Hypoxia-induced Haem Oxygenase-1 gene expression in neonatal rat cardiac myocytes

Long, Xilin; Wu, Guihua; Rozanski, Dennis J.; Boluyt, Marvin O.; Crow, Michael T.; Lakatta, Edward G.

doi:10.1046/j.1444-2892.2001.00100.x

Cited by 9 publications

(2 citation statements)

References 34 publications

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“…This choice is justified because, on one side activation/translocation of PKC occurs after hypoxia exposure [Long et al, 2001; Cataldi et al, 2004] and, on the other correlates with the expression of lipid microdomains [Bécart et al, 2003; Botto et al, 2007]. Furthermore, an inhibition in the expression of γENaC has been described in response to extreme hypoxia [Planes et al, 2002]; HO‐1 expression is implicated in antioxidant response to hypoxia [Long et al, 2001; Sato et al, 2006]; finally, AQP5 is the specific protein for water transport in alveolar cells [Verkaman et al, 2000; Johnson, 2007]. Figure 2 shows the total content of the above mentioned proteins in MEF in the two cell lines.…”

Section: Resultsmentioning

confidence: 99%

Hypoxia‐induced modifications in plasma membranes and lipid microdomains in A549 cells and primary human alveolar cells

Botto¹,

Beretta²,

Bulbarelli³

et al. 2008

J of Cellular Biochemistry

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We evaluated the response to mild hypoxia exposure of A549 alveolar human cells and of a continuous alveolar cell line from human excised lungs (A30) exposed to 5% O(2) for 5 and 24 h. No signs of increased peroxidation and of early apoptosis were detected. After 24 h of hypoxia total cell proteins/DNA ratio decreased significantly by about 20%. Similarly, we found a decrease in membrane phospholipid and cholesterol content. The membrane fluidity assessed by fluorescence anisotropy measurements was unchanged. We also prepared the detergent resistant membrane fraction (DRM) to analyze the distribution of the two types of lipid microdomains, caveolae and lipid rafts. The DRM content of Cav-1, marker of caveolae, was decreased, while CD55, marker of lipid rafts, increased in both cell lines. Total content of these markers in the membranes was unchanged indicating remodelling of their distribution between detergent-resistant and detergent-soluble fraction of the cellular membrane. The changes in protein markers distribution did not imply changes in the corresponding mRNA, except in the case of Cav-1 for A30 line. In the latter case we found a parallel decrease in Cav-1 and in the corresponding mRNA. We conclude that an exposure to a mild degree of hypoxia triggers a significant remodelling of the lipid microdomains expression, confirming that they are highly dynamic structures providing a prompt signalling platform to changes of the pericellular microenvironment.

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Section: Resultsmentioning

confidence: 99%

Hypoxia‐induced modifications in plasma membranes and lipid microdomains in A549 cells and primary human alveolar cells

Botto¹,

Beretta²,

Bulbarelli³

et al. 2008

J of Cellular Biochemistry

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“…Hypoxia causes a series of biochemical and pathophysiological changes, which involve changes of cytokine signaling leading to altered gene transcription and ultimately to membrane damage and cell death (Long et al, 2001;Lushchak and Bagnyukova, 2007;Yachie et al, 1999). However, there are conflicting reports on the response of HO-1 to hypoxic stress in mammals.…”

Section: Introductionmentioning

confidence: 99%

Inductive transcription and protective role of fish heme oxygenase-1 under hypoxic stress

Wang

Zhong

Qiao

et al. 2008

Journal of Experimental Biology

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SUMMARYHeme oxygenase-1 is the rate-limiting enzyme in the degradation of heme into biliverdin, carbon monoxide and free divalent iron. In this study, we cloned heme oxygenase isoform 1 (CaHO-1) from a hypoxia-tolerant teleost fish Carassius auratus. The fulllength cDNA of CaHO-1 is 1247 bp and encodes a protein of 272 amino acids. RT-PCR and real-time PCR analysis indicated that CaHO-1 was predominantly transcribed in posterior kidney, head kidney, gill and intestine, and induction of gene transcription was observed predominantly in posterior kidney under hypoxic stress. Moreover, the hypoxia-induced transcription was confirmed in goldfish larvae and in in vitro cultured CAB cells. Fluorescence of the HO-1-GFP fusion protein revealed a cytoplasmic and plasma membrane localization, which was consistent with the putative transmembrane structure. Subsequently, we established a stably transfected CAB/pcDNA3.1-HO-1 cell line and a control CAB/pcDNA3.1 cell line, and found that the number of dead cells was obviously reduced in the pcDNA3.1-HO-1-transfected group following 4 days of hypoxic (1% O 2 ) treatment in comparison with numerous detached dead cells in the control pcDNA3.1-transfected cells. Furthermore, a significant cell viability difference between the two kinds of transfected cells during hypoxia-reoxygenation was revealed. Therefore, the data suggest that fish HO-1 might play a significant protective role in cells in response to hypoxic stress.

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Characterization of duplicated heme oxygenase-1 genes and their responses to hypoxic stress in blunt snout bream (Megalobrama amblycephala)

Guan

Guo

Sun

et al. 2017

Fish Physiol Biochem

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The heme oxygenase (HO)-1 is a cytoprotective enzyme that can be involved in cytoprotection against hypoxia stress. In this study, we cloned duplicated HO-1a and HO-1b cDNAs in hypoxia-sensitive blunt snout bream (Megalobrama amblycephala). HO-1a and HO-1b encode peptides with 272 amino acids and 246 amino acids, respectively, and they share a low sequence identity of 55%. HO-1a and HO-1b mRNAs were maternally deposited in the zygote, and the mRNAs decreased to the lowest levels at 8 hpf. Both mRNAs were significantly (p < 0.01) expressed from 12 hpf and fluctuated but maintained a high level after 16 hpf. Using in situ hybridization, HO-1a and HO-1b mRNAs were ubiquitously expressed in embryos at 12 hpf. At 24 and 36 hpf, HO-1b transcripts were detected in the mid- and hindbrain, respectively, whereas HO-1a was mainly transcribed in the eyes and endoderm at 24 hpf and in the brain at 36 hpf. In adult fish, HO-1a was abundantly expressed in the heart, liver, gill, kidney, spleen, and brain, while HO-1b mRNA was detected mainly in the kidney. After exposure to hypoxic stress, both HO-1a and HO-1b mRNAs were upregulated significantly in the gill and liver but downregulated significantly in the brain (p < 0.01). These findings suggest that duplicated HO genes have evolved divergently and yet play overlapping biological roles in regulating the response to hypoxia in M. amblycephala.

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Hypoxia-induced Haem Oxygenase-1 gene expression in neonatal rat cardiac myocytes

Cited by 9 publications

References 34 publications

Hypoxia‐induced modifications in plasma membranes and lipid microdomains in A549 cells and primary human alveolar cells

Hypoxia‐induced modifications in plasma membranes and lipid microdomains in A549 cells and primary human alveolar cells

Inductive transcription and protective role of fish heme oxygenase-1 under hypoxic stress

Characterization of duplicated heme oxygenase-1 genes and their responses to hypoxic stress in blunt snout bream (Megalobrama amblycephala)

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