In vivo expression of peptidylarginine deiminase in Drosophila melanogaster

Autoři: Olena Mahneva aff001;  Monica G. Risley aff001;  Ciny John aff001;  Sarah L. Milton aff001;  Ken Dawson-Scully aff001;  William W. Ja aff003
Působiště autorů: Department of Biological Sciences, Florida Atlantic University, Boca Raton, Florida, United States of America aff001;  International Max Planck Research School (IMPRS) for Brain and Behavior, Boca Raton, Florida, United States of America aff002;  Department of Neuroscience, The Scripps Research Institute, Jupiter, Florida, United States of America aff003;  Center on Aging, The Scripps Research Institute, Jupiter, Florida, United States of America aff004
Vyšlo v časopise: PLoS ONE 15(1)
Kategorie: Research Article


Peptidylarginine deiminase (PAD) modifies peptidylarginine and converts it to peptidylcitrulline in the presence of elevated calcium. Protein modification can lead to severe changes in protein structure and function, and aberrant PAD activity is linked to human pathologies. While PAD homologs have been discovered in vertebrates—as well as in protozoa, fungi, and bacteria—none have been identified in Drosophila melanogaster, a simple and widely used animal model for human diseases. Here, we describe the development of a human PAD overexpression model in Drosophila. We established fly lines harboring human PAD2 or PAD4 transgenes for ectopic expression under control of the GAL4/UAS system. We show that ubiquitous or nervous system expression of PAD2 or PAD4 have minimal impact on fly lifespan, fecundity, and the response to acute heat stress. Although we did not detect citrullinated proteins in fly homogenates, fly-expressed PAD4—but not PAD2—was active in vitro upon Ca2+ supplementation. The transgenic fly lines may be valuable in future efforts to develop animal models of PAD-related disorders and for investigating the biochemistry and regulation of PAD function.

Klíčová slova:

Biological locomotion – Drosophila melanogaster – Fecundity – Heat treatment – Hyperthermia – Protein extraction – Thermal stresses – Citrullination


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