5 results match your criteria: "University of Ibaraki[Affiliation]"
Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases.
Int J Mol Sci
January 2020
UDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Paul Sabatier, Université de Toulouse Midi-Pyrénées, U1056, Toulouse 31059, France.
Deimination, also known as citrullination, corresponds to the conversion of the amino acid arginine, within a peptide sequence, into the non-standard amino acid citrulline. This post-translational modification is catalyzed by a family of calcium-dependent enzymes called peptidylarginine deiminases (PADs). Deimination is implicated in a growing number of physiological processes (innate and adaptive immunity, gene regulation, embryonic development, etc.
View Article and Find Full Text PDFPeptidylarginine Deiminase Inhibitor Cl-Amidine Attenuates Cornification and Interferes with the Regulation of Autophagy in Reconstructed Human Epidermis.
J Invest Dermatol
September 2019
Unité Différenciation Epithéliale et Autoimmunité Rhumatoïde, Institut National de la Santé Et de la Recherche Médicale, Université de Toulouse Midi-Pyrénées, Toulouse, France. Electronic address:
Deimination, a post-translational modification catalyzed by a family of enzymes called peptidylarginine deiminases (PADs), is the conversion of arginine into citrulline residues in a protein. Deimination has been associated with numerous physiological and pathological processes. Our aim was to study its implication in the homeostasis of human epidermis, where three PADs are expressed, namely PAD1, 2, and 3.
View Article and Find Full Text PDFLowering relative humidity level increases epidermal protein deimination and drives human filaggrin breakdown.
J Dermatol Sci
May 2017
UDEAR, Institut National de la Santé Et de la Recherche Médicale, Université de Toulouse Midi-Pyrénées, Centre National de la Recherche Scientifique, Toulouse, France. Electronic address:
Background: Deimination (also known as citrullination), the conversion of arginine in a protein to citrulline, is catalyzed by a family of enzymes called peptidylarginine deiminases (PADs). Three PADs are expressed in the epidermis, one of their targets being filaggrin. Filaggrin plays a central role in atopic dermatitis and is a key protein for the epidermal barrier.
View Article and Find Full Text PDFDeimination of Human Hornerin Enhances its Processing by Calpain-1 and its Cross-Linking by Transglutaminases.
J Invest Dermatol
February 2017
Unité Différenciation Epithéliale et Autoimmunité Rhumatoïde, Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse Midi-Pyrénées, Université Toulouse III, Toulouse, France. Electronic address:
Article Synopsis
- HRNR shares structural and functional similarities with filaggrin, playing a vital role in the epidermal barrier and processed similarly in keratinocytes.
- HRNR undergoes deimination and proteolytic cleavage by calpain-1, with deiminated HRNR showing increased interaction with transglutaminases.
- This research reveals new insights into the metabolism of HRNR, highlighting the significance of deimination in the cornification process.
Antibacterial diterpenes and their fatty acid conjugates from rice leaves.
Phytochemistry
May 2004
School of Agriculture, University of Ibaraki, Ami, Ibaraki 300-0393, Japan.
Article Synopsis
- Six compounds related to oryzalide were isolated from the extract of a rice plant known for its resistance to bacterial leaf blight, specifically using the "Norin-27" cultivar.
- Their structures were identified as kaurane analogues, which include both standard forms and those attached to fatty acids.
- The compounds include various forms of ent-15,16-epoxy-kauran derivatives, highlighting the diversity in structure, such as enol forms and different fatty acid attachments.