Cited by 132

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Rac2 is critical for neutrophil primary granule exocytosis

Abdel-Latif, Dalia, Steward, Melissa, Macdonald, Dawn L., Francis, Gordon A., Dinauer, Mary C., Lacy, Paige·2004·Blood

Abstract

Neutrophil degranulation is important in many inflammatory disorders, although the intracellular mechanisms underlying this process remain poorly understood. The Rho GTPase, Rac2, has been implicated in control of degranulation in earlier studies. We hypothesized that Rac2 selectively regulates neutrophil primary granule release. Using bone marrow and peritoneal exudate neutrophils from rac2-/- mice in comparison with similar cells from wild-type C57Bl/6 mice, we found that primary granule myeloperoxidase and elastase release was absent in Rac2-/- neutrophils in response to chemoattractant stimulation, cytochalasin B/f-Met-Leu-Phe (CB/fMLP), and CB/leukotriene B4. Rac2-/- neutrophils also failed to exhibit mobilization of the primary granule marker CD63+ during CB/fMLP stimulation as determined by confocal microscopy. Priming of Rac2-/- neutrophils with tumor necrosis factor (TNF) or by peritoneal elicitation did not rescue the defect in primary granule release. However, phosphorylation of p38 mitogen-activated protein (MAP) kinase in Rac2-/- neutrophils was evident in response to CB/fMLP and/or TNF. Primary granule density and morphology were normal in Rac2-/- neutrophils. Secondary specific and tertiary granule release, measured by lactoferrin immunoassay and zymography, was normal in response to CB/fMLP and adhesion to fibronectin. These findings suggest an obligatory role for Rac2 in regulation of primary granule release by neutrophils.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1182/blood-2003-07-2624

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 43

  1. Borregaard N, Cowland JB. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood. 1997;89: 3503-3521. · DOI
  2. Barrowman MM, Cockcroft S, Gomperts BD. Two roles for guanine nucleotides in the stimulus-secretion sequence of neutrophils. Nature. 1986;319: 504-507. · DOI
  3. Nüsse O, Lindau M. The dynamics of exocytosis in human neutrophils. J Cell Biol.1988;107: 2117-2123. · DOI
  4. Brown AM, O'Sullivan AJ, Gomperts BD. Induction of exocytosis from permeabilized mast cells by the guanosine triphosphatases Rac and Cdc42. Mol Biol Cell. 1998;9: 1053-1063. · DOI
  5. Ridley AJ. Rho family proteins: coordinating cell responses. Trends Cell Biol.2001;11: 471-477. · DOI
  6. Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature. 2002;420: 629-635. · DOI · Paper page
  7. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R. rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem.1989;264: 16378-16382. · DOI · Paper page
  8. Heyworth PG, Bohl BP, Bokoch GM, Curnutte JT. Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox: evidence for its interaction with flavocytochrome b558. J Biol Chem.1994;269: 30749-30752. · DOI
  9. Li S, Yamauchi A, Marchal CC, Molitoris JK, Quilliam LA, Dinauer MC. Chemoattractant-stimulated Rac activation in wild-type and Rac2-deficient murine neutrophils: preferential activation of Rac2 and Rac2 gene dosage effect on neutrophil functions. J Immunol.2002;169: 5043-5051. · DOI · Paper page
  10. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2. Science. 1991;254: 1512-1515. · DOI · Paper page
  11. DeLeo FR, Quinn MT. Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins. J Leukoc Biol.1996;60: 677-691. · DOI
  12. Knaus UG, Morris S, Dong HJ, Chernoff J, Bokoch GM. Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors. Science. 1995;269: 221-223. · DOI
  13. Minden A, Lin A, Claret FX, Abo A, Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 1995;81: 1147-1157. · DOI
  14. Mocsai A, Jakus Z, Vantus T, Berton G, Lowell CA, Ligeti E. Kinase pathways in chemoattractant-induced degranulation of neutrophils: the role of p38 mitogen-activated protein kinase activated by Src family kinases. J Immunol.2000;164: 4321-4331. · DOI
  15. Guillemot JC, Montcourrier P, Vivier E, Davoust J, Chavrier P. Selective control of membrane ruffling and actin plaque assembly by the Rho GTPases Rac1 and CDC42 in FcϵRI-activated rat basophilic leukemia (RBL-2H3) cells. J Cell Sci.1997;110: 2215-2225. · DOI
  16. Hong-Geller E, Cerione RA. Cdc42 and Rac stimulate exocytosis of secretory granules by activating the IP3/calcium pathway in RBL-2H3 cells. J Cell Biol.2000;148: 481-494. · DOI
  17. Prepens U, Just I, Eichel-Streiber C, Aktories K. Inhibition of FcϵRI-mediated activation of rat basophilic leukemia cells by Clostridium difficile toxin B (monoglucosyltransferase). J Biol Chem.1996;271: 7324-7329. · DOI
  18. Djouder N, Schmidt G, Frings M, Cavalie A, Thelen M, Aktories K. Rac and phosphatidylinositol 3-kinase regulate the protein kinase B in FcϵRI signaling in RBL 2H3 mast cells. J Immunol.2001;166: 1627-1634. · DOI
  19. Roberts AW, Kim C, Zhen L, et al. Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense. Immunity. 1999;10: 183-196. · DOI · Paper page
  20. Kim C, Dinauer MC. Rac2 is an essential regulator of neutrophil nicotinamide adenine dinucleotide phosphate oxidase activation in response to specific signaling pathways. J Immunol.2001;166: 1223-1232. · DOI · Paper page
  21. Ambruso DR, Knall C, Abell AN, et al. Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc Natl Acad Sci U S A. 2000;97: 4654-4659. · DOI · Paper page
  22. Williams DA, Tao W, Yang F, et al. Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency. Blood. 2000;96: 1646-1654.
  23. Lowell CA, Fumagalli L, Berton G. Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J Cell Biol.1996;133: 895-910. · DOI
  24. Voncken JW, van Schaick H, Kaartinen V, et al. Increased neutrophil respiratory burst in bcr-null mutants. Cell. 1995;80: 719-728. · DOI
  25. Gu Y, Jia B, Yang FC, et al. Biochemical and biological characterization of a human Rac2 GTPase mutant associated with phagocytic immunodeficiency. J Biol Chem.2001;276: 15929-15938. · DOI · Paper page
  26. Lacy P, Mahmudi-Azer S, Bablitz B, et al. Rapid mobilization of intracellularly stored RANTES in response to interferon-γ in human eosinophils. Blood. 1999;94: 23-32. · DOI
  27. Mocsai A, Ligeti E, Lowell CA, Berton G. Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck. J Immunol.1999;162: 1120-1126. · DOI
  28. Kleiner DE, Stetler-Stevenson WG. Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem.1994;218: 325-329. · DOI
  29. Lacy P, Latif DA, Steward M, Musat-Marcu S, Man SF, Moqbel R. Divergence of mechanisms regulating respiratory burst in blood and sputum eosinophils and neutrophils from atopic subjects. J Immunol.2003;170: 2670-2679. · DOI
  30. McLaren DJ, Mackenzie CD, Ramalho-Pinto FJ. Ultrastructural observations on the in vitro interaction between rat eosinophils and some parasitic helminths (Schistosoma mansoni, Trichinella spiralis and Nippostrongylus brasiliensis). Clin Exp Immunol.1977;30: 105-118.
  31. Bentwood BJ, Henson PM. The sequential release of granule constituents from human neutrophils. J Immunol.1980;124: 855-862. · DOI
  32. Clark RA, Borregaard N. Neutrophils autoinactivate secretory products by myeloperoxidase-catalyzed oxidation. Blood. 1985;65: 375-381. · DOI
  33. Wojtecka-Lukasik E, Maslinski S. Fibronectin and fibrinogen degradation products stimulate PMN-leukocyte and mast cell degranulation. J Physiol Pharmacol.1992;43: 173-181.
  34. Ligeti E, Mocsai A. Exocytosis of neutrophil granulocytes. Biochem Pharmacol.1999;57: 1209-1214. · DOI
  35. Sengelov H, Kjeldsen L, Borregaard N. Control of exocytosis in early neutrophil activation. J Immunol.1993;150: 1535-1543. · DOI
  36. Zu YL, Qi J, Gilchrist A, et al. p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or FMLP stimulation. J Immunol.1998;160: 1982-1989. · DOI
  37. Cataldo DD, Tournoy KG, Vermaelen K, et al. Matrix metalloproteinase-9 deficiency impairs cellular infiltration and bronchial hyperresponsiveness during allergen-induced airway inflammation. Am J Pathol.2002;161: 491-498. · DOI
  38. Hoffstein S, Weissmann G. Microfilaments and microtubules in calcium ionophore-induced secretion of lysosomal enzymes from human polymorphonuclear leukocytes. J Cell Biol.1978;78: 769-781. · DOI
  39. Gu Y, Filippi MD, Cancelas JA, et al. Hematopoietic cell regulation by Rac1 and Rac2 guanosine triphosphatases. Science. 2003;302: 445-449. · DOI · Paper page
  40. Herlaar E, Brown Z. p38 MAPK signalling cascades in inflammatory disease. Mol Med Today. 1999;5: 439-447. · DOI
  41. Mellor H, Parker PJ. The extended protein kinase C superfamily. Biochem J.1998;332: 281-292. · DOI
  42. Benard V, Bohl BP, Bokoch GM. Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J Biol Chem.1999;274: 13198-13204. · DOI · Paper page
  43. Geijsen N, van Delft S, Raaijmakers JA, et al. Regulation of p21rac activation in human neutrophils. Blood. 1999;94: 1121-1130. · DOI

Cited by

See all 132

Metadata

Authors
Abdel-Latif, D., Steward, M., Macdonald, D. L., Francis, G. A., Dinauer, M. C., & Lacy, P.
Venue
Blood
Published
2004-08-01
Volume
104
Issue
3
Pages
832-839
ISSN
  • 0006-4971
  • 1528-0020
Cited by
132
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review