CD38 knockout mice show significant protection against ischemic brain damage despite high level poly-ADP-ribosylation
Open accessAbstract
Several enzymes in cellular bioenergetics metabolism require NAD+ as an essential cofactor for their activity. NAD+ depletion following ischemic insult can result in cell death and has been associated with over-activation of poly-ADP-ribose polymerase PARP1 as well as an increase in NAD+ consuming enzyme CD38. CD38 is an NAD+ glycohydrolase that plays an important role in inflammatory responses. To determine the contribution of CD38 activity to the mechanisms of post-ischemic brain damage we subjected CD38 knockout (CD38KO) mice and wild-type (WT) mice to transient forebrain ischemia. The CD38KO mice showed a significant amelioration in both histological and neurologic outcome following ischemic insult. Decrease of hippocampal NAD+ levels detected during reperfusion in WT mice was only transient in CD38KO animals, suggesting that CD38 contributes to post-ischemic NAD+ catabolism. Surprisingly, pre-ischemic poly-ADP-ribose (PAR) levels were dramatically higher in CD38KO animals compared to WT animals and exhibited reduction post-ischemia in contrast to the increased levels in WT animals. The high PAR levels in CD38 mice were due to reduced expression levels of poly-ADP-ribose glycohydrolase (PARG). Thus, the absence of CD38 activity can not only directly affect inflammatory response, but also result in unpredicted alterations in the expression levels of enzymes participating in NAD+ metabolism. Although the CD38KO mice showed significant protection against ischemic brain injury, the changes in enzyme activity related to NAD+ metabolism makes the determination of the role of CD38 in mechanisms of ischemic brain damage more complex.
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CD38 is expressed in brain, and CD38 knockout mice show significant protection against ischemic brain damage.
“Despite CD38 being a lymphocyte differentiation antigen, it is also expressed in the brain (Mizuguchi et al., 1995), and CD38 knockout mice show significant protection against ischemic brain damage (Long et al., 2017).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Long et al., 2017
Cd38-knockout mice are protected from neuronal cell death on ischaemic brain injury.
“Cd38-knockout mice are also protected from neuronal cell death on ischaemic brain injury162.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [162]
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- Authors
- Long, A., Park, J. H., Klimova, N., Fowler, C., Loane, D. J., & Kristian, T.
- Affiliations
- VA Maryland Health Care System (US)
- University of Maryland, Baltimore (US)
- Venue
- Neurochemical Research
- Published
- 2016-08-12
- Volume
- 42
- Issue
- 1
- Pages
- 283-293
- ISSN
- 0364-3190 (ISSN-L)
- 1573-6903
- PMC
- PMC5580240
- OpenAlex
- W2514539965
- Cited by
- 44
- References
- 33
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 8 · 2023: 7 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 2 · 2017: 5
- FWCI
- 2.49
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Neurochemical Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01BX000917)
- National Institute of Neurological Disorders and Stroke (R01NS082308)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Neuroscience › Neurology › Neurological Disorders and Treatments
- Life Sciences › Neuroscience › Neurology › Neurological Disease Mechanisms and Treatments
- Keywords
- CD38, NAD+ metabolism, ischemic brain injury, transient forebrain ischemia, poly(ADP-ribose), PARP1, poly(ADP-ribose) glycohydrolase, NAD+ depletion, reperfusion, neuroprotection, hippocampus, inflammation
- MeSH terms
- Animals, Cells, Cultured, Brain Ischemia, Glycoside Hydrolases, Hippocampus, Male, Membrane Glycoproteins, Mice, Inbred C57BL, Poly Adenosine Diphosphate Ribose, Random Allocation, Mice, Knockout, Mice, ADP-ribosyl Cyclase 1
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