Exocytosis of Neutrophil Granule Subsets and Activation of Prolyl Isomerase 1 Are Required for Respiratory Burst Priming
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This study tested the hypothesis that priming the neutrophil respiratory burst requires both granule exocytosis and activation of the prolyl isomerase Pin1. Fusion proteins containing the TAT cell permeability sequence and either the SNARE domain of syntaxin-4 or the N-terminal SNARE domain of SNAP-23 were used to examine the role of granule subsets in TNF-mediated respiratory burst priming using human neutrophils. Concentration-inhibition curves for exocytosis of individual granule subsets and for priming of fMLF-stimulated superoxide release and phagocytosis-stimulated H 2 O 2 production were generated. Maximal inhibition of priming ranged from 72 to 88%. Linear regression lines for inhibition of priming versus inhibition of exocytosis did not differ from the line of identity for secretory vesicles and gelatinase granules, while the slopes or the y-intercepts were different from the line of identity for specific and azurophilic granules. Inhibition of Pin1 reduced priming by 56%, while exocytosis of secretory vesicles and specific granules was not affected. These findings indicate that exocytosis of secretory vesicles and gelatinase granules and activation of Pin1 are independent events required for TNF-mediated priming of neutrophil respiratory burst.
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PMNs carry three different types of granules: primary azurophilic, secondary specific, and tertiary gelatinase granules, which contain distinct anti-microbial effector molecules.
“PMNs carry three different types of granules (Fig. 1): primary azurophilic, secondary specific, and tertiary gelatinase granules. These granules contain distinct anti-microbial effector molecules.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [115]
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- Authors
- McLeish, K. R., Uriarte, S. M., Tandon, S., Creed, T. M., Le, J., & Ward, R. A.
- Affiliations
- University of Louisville (US)
- Venue
- Journal of Innate Immunity
- Publisher
- S. Karger AG
- Published
- 2013
- Volume
- 5
- Issue
- 3
- Pages
- 277-289
- ISSN
- 1662-811X (ISSN-L)
- 1662-8128
- PMC
- PMC3691856
- OpenAlex
- W1981754471
- Cited by
- 32
- References
- 34
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 5 · 2022: 3 · 2021: 4 · 2020: 4 · 2019: 1 · 2018: 1 · 2017: 5 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 1
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Innate Immunity (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 BX001838)
- National Heart, Lung, and Blood Institute (R00HL087924)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- neutrophil respiratory burst, exocytosis, Pin1, peptidyl-prolyl isomerase, secretory vesicles, specific granules, azurophilic granules, superoxide release, hydrogen peroxide production, syntaxin 4, SNAP23, SNARE proteins, neutrophil activation
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Enzyme Activation, Exocytosis, Female, Humans, Male, N-Formylmethionine Leucyl-Phenylalanine, Neutrophils, Tumor Necrosis Factor-alpha, Respiratory Burst, Peptidylprolyl Isomerase, Secretory Vesicles, Qa-SNARE Proteins, Qb-SNARE Proteins, Qc-SNARE Proteins
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