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Kinase Pathways in Chemoattractant-Induced Degranulation of Neutrophils: The Role of p38 Mitogen-Activated Protein Kinase Activated by Src Family Kinases
Open accessAbstract
The aim of the present study was to investigate the role of tyrosine phosphorylation pathways in fMLP-induced exocytosis of the different secretory compartments (primary and secondary granules, as well as secretory vesicles) of neutrophils. Genistein, a broad specificity tyrosine kinase inhibitor, blocked the exocytosis of primary and secondary granules, but had only a marginal effect on the release of secretory vesicles. Genistein also inhibited the phosphorylation of extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein kinases (MAPK), raising the possibility that inhibition of ERK and/or p38 MAPK might be responsible for the effect of the drug on the degranulation response. Indeed, SB203580, an inhibitor of p38 MAPK, decreased the release of primary and secondary granules, but not that of secretory vesicles. However, blocking the ERK pathway with PD98059 had no effect on any of the exocytic responses tested. PP1, an inhibitor of Src family kinases, also attenuated the release of primary and secondary granules, and neutrophils from mice deficient in the Src family kinases Hck, Fgr, and Lyn were also defective in secondary granule release. Furthermore, activation of p38 MAPK was blocked by both PP1 and the hck−/−fgr−/−lyn−/− mutation. Taken together, our data indicate that fMLP-induced degranulation of primary and secondary granules of neutrophils is mediated by p38 MAPK activated via Src family tyrosine kinases. Although piceatannol, a reportedly selective inhibitor of Syk, also prevented degranulation and activation of p38 MAPK, no fMLP-induced phosphorylation of Syk could be observed, raising doubts about the specificity of the inhibitor.
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Cited by
Neutrophil cell surface receptors and their intracellular signal transduction pathways
Futosi, K., Fodor, S., & Mócsai, A. (2013) · International Immunopharmacology · doi:10.1016/j.intimp.2013.06.034 · Cited by 642
Neutrophil chemoattractant receptors in health and disease: Double-edged swords
Metzemaekers, M., Gouwy, M., & Proost, P. (2020) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-0412-0 · Cited by 570
Mechanisms of Degranulation in Neutrophils
Lacy, P. (2006) · Allergy, Asthma & Clinical Immunology · doi:10.1186/1710-1492-2-3-98 · Cited by 473
Syk is required for integrin signaling in neutrophils
Mócsai, A., Zhou, M., Meng, F., Tybulewicz, V. L., & Lowell, C. A. (2002) · Immunity · doi:10.1016/s1074-7613(02)00303-5 · Cited by 421
Self-citationFachini-Queiroz, F. C., Kummer, R., Estevão-Silva, C. F., Carvalho, M. D. D. B., Cunha, J. M., Grespan, R., Bersani-Amado, C. A., & Cuman, R. K. N. (2012) · Evidence-Based Complementary and Alternative Medicine · doi:10.1155/2012/657026 · Cited by 304
Metadata
- Authors
- Mócsai, A., Jakus, Z., Vántus, T., Berton, G., Lowell, C. A., & Ligeti, E.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2000-04
- Volume
- 164
- Issue
- 8
- Pages
- 4321-4331
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2096204372
- Cited by
- 287
- References
- 66
- FWCI
- 6.19
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Kinase Pathways in Chemoattractant-Induced Degranulation of Neutrophils: The Role of p38 Mitogen-Activated Protein Kinase Activated by Src Family Kinases. https://app.cochat.ai/papers/10.4049/jimmunol.164.8.4321
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- Mócsai, A., Jakus, Z., Vántus, T., Berton, G., Lowell, C. A., & Ligeti, E. (2000). Kinase Pathways in Chemoattractant-Induced Degranulation of Neutrophils: The Role of p38 Mitogen-Activated Protein Kinase Activated by Src Family Kinases. The Journal of Immunology. https://doi.org/10.4049/jimmunol.164.8.4321
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