such as multiple sclerosis. MBP may affect different cell types in each case. PAD3 expression has been linked to sheep wool modification.

Citrullination of trichohyalin allows it to bind and cross-link keratin filaments, directing growth of the wool fiber. PAD4 regulates gene expression through histone modifications.

DNA is wrapped around histones, and the histone proteins can control DNA expression when chemical groups are added and removed. This process is known as post-translational processing or post-translational modification, because it takes place on the protein after the DNA is translated.

The role of post-translational processing in gene regulation is the subject of the growing field of study, epigenetics. One modification mechanism is methylation. A methyl group CH 3 binds to an arginine on the histone protein, altering DNA binding to the histone and allowing transcription to take place. When PAD converts arginine to citrulline on a histone, it blocks further methylation of the histone, inhibiting transcription.

The presence of anti-citrullinated protein antibody is a standard test for rheumatoid arthritis, and it is associated with more severe disease.

Citrullinated proteins are also found in the cellular debris accompanying the destruction of cells in alzheimer disease , and after smoking cigarettes. So citrullination seems to be part of the mechanism that stimulates the immune system in autoimmune disease.

However, citrullinated proteins can also be found in healthy colon mucosa. The first comprehensive textbook on deimination was published in Citrullinated peptides and proteins can be detected using antibodies targeting the citrullinated residues, or detected using mass spectrometry -based proteomics technologies.

Furthermore, the mass shift is identical to the mass shift caused by deamidation of the amino acid asparagine or glutamine side chain, which are common modifications. Citrulline residues can be chemically modified with butanedione or biotinylation prior to analysis, leading to a different mass shift, and this strategy has successfully been used to facilitates identification by mass spectrometry.

Another approach is to utilize the neutral loss of isocyanic acid HNCO from citrulline residues when submitted to low energy collision induced dissociation fragmentation in mass spectrometers.

Finally, the loss of positive charge at physiological pH caused by citrullination can be utilized. Prior to bottom-up proteomics analysis, proteins are enzymatically cleaved into peptides. Commonly the protease trypsin is used, which cleaves after the positively charged arginine and lysine residues. However, trypsin is unable to cleave after a citrulline residue which is neutral. A missed cleavage after a citrulline residue together with the correct mass shift can be used as a specific and sensitive marker for citrullination, and the strategy is compatible with standard bottom-up proteomics workflows.

From Wikipedia, the free encyclopedia. Biological process. Clinical Chemistry. August The Journal of Rheumatology. Archived from the original on Retrieved Zendman; Walther J.

Pruijn November Nucleic Acids Research. Neurochemical Research. Science Translational Medicine. Autoimmunity Reviews. Journal of Proteome Research. Protein Deimination in Human Health and Disease. New York: Springer. Rapid Communications in Mass Spectrometry. Analytical and Bioanalytical Chemistry. Journal of the American Society for Mass Spectrometry. Protein primary structure and posttranslational modifications.

Palmitoylation Prenylation. Succinimide formation ADP-ribosylation. Deamidation Glycosylation. Citrullination Methylation ADP-ribosylation. Diphthamide formation Adenylylation. Disulfide bond ADP-ribosylation. Sulfilimine bond. Lysine tyrosylquinone LTQ formation. Tryptophan tryptophylquinone TTQ formation. Categories : Post-translational modification Protein structure.

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Serine — Tyrosine — Glycine p-Hydroxybenzylidene-imidazolinone formation. Allysine — Allysine — Allysine — Lysine Desmosine.

An Overview of the Intrinsic Role of Citrullination in Autoimmune Disorders

Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline. Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code. Instead, it is the result of a post-translational modification. Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family. Arginine is positively charged at a neutral pH, whereas citrulline has no net charge. This increases the hydrophobicity of the protein, which can lead to changes in protein folding , affecting the structure and function.

Aljaddawi, Sana G. Alattas, Elrashdy M. Box , Jeddah , Saudi Arabia. A protein undergoes many types of posttranslation modification. Citrullination is one of these modifications, where an arginine amino acid is converted to a citrulline amino acid.


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 .


An Overview of the Intrinsic Role of Citrullination in Autoimmune Disorders

It seems that you're in Germany. We have a dedicated site for Germany. Published in , 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.

Deimination is a relatively new post-translational modification of proteins, whose recognition is ever-increasing. First linked to the pathology of rheumatoid arthritis RA , deimination is a process by which selected positively charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl arginine deiminase PAD family of enzymes. Although the medical literature is rich with articles about the possible significance of deiminated proteins in RA, Protein Deimination in Human Health and Disease is the first publication to compile this knowledge and the growing amount of new information now known about the presence of deiminated proteins in the eye, skin, hair, gums, lung and nervous system, as well. As a result, this process has now been linked to numerous additional conditions besides RA, including cancer, glaucoma, Alzheimer's disease, Parkinson's disease, multiple sclerosis, spinal cord and peripheral nerve injury, Creutzfeldt-Jakob disease, among many others. Chronicling the earliest studies of deimination up to the present, this volume distills what is currently known about citrullination of proteins in the human body and is the first book of its kind on the topic.

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Protein Deimination in Human Health and Disease - Ebook

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