Importance of Citrullination on Hair Protein Molecular Assembly During Trichocytic Differentiation View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2014

AUTHORS

Kenji Kizawa , Masaki Unno , Claus W. Heizmann , Hidenari Takahara

ABSTRACT

In mammalian hair follicles, Ca2+-dependent peptidylarginine deiminases catalyze the conversion of arginines into citrullines in S100A3, a cysteine-rich member of the S100 protein family, and trichohyalin, a member of the S100 fused-type protein family. These irreversible posttranslational modifications were first described in the inner root sheath and medulla, and later, in hair cuticles. In the inner root sheath and medullary cells, arginine residues in the repetitive peptide domains of trichohyalin are converted to peptidylcitrullines. Consequently, the α-helix rich structures are unfolded due to decreased intramolecular ionic interaction. Citrullinated trichohyalin, which is susceptible to further introduction of isopeptide bonds, is cross-linked to keratin intermediate filaments, the cornified envelope, or to itself in the inner root sheath. Interconnected trichohyalin is predominantly deposited in amorphous vacuoles of the mature medulla. In cuticular cells, hair-dominant-type peptidylarginine deiminase specifically converts a symmetric pair of Arg51 on the S100A3 dimer to a citrulline pair. The citrullinated S100A3 dimer assembles as a homotetramer in the presence of Ca2+ and Zn2+. This trichocytic pathway is likely to be associated with homeostatic Ca2+ and Zn2+ regulation during hair cuticular maturation. This chapter summarizes previous reports of pioneering research updated with our current view of protein deimination in the hair follicle. More... »

PAGES

129-148

References to SciGraph publications

Book

TITLE

Protein Deimination in Human Health and Disease

ISBN

978-1-4614-8316-8
978-1-4614-8317-5

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4614-8317-5_8

DOI

http://dx.doi.org/10.1007/978-1-4614-8317-5_8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048426358


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