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Structures and Functions of Peptidylarginine Deiminases

2017
Molecular structures of peptidylarginine deiminase (PAD) isozymes are strongly associated with their functions. This chapter summarizes the X-ray structures of PAD1, PAD2, and PAD4 as well as that of the PAD from the periodontal pathogen Porphyromonas gingivalis.
Masaki Unno   +2 more
openaire   +1 more source

Peptidylarginine deiminase in rat and mouse hemopoietic cells

Experientia, 1990
Peptidylarginine (protein-L-arginine) deiminase activities have been demonstrated in extracts of rat and mouse peritoneal macrophages, bone marrow cells, splenic adherent cells, neutrophils, and mouse monocyte/macrophage cell lines. The enzyme in these cells is indistinguishable from the skeletal muscle enzyme with respect to immunochemical properties.
S, Nagata, T, Senshu
openaire   +2 more sources

Immunohistochemical Demonstration of Peptidylarginine Deiminase in Human Sweat Glands

The American Journal of Dermatopathology, 1990
Human skin is known to contain protein-bound citrulline. This is the product of enzymatic deimination of arginine residues catalyzed by peptidylarginine deiminase. We probed frozen sections of human skin with a rabbit antiserum raised to rat skeletal muscle peptidylarginine deiminase using the avidin-biotin-peroxidase complex technique.
Y, Urano   +8 more
openaire   +2 more sources

Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils

Journal of Leukocyte Biology, 2001
AbstractPeptidylarginine deiminase, registered as PAD V in the DDBJ/GenBank/EMBL data banks, is expressed in HL-60 cells differentiated into granulocytes or monocytes. We analyzed PAD activities in density-fractionated human peripheral blood cell fractions. PAD activity with similar substrate specificity to that of PAD V was found in the eosinophil and
H, Asaga   +4 more
openaire   +2 more sources

Increased peptidylarginine deiminase type II in hypoxic astrocytes

Biochemical and Biophysical Research Communications, 2004
Peptidylarginine deiminase type II (PAD 2) is the primary enzyme responsible for conversion of protein bound arginine to citrulline in the central nervous system. Evidence suggests that glial fibrillary acidic protein (GFAP), the main intermediate filament in astrocytes, is deiminated, but not much is known regarding factors that control this enzymatic
Thiagarajan, Sambandam   +6 more
openaire   +2 more sources

Transcriptional regulation of peptidylarginine deiminase expression in human keratinocytes

Journal of Dermatological Science, 2009
Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzyme catalyzes the conversion of arginine residues to citrulline residues in the presence of calcium ion, which is an elaborate post-translational modification on the target protein. Recently, five isoforms have been identified in mammals.
Shibo, Ying   +9 more
openaire   +2 more sources

The enzymology of human peptidylarginine deiminase 4

2005
The human peptidylarginine deiminase 4 gene and several mutations were recently linked to rheumatoid arthritis susceptibility. Though it is known that these mutations can result in a longer lived mRNA, nothing was known as to whether these mutations, 3 of which result in codon changes, affected the enzyme activity of peptidylarginine deiminase 4 (PAD4).
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INHIBITORS OF PEPTIDYLARGININE DEIMINASES

2022
BYUN DANIEL H   +15 more
openaire   +5 more sources

Peptidylarginine Deiminase Enzymes

2014
Sunish Mohanan, Scott Coonrod
openaire   +1 more source

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