Characterization of Mitochondrial and Extra-mitochondrial Oxygen Consuming Reactions in Human Hematopoietic Stem Cells
Open accessAbstract
This study was aimed to characterize the mitochondrial and extra-mitochondrial oxygen consuming reactions in human CD34+ hematopoietic stem cells. Cell samples were collected by apheresis following pre-conditioning by granulocyte colony-stimulating factor and isolated by anti-CD34 positive immunoselection. Polarographic analysis of the CN-sensitive endogenous cell respiration revealed a low mitochondrial oxygen consumption rate. Differential absorbance spectrometry on whole cell lysate and two-dimensional blue native-PAGE analysis of mitoplast proteins confirmed a low amount of mitochondrial respiratory chain complexes thus qualifying the hematopoietic stem cell as a poor oxidative phosphorylating cell type. Confocal microscopy imaging showed, however, that the intracellular content of mitochondria was not homogeneously distributed in the CD34+ hematopoietic stem cell sample displaying a clear inverse correlation of their density with the expression of the CD34 commitment marker. About half of the endogenous oxygen consumption was extra-mitochondrial and completely inhibitable by enzymatic scavengers of reactive oxygen species and by diphenylene iodinium. By spectral analysis, flow cytometry, reverse transcriptase-PCR, immunocytochemistry, and immunoprecipitation it was shown that the extra-mitochondrial oxygen consumption was contributed by the NOX2 and NOX4 isoforms of the O2-*. producer plasma membrane NAD(P)H oxidase with low constitutive activity. A model is proposed suggesting for the NAD(P)H oxidase a role of O2 sensor and/or ROS source serving as redox messengers in the activation of intracellular signaling pathways leading (or contributing) to mitochondriogenesis, cell survival, and differentiation in hematopoietic stem cells.
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Calmodulin affinity to eNOS is regulated via phosphorylation of Thr495.
“In turn, CaM affinity to eNOS is regulated via phosphorylation of Thr495.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [741]
Phosphorylation of Thr495 impairs calmodulin binding, thus blocking Ca2+/calmodulin-dependent activation of eNOS.
“Thr495 is located in the CaM-binding site of eNOS, and the phosphorylation of Thr495 impairs CaM binding, thus blocking Ca2+/CaM-dependent activation of the enzyme”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [741]
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References 73 · Cited by 209
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- Authors
- Piccoli, C., Ria, R., Scrima, R., Cela, O., D'Aprile, A., Boffoli, D., Falzetti, F., Tabilio, A., & Capitanio, N.
- Affiliations
- University of Perugia (IT)
- University of Foggia (IT)
- Corresponding author
- Capitanio, Nazzareno
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 280
- Issue
- 28
- Pages
- 26467-26476
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2002248781
- Cited by
- 209
- References
- 73
- Citations by year
- 2026: 1 · 2024: 10 · 2023: 7 · 2022: 10 · 2021: 5 · 2020: 7 · 2019: 8 · 2018: 9 · 2017: 10 · 2016: 9 · 2015: 11 · 2014: 21 · 2013: 20 · 2012: 16
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion)
- CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- hematopoietic stem cells, CD34+ cells, mitochondrial oxygen consumption, NADPH oxidase, NOX2, NOX4, reactive oxygen species, respiratory chain complexes, oxidative phosphorylation, mitochondrial distribution, CD34 expression, redox signaling, mitochondrial biogenesis
- MeSH terms
- Cell Line, Cells, Cultured, Electron Transport, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Hematopoietic Stem Cells, Humans, Image Processing, Computer-Assisted, Immunohistochemistry, Microscopy, Fluorescence, Mitochondria, Models, Biological, Oxidation-Reduction, Oxygen, Oxygen Consumption, Phosphorylation, Protein Binding, Spectrophotometry, Immunoblotting, Electrophoresis, Gel, Two-Dimensional, Signal Transduction, Granulocyte-Macrophage Colony-Stimulating Factor, Reactive Oxygen Species, Microscopy, Confocal, Antigens, CD34, NADPH Oxidases, Reverse Transcriptase Polymerase Chain Reaction, Protein Structure, Quaternary, Immunoprecipitation
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