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Cited by 256Heme Oxygenase-1 and Carbon MonoxideNitric Oxide and Endothelin EffectsHemoglobin structure and function

The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.

Antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes

Turkseven, Saadet, Kruger, Adam, Mingone, Christopher J., Kaminski, Pawel, Inaba, Muneo, Rodella, Luigi F., Ikehara, Susumu, Wolin, Michael S., Abraham, Nader G.·2005·American Journal of Physiology-Heart and Circulatory Physiology
DOI 10.1152/ajpheart.00024.2005
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Abstract

Increased heme oxygenase (HO)-1 activity attenuates endothelial cell apoptosis and decreases superoxide anion (O 2−) formation in experimental diabetes by unknown mechanisms. We examined the effect of HO-1 protein and HO activity on extracellular SOD (EC-SOD), catalase, O 2−, inducible nitric oxide synthase (iNOS), and endothelial nitric oxide synthase (eNOS) levels and vascular responses to ACh in control and diabetic rats. Vascular EC-SOD and plasma catalase activities were significantly reduced in diabetic compared with nondiabetic rats ( P < 0.05). Upregulation of HO-1 expression by intermittent administration of cobalt protoporphyrin, an inducer of HO-1 protein and activity, resulted in a robust increase in EC-SOD but no significant change in Cu-Zn-SOD. Administration of tin mesoporphyrin, an inhibitor of HO-1 activity, decreased EC-SOD protein. Increased HO-1 activity in diabetic rats was associated with a decrease in iNOS but increases in eNOS and plasma catalase activity. On the other hand, aortic ring segments from diabetic rats exhibited a significant reduction in vascular relaxation to ACh, which was reversed with cobalt protoporphyrin treatment. These data demonstrate that an increase in HO-1 protein and activity, i.e., CO and bilirubin production, in diabetic rats brings about a robust increase in EC-SOD, catalase, and eNOS with a concomitant increase in endothelial relaxation and a decrease in O 2−. These observations in experimental diabetes suggest that the vascular cytoprotective mechanism of HO-1 against oxidative stress requires an increase in EC-SOD and catalase.

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Crossref · 10.1152/ajpheart.00024.2005

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Metadata

Authors
Turkseven, S., Kruger, A., Mingone, C. J., Kaminski, P., Inaba, M., Rodella, L. F., Ikehara, S., Wolin, M. S., & Abraham, N. G.
ORCID
Venue
American Journal of Physiology-Heart and Circulatory Physiology
Publisher
American Physiological Society
Published
2005-08
Volume
289
Issue
2
Pages
H701-H707
ISSN
  • 0363-6135 (ISSN-L)
  • 1522-1539
DOI
10.1152/ajpheart.00024.2005
OpenAlex
W2160708843
Cited by
256
References
57
Citations by year
2026: 2 · 2025: 2 · 2024: 5 · 2023: 6 · 2022: 13 · 2021: 18 · 2020: 12 · 2019: 15 · 2018: 8 · 2017: 8 · 2016: 11 · 2015: 7 · 2014: 8 · 2013: 10 · 2012: 17
FWCI
7.40
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Heart and Circulatory Physiology (publishedVersion)
  • PubMed (publishedVersion)
  • Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion)
Funders
National Heart, Lung, and Blood Institute (P01HL034300, HL 34300, HL55601)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
  • Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords
heme oxygenase-1, superoxide dismutase, catalase, experimental diabetes, oxidative stress, endothelial nitric oxide synthase, inducible nitric oxide synthase, cobalt protoporphyrin, tin mesoporphyrin, endothelium-dependent relaxation, acetylcholine, vascular function, bilirubin, carbon monoxide, endothelial cell apoptosis
MeSH terms
Acetylcholine, Animals, Antioxidants, Aorta, Blood Vessels, Catalase, Cobalt, Diabetes Mellitus, Experimental, Endothelium, Vascular, Enzyme Induction, Heme Oxygenase (Decyclizing), Immunohistochemistry, Protoporphyrins, Superoxides, Superoxide Dismutase, Vasodilator Agents, Rats, Sprague-Dawley, Nitric Oxide Synthase, Rats, Heme Oxygenase-1, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type III

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