Heme Oxygenase-1 (HO-1) Antibody Review

Introduction

a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide. PMID: 15105257
a stress-induced antiinflammatory protein. PMID: 17265482
a marker of cellular response to oxidative stress, may represent a candidate biomarker of ageing. PMID: 17221286
a protective gene with anti-inflammatory and anti-apoptotic actions. PMID: 17219692
plays an important role in the early adaptation processes. PMID: 17203280
highly inducible by a large number of physical and chemical factors. PMID: 17065227
oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic. PMID: 17018578
a protective gene with anti-inflammatory and anti-apoptotic actions. PMID: 17003813
the inducible isoform of heme oxygenase, is a cytoprotective enzyme that plays a central role in the defense against oxidative and inflammatory insults in the lung. PMID: 16980551
the rate-limiting enzyme in heme catabolism, can be induced in response to various oxidative stimuli, and its induction is thought to be critical in the cellular defense against oxidative tissue injuries. PMID: 16964402
a key regulator of pregnancy success. PMID: 16386310
plays an important role in angiogenesis. PMID: 14517400

Normal Expression

Cytoplasmic HO-1 was clearly detected by fluorescence microscopy. PMID: 16966997
fluorescence detection suggests that HO-1 was present also in the nucleus, and in the nucleoli. PMID: 14766239
HO-1 immunoreactivity was observed in vascular endothelial cells, odontoblasts and some fibroblasts cells in normal human dental pulp. PMID: 16704082
The results from immunohistochemistry demonstrated that HO-1 expression was significantly higher in cigarette smokers (p < 0.05). HO-1 was noted in the basal layers of epithelium, inflammatory cells, and fibroblasts in specimens from cigarette smoking. PMID: 15853972
Ectoplacental cone in embryonic day (E) 6.5 embryo already showed HO-1 protein expression, which became restricted only to trophoblastic cells after placenta formation was completed on day E14.5. The placenta of E13.5-E14.5 embryos expressed high levels of HO-1 mRNA, which was decreased significantly towards the end of pregnancy. However, HO-1 expression in placenta was significantly higher than uterus throughout the gestational period. PMID: 15081633
HO-1 was constitutively expressed only in Kupffer cell cultures but was also inducible in hepatocytes. PMID: 14623930
HO-1 was immunodetected in preparations from cartilage and also in chondrocytes cultured in the absence of stimulation. PMID: 14599563
Immunohistochemistry showed that in biopsy specimens from normal livers, HO-1 protein expression was restricted to Kupffer cells. Biopsy specimens from cirrhotic patients displayed HO-1 protein both in macrophages and in myofibroblasts within fibrotic septa. PMID: 12891549
Expression pattern of HO-1 immunoreactive protein was studied in liver biopsies by immunohistochemistry, revealing constitutive expression in Kupffer cells but not in hepatocytes. HO-1 was, however, inducible in hepatocytes and vascular tissue under pathological conditions, e.g. associated with fatty degeneration or liver malignancies. PMID: 12865654
HO-1 is an inducible form expressed mainly in macrophages. In rat ontogeny, HO-1 immunoreactivity was detected in mononuclear cells in the yolk sac at 10 days of gestation. HO-1-expressing cells were then detected in the fetal liver and their numbers increased during the gestational period. The numbers of HO-1-positive cells and HO-1 mRNA levels in the liver peaked at 18 days of gestation. PMID: 12846555
HO-1 is expressed in various tissue macrophages, especially Kupffer cells. Immunohistochemistry in the control rat liver revealed that Kupffer cells constitute a major cellular component expressing HO-1, while hepatocytes exhibited little expression. PMID: 11436987
HO-1 and HO-2 were immunolocalized in the cytoplasm and/or nuclei of brown adipocytes, in parenchymal capillaries, arteries and in some veins and nerves. Whereas cold exposure did not affect HO-2 expression, it significantly increased the expression of HO-1. PMID: 11150503
HO-1 was expressed mainly in a subpopulation of Kupffer cells, and the expression in hepatic stellate cells, sinusoidal endothelial cells, and hepatocytes was little, if any. PMID: 11124818
Stronger HO-1 expression was detected in the internal layer of the median eminence (ME) of aged than of young rats. Moreover, the cells expressing HO-1 were larger in the aged than the young animals. Electron microscopy indicated these cells with HO-1-like immunoreactivity (HO-1-LI) to be astrocytes. PMID: 10477115
In normal and BPH tissue, columnar epithelial cells of acini and ducts and cells in stroma displayed HO-1 immunoreactivity; in all cells, perinuclear staining was prominent. PMID: 8650873

Abnormal Expression

Many HO-1 positive cells were found particularly in the alveolar macrophages during immunostaining. These findings suggest that HO-1 is related to lung injury arising from exposure to crystalline silica. PMID: 16612041
HO-1 was expressed more abundantly in the lesions of synovial tissue from patients with rheumatoid arthritis (RA) than in those from the other patient groups. PMID: 16572448
HO-1 expression was more expressed in left ventricles of myocardium in basic conditions and after ischemia/reperfusion as well as after its previous induction by hemin. PMID: 16553297
Increased HO-1 immunoreactivity was detected in hippocampal and cortical neurons after 1 hour of ischemia, and was also observed in astroglial cells. PMID: 16464361
Glial HO-1 expression in the MCI temporal cortex and hippocampus was significantly greater than in the non-demented group and did not differ from AD values. PMID: 16399210
Glial heme oxygenase-1 is over-expressed in the CNS of subjects with Alzheimer disease (AD), Parkinson disease (PD) and multiple sclerosis (MS). PMID: 16222706
HO-1 positive correlate with the process of inflammation in allergic rhinitis guinea pigs, which suggests that the endogenous carbon monoxide might play a significant role in the pathogenesis of allergic rhinitis. PMID: 16124649
expressed in carotid atherosclerotic plaques infected by Helicobacter pylori and is more prevalent in asymptomatic subjects. PMID: 16100019
There is a higher expression of HO-1 in patients with coronary heart disease (CHD). The levels of HO-1 protein are associated with the severity of CHD. PMID: 15869055
There is a higher expression of HO-1 in patients with acute myocardial infarction, and a lower expression in patients with normal coronary artery. PMID: 15355615
Immunohistochemical studies showed that HO-1 was expressed in a variety of cell types, including the airway epithelia, alveolar macrophages and vascular smooth muscular cells in injured lungs following limb ischemia/reperfusion in rats. PMID: 15294108
Macrophage HO-1 staining was increased in diseased lungs as compared with normal control subjects and correlated with myeloperoxidase staining. PMID: 15184199
HO-1 was found to stain neurons and microglia/macrophages in cases with traumatic brain injury (TBI), whereas no positive staining except for a few round cells in the arachnoidal space was observed in control cases. PMID: 12935610
HO-1 is expressed in the lung and liver tissues in a rat model of burns. PMID: 12052367
HO-1 can be induced in the retina in vitro by conditions of oxidative stress and that enzyme expression is confined exclusively to Muller cells. PMID: 11328753
Expressed in neurofibrillary tangles, senile plaque neurites, granulovacuolar degeneration, and neuropil threads in Alzheimer disease brain. PMID: 8030754

Expression Alteration

HO-1 was markedly up-regulated after IRI, and its expression was decreased by cyclosporine (2.06 folds). PMID: 17219692
Heme oxygenase-1 expression increased dramatically in cytosolic and mitochondrial fractions of human alveolar (A549), or bronchial epithelial cells (Beas-2b) exposed to either hemin, lipopolysaccharide, or CSE. PMID: 17079780
HO-2 may down-regulate the expression of HO-1, thereby directing the co-ordinated expression of HO-1 and HO-2. PMID: 17064313
The cadmium can induce the apoptosis of the human embryonic kidney cells and up-regulate the expression of HO-1. PMID: 16600087
the expression of PBMC HO-1 protein and mRNA increased significantly in asthmatic patients, and HO-1 may play a significant role in the pathogenesis of asthma. The expression of HO-1 may bear a relation with severity of asthma. PMID: 16196283
HO-1 and iNOS protein expression was induced by ovariectomy (Ovx) and was extremely high 2-6 weeks after Ovx compared with the sham-operated group. PMID: 15925283
HO-1 expression drastically decreases during human and rat DC maturation induced in vitro. PMID: 15920011
Exercise-induced expression of heme oxygenase-1 in human lymphocytes. PMID: 15875813
a cytoprotective protein and has recently been identified as a graft survival gene, and its expression is increased in small-for-size liver allografts. PMID: 15849554
There was a close correlation between bilirubin and HO-1 expression, and both bilirubin and HO-1 were observed in damaged neurons at early times, and astrocytes at later times (weeks), after kainate injection. PMID: 15751016
Heart failure (HF) causes increased pulmonary HO-1 expression and activity, which emanates largely from siderophages. Up-regulation of HO-1 may have pulmonary protective in HF. PMID: 15621048
Heme oxygenase protein is elevated in the lungs of patients with acute respiratory distress syndrome (ARDS) and may contribute to the changes in iron mobilization, signaling, and regulation seen in this condition. PMID: 15190962
There is a possible age-related decline in HO-1 expression, whereas catalase expression remains unchanged with aging. PMID: 15111615
HO-1 and ferritin underwent an age-related increase in human brain, especially in the cerebral cortex. Our results also indicate that various stress responses may persist in the aged human brain. PMID: 12935634
expression of HO-1 is increased within the lung tissue in allergic airway inflammation and the overexpression of HO-1 could enhanced allergic airway inflammation. PMID: 12486335
HO-1 expression is increased in human lung allografts with acute cellular rejection and obliterative bronchiolitis. PMID: 12398878
lung HO-1 protein and activity are upregulated only during early chronic hypoxia, whereas persistent COHb elevations indicate high endogenous CO production rates at nonpulmonary sites. PMID: 10749758
HO-1 immunoreactivity is greatly increased in neurons and astrocytes of the hippocampus and cerebral cortex of individuals with AD and colocalizes to senile plaques and neurofibrillary tangles. PMID: 10746601

Function

contribute to host defense reactions against various stresses. In addition, recent reports have suggested that HO-1 modulates immunocyte activation and functions. PMID: 17234154
a rate-limiting enzyme in heme catabolism, has also been shown to accumulate during glioma progression and to play a critical role in FoxP3 mediated immune suppression. PMID: 17216339
HO-1/CO system has a potent protective effect on acute liver injury induced by carbon tetrachloride in rats. Induction of HO-1 expression and low concentration of CO can inhibit the progress of hepatic damage. PMID: 17173083
a link between HO-1, regulated via the cGMP system and NO-induced cytotoxicity in human pulp cells, suggest a protective role for HO-1 in pulpal inflammation. PMID: 17138185
plays a major role in mediating cytoprotection and iron homeostasis against NO toxicity in immortalized and malignant oral keratinocytes. PMID: 17095152
has anti-inflammatory effects, probably via enhancement of the secretion of IL-10 and promotion of the percentage of CD4+CD25(high) Treg. PMID: 17056518
HO-1 modulates oxidative stress and white matter injury in the acutely injured spinal cord. This modulation may be partially attributed to the ability of HO-1 to stabilize the blood-spinal cord barrier and limit neutrophil infiltration. PMID: 17047682
HO-1 induction protects astrocytes from the oxidative toxicity of Hb, but has no effect on neuronal injury. PMID: 16999934
Basal rather than induced heme oxygenase-1 levels are crucial in the antioxidant cytoprotection. PMID: 16982915
the first report showing the protective role of HO-1 against irritant-induced gastric lesions. PMID: 16945925
HO-1 may prevent the generation of oxidative stress only when the anti-oxidant defence system is still operative. PMID: 16895548
HO-1 activation is a key mediator of the anti-inflammatory effects of acute alcohol on monocytes. PMID: 16888021
Heme oxygenase-1 (HO-1) protects endothelial cells (EC) from undergoing apoptosis. This effect is mimicked by CO, generated via the catabolism of heme by HO-1. PMID: 16849502
HO-1 seems to mediate the protective response of pancreatic islets against the oxidative stress that is due to high glucose conditions. PMID: 16778382
upregulation of HO-1 provides protection against renal injury that follows unilateral ureteral obstruction (UUO). PMID: 16597687
vascular HO-1 exerts its protective effect against cardiovascular damage, possibly through the inhibition of oxidative stress. PMID: 16181103
early HO-1 mRNA expression in leukocytes may represent oxidative stress and may predict the severity of liver and renal dysfunction during sepsis. PMID: 15834314
HO-1 may be related to lung disorder induced by dust and therefore can act as a biomarker of lung injury due to dust exposure. PMID: 15814490
determination of glial HO-1-ir is a useful histochemical marker for early stages of striatal damage. PMID: 15652698
HO-1 reduces the oxidative cell injury and protects the endothelial cells, if its expression is appropriately controlled. PMID: 15378604
HO-1 has been shown to have anti-inflammatory, antiapoptotic, and antiproliferative effects, and it is now known to have salutary effects in diseases as diverse as atherosclerosis and sepsis. PMID: 12091240
overexpression of HO-1 in the cardiomyocyte protects against ischemia and reperfusion injury, thus improving the recovery of cardiac function. PMID: 11463724

Diagnostic and Therapeutic Value

HO-1 or exposure to its end product CO counters autoimmune neuroinflammation and thus might be used therapeutically to treat multiple sclerosis (MS). PMID: 17256058
a cytoprotective enzyme, can be induced in tumors in response to anti-cancer therapies. PMID: 17148680
The capability of whole-body temporal imaging of HO-1 expression provides a valuable tool in the development of novel strategies to modulate HO-1 expression in liver transplantation. PMID: 17058249
a potential therapeutic application for HO-1 gene in improving islet survival/function in human islet transplantation. PMID: 17003650
heme oxygenase-1 provides neuroprotection against acute excitotoxicity and suggest that potential intervention that can increase heme oxygenase-1 activity within the brain should be considered as a therapeutic target in acute and potentially chronic neurological disorders. PMID: 16828975
expression of HO-1 in a graft recipient can be essential for long-term graft survival and for induction of tolerance and that modulation of HO-1 expression/activity can be used therapeutically to synergize in the generation of graft tolerance. PMID: 16473885
an increase in HO-1 during transplantation is more protective than high HO-1 expression before transplantation. PMID: 15996234
HO-1 has thus emerged as a key target molecule with therapeutic implications. PMID: 15933765
Transplantation of human MSCs could up-regulate HO-1 expression in infarct rat hearts, which might play an important role in protecting transplanted MSCs, cardiomyocytes survival, and cardiac function improvement during the early stage after MI. PMID: 15797262
HO-1 may be a novel therapeutic target in patients with inflammatory bowel disease. PMID: 15298625
HO-1 could be used clinically as a marker for tumors possessing the potential for lymph node metastasis. PMID: 14662411
The expression of HO-1 is increased within the lung tissue in allergic airway inflammation. Measurement of HO-1 activity may be clinically useful in the management of asthma. PMID: 11591199
high heme oxygenase-1 expression in oral SCCs can be useful in identifying patients at low risk of lymph node metastasis. PMID: 10378773

Review Articles

Heme oxygenase-1 and cardiovascular disease. PMID: 16528678
Heme oxygenase-1: from bench to bedside. PMID: 15901614
Development of vascular biology over the past 10 years: heme oxygenase-1 in cardiovascular homeostasis. PMID: 15760253
Heme oxygenase-1: redox regulation of a stress protein in lung and cell culture models. PMID: 15650398
Heme oxygenase-1 (HO-1), a protective gene that prevents chronic graft dysfunction. PMID: 15649645
Heme oxygenase-1 as a protective gene. PMID: 15499991
Protective role of heme oxygenase-1 in renal ischemia. PMID: 15345147
Complex role of heme oxygenase-1 in angiogenesis. PMID: 15345146
Heme oxygenase-1: a novel therapeutic target in oxidative tissue injuries. PMID: 15180563
Heme oxygenase-1: transducer of pathological brain iron sequestration under oxidative stress. PMID: 15105257
Role of heme oxygenase-1 in cardiovascular function. PMID: 14529547
Heme oxygenase-1: unleashing the protective properties of heme. PMID: 12909459
Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress. PMID: 12470502
Heme oxygenase-1 system in organ transplantation. PMID: 12394829
Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs. PMID: 12086318
Heme oxygenase-1: role in brain aging and neurodegeneration. PMID: 11053673
Heme oxygenase-1: function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. PMID: 8679227

Applications

ELISA

HO-1 concentration was measured in cerebral spinal fluid samples from 48 infants and children following TBI and 7 control patients by ELISA. PMID: 16943657
Serum HO-1 and 8-hydroxydeoxyguanosine (a marker of oxidative stress) were measured by enzyme-linked immunosorbent assay. Levels of HO-1 were measured by immunohistochemistry and immunoblotting. PMID: 16858012

Flow Cytometry (FC)

By using flow cytometry the present investigation demonstrated a rise in the cytoplasmic expression of HO-1 in lympho- (L), mono- (M) and granulocytes (G) of 9 endurance-trained male subjects after a half marathon run. PMID: 9890653

Immuno-Electron Microscopy

The mitochondrial localization of heme oxygenase-1 in Beas-2b was confirmed using immunogold-electron microscopy and immunofluorescence labeling on confocal laser microscopy. PMID: 17079780

Immunohistochemistry (IHC)

HO-1 expression were evaluated by immunohistochemical examination of the colonic tissue. PMID: 17124609
To determine the time-course of human subcutaneous hemorrhage, heme oxygenase (HO)-1 expression and macrophage infiltration were observed using an immunohistochemical technique and semiquantitative analysis. PMID: 16039813
Immunohistochemical stainings for HO-1 were performed in paraffin-embedded ischemic colitis tissues. PMID: 15908766
The levels of HO-1 protein expression in monocyte and lymphocyte in the subjects were tested by immunohistochemistry and western blot. PMID: 15869055
Immunohistochemical staining showed that HO-1 was mainly produced by infiltrating macrophages. PMID: 15589739
Immunohistochemical studies demonstrated that HO-1 expression occurred predominantly in hepatocytes, but not in non-parenchymal cells. PMID: 15547665
Levels of HO-1 protein expression in monocyte and lymphocyte isolated from the patients were determined by immunohistochemistry and Western blot. PMID: 15355615
Immunohistochemical analysis of heme oxygenase-1 in preneoplastic and neoplastic lesions during chemical hepatocarcinogenesis. PMID: 15312126
HO-1 and VEGF proteins were analyzed by immunohistochemistry in cadaveric and living donor kidneys after ischemia-reperfusion. PMID: 14638927
Immunohistochemical results showed that HO-1 expressed primarily in skeletal muscle cytoplasma after ischemia-reperfusion of hind limb in rats. PMID: 12916305
In the present study, immunohistochemistry was used to assess HO-1 expression in various postmortem human brain specimens derived from PD and control subjects. PMID: 9514830
Regulation and immunohistochemical analysis of stress protein heme oxygenase-1 in rat kidney with myoglobinuric acute renal failure. PMID: 9367889
Presently, we have determined the pattern of tissue expression of the stress-inducible isozyme, HO-1 (HSP32), in human prostate under normal and pathologic conditions, by immunohistochemistry. PMID: 8650873
Using immunohistochemistry and immunofluorescent labeling in conjunction with laser scanning confocal microscopy, we observed intense immunoreactivity of heme oxygenase-1 in neurons of the hippocampus and temporal cortex of Alzheimer-diseased (AD) brain relative to age-matched control specimens PMID: 7778849

Radioimmunoassay (RIA)

Quantification of brain HO-1 protein by HO-1 radioimmunoassay revealed a fourfold increase at 6 h posttreatment. PMID: 1737989

Western Blot (WB)

The expression of cell cycle related proteins, of Bcl-2 and of HO-1 were analyzed by western blot. The cellular localization and expression of HO-1 were detected by immnunohistochemistry. PMID: 17169158
The expression of HO-1 was observed by western blot analysis and immunostaining in the lungs of rats. PMID: 16612041
The tissue HO-1 and iNOS mRNA and protein levels were estimated with reverse transcription polymerase chain reaction and Western blot method. PMID: 15607619
subcellular localization of HO-1 using confocal laser scanning microscopy (CLSM) and the expression by Western blot in primary astroglial cells during differentiation and after exposure to glutamate (100microM). PMID: 14766239
Using immunocytochemistry and Western blotting, this study demonstrates the development changes of HO-1 protein expression in normal brain from rats at postnatal day 7 (P7), P14, P21, and adult. PMID: 9541737