The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
PAD4 mediated histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular trap-like structures
Open accessAbstract
NETosis, the process wherein neutrophils release highly decondensed chromatin called neutrophil extracellular traps (NETs), has gained much attention as an alternative means of killing bacteria. In vivo, NETs are induced by bacteria and pro-inflammatory cytokines. We have reported that peptidylarginine deiminase 4 (PAD4), an enzyme that converts Arg or monomethyl-Arg to citrulline in histones, is essential for NET formation. The areas of extensive chromatin decondensation along the NETs were rich in histone citrullination. Here, upon investigating the effect of global citrullination in cultured cells, we discovered that PAD4 overexpression in osteosarcoma U2OS cells induces extensive chromatin decondensation independent of apoptosis. The highly decondensed chromatin is released to the extracellular space and stained strongly by a histone citrulline-specific antibody. The structure of the decondensed chromatin is reminiscent of NETs but is unique in that it occurs without stimulation of cells with pro-inflammatory cytokines and bacteria. Furthermore, histone citrullination during chromatin decondensation can dissociate heterochromatin protein 1 beta (HP1β) thereby offering a new molecular mechanism for understanding how citrullination regulates chromatin function. Taken together, our study suggests that PAD4 mediated citrullination induces chromatin decondensation, implicating its essential role in NET formation under physiological conditions in neutrophils.
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1 retracted
Marcos, V., Zhou, Z., Yildirim, A. Ö., Bohla, A., Hector, A., Vitkov, L., Wiedenbauer, E.-M., Krautgartner, W. D., Stoiber, W., Belohradsky, B. H., et al. (2010) · Nature Medicine · doi:10.1038/nm.2209 · Cited by 212
RetractedChromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · cited 2×
“Acetylation, methylation and phosphorylation of histone proteins regulate chromatin functions, such as transcription as well as chromatin condensation and decondensation (Shilatifard, 2006; Kouzarides, 2007; Li et al., 2007).”
InfluentialNeutrophil Extracellular Traps Kill Bacteria
Brinkmann, V., Reichard, U., Goosmann, C., Fauler, B., Uhlemann, Y., Weiss, D. S., Weinrauch, Y., & Zychlinsky, A. (2004) · Science · doi:10.1126/science.1092385 · Cited by 10,268
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,533
Novel cell death program leads to neutrophil extracellular traps
Fuchs, T. A., Abed, U., Goosmann, C., Hurwitz, R., Schulze, I., Wahn, V., Weinrauch, Y., Brinkmann, V., & Zychlinsky, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606027 · Cited by 3,197
Neutrophils and immunity: challenges and opportunities
Nathan, C. (2006) · Nature reviews. Immunology · doi:10.1038/nri1785 · Cited by 2,971
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Self-citationPAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps
Li, P., Li, M., Lindberg, M. R., Kennett, M. J., Xiong, N., & Wang, Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100239 · Cited by 1,495
Self-citationThe structure of DNA in the nucleosome core
Richmond, T. J., & Davey, C. A. (2003) · Nature · doi:10.1038/nature01595 · Cited by 1,286
Suzuki, A., Yamada, R., Chang, X., Tokuhiro, S., Sawada, T., Suzuki, M., Nagasaki, M., Nakayama-Hamada, M., Kawaida, R., Ono, M., et al. (2003) · Nature Genetics · doi:10.1038/ng1206 · Cited by 1,168
Cited by
Neutrophil extracellular traps in immunity and disease
Papayannopoulos, V. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.105 · Cited by 3,397
Severe COVID-19 Is Marked by a Dysregulated Myeloid Cell Compartment
Schulte-Schrepping, J., Reusch, N., Paclik, D., Baßler, K., Schlickeiser, S., Zhang, B., Krämer, B., Krammer, T., Brumhard, S., Bonaguro, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.001 · Cited by 1,461
Diabetes primes neutrophils to undergo NETosis, which impairs wound healing
Wong, S. L., Demers, M., Martinod, K., Gallant, M., Wang, Y., Goldfine, A. B., Kahn, C. R., & Wagner, D. D. (2015) · Nature Medicine · doi:10.1038/nm.3887 · Cited by 1,264
Self-citationTohme, S., Yazdani, H. O., Al-Khafaji, A. B., Chidi, A. P., Loughran, P., Mowen, K., Wang, Y., Simmons, R. L., Huang, H., & Tsung, A. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-1591 · Cited by 694
Self-citationMartinod, K., Demers, M., Fuchs, T. A., Wong, S. L., Brill, A., Gallant, M., Hu, J., Wang, Y., & Wagner, D. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301059110 · Cited by 532
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Metadata
- Authors
- Leshner, M., Wang, S., Lewis, C., Zheng, H., Chen, X. A., Santy, L., & Wang, Y.
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2012
- Volume
- 3
- Pages
- 307-307
- ISSN
- 1664-3224 (ISSN-L)
- OpenAlex
- W2102221395
- Cited by
- 485
- References
- 32
- FWCI
- 7.15
- Type
- journal article
- Language
- en
- Open access
- gold
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- CoChat. (2026). Citation check: PAD4 mediated histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular trap-like structures. https://app.cochat.ai/papers/10.3389/fimmu.2012.00307
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- Leshner, M., Wang, S., Lewis, C., Zheng, H., Chen, X. A., Santy, L., & Wang, Y. (2012). PAD4 mediated histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular trap-like structures. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2012.00307
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