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Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 3

act(p(HGNC:NR3C1)) positiveCorrelation p(HGNC:SERPINA1) View Subject | View Object

Under the same experimental conditions, A1AT blocked the ability of hemin to reduce GR activity (Fig. 10). PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

act(p(PFAM:"Pkinase_C")) negativeCorrelation p(HGNC:SERPINA1) View Subject | View Object

However, in the presence of A1AT, hemin did not change PKC activity significantly. PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

Out-Edges 13

p(HGNC:SERPINA1) decreases bp(GO:"neutrophil migration") View Subject | View Object

Under the same experimental conditions, addition of 1 mg/ ml A1AT significantly prevented hemin-induced neutrophil spreading and adhesion (Fig. 3A). PubMed:28716864

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Cell Ontology (CL)
endothelial cell
Text Location
Results

p(HGNC:SERPINA1) decreases bp(MESH:"Cell Adhesion") View Subject | View Object

Under the same experimental conditions, addition of 1 mg/ ml A1AT significantly prevented hemin-induced neutrophil spreading and adhesion (Fig. 3A). PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

p(HGNC:SERPINA1) decreases a(MESH:"Cell Adhesion Molecules") View Subject | View Object

Based on the previous findings that hemin induces neutrophil adhesion to endothelial cells [8] and that A1AT protects endothelial cells from neutrophil adhesion induced by fMLP [27], we investigated whether A1AT, as a scavenger of hemin, can prevent hemin-induced neutrophil adhesion to HUVECs. As shown in Fig. 4, neutrophils treated with hemin or fMLP (used as a positive control) exhibited a 3-fold higher adhesion to HUVECs compared with controls. However, the adherence of neutrophils treated with hemin/A1AT did not differ from controls (Fig. 4). PubMed:28716864

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Cell Ontology (CL)
endothelial cell
Text Location
Results

p(HGNC:SERPINA1) decreases p(HGNC:VIM) View Subject | View Object

In the presence of A1AT, this latter effect of hemin was significantly inhibited and did not differ from controls (Fig. 5B). PubMed:28716864

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Cell Ontology (CL)
endothelial cell
Text Location
Results

p(HGNC:SERPINA1) decreases p(HGNC:CXCL8) View Subject | View Object

In the presence of A1AT, hemin-induced release of IL-8 protein was inhibited significantly (Fig. 7B). PubMed:28716864

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Cell Ontology (CL)
endothelial cell
Text Location
Results

p(HGNC:SERPINA1) decreases a(MESH:"Reactive Oxygen Species") View Subject | View Object

The ability of hemin to trigger ROS production in neutrophils was abrogated significantly in the presence of A1AT (Fig. 8). PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

p(HGNC:SERPINA1) decreases p(HGNC:HMOX1) View Subject | View Object

In the presence of A1AT, hemin effect on HMOX1 expression was diminished significantly (Fig. 9A). PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

p(HGNC:SERPINA1) positiveCorrelation act(p(HGNC:NR3C1)) View Subject | View Object

Under the same experimental conditions, A1AT blocked the ability of hemin to reduce GR activity (Fig. 10). PubMed:28716864

Appears in Networks:
Annotations
Cell Ontology (CL)
neutrophil
Text Location
Results

p(HGNC:SERPINA1) negativeCorrelation act(p(PFAM:"Pkinase_C")) View Subject | View Object

However, in the presence of A1AT, hemin did not change PKC activity significantly. PubMed:28716864

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Cell Ontology (CL)
neutrophil
Text Location
Results

p(HGNC:SERPINA1) decreases p(HGNC:ELANE) View Subject | View Object

The main function of A1AT is to inhibit neutrophil elastase and proteinase 3. PubMed:28716864

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Cell Ontology (CL)
neutrophil
MeSH
Serum
MeSH
Malaria
Text Location
Discussion

p(HGNC:SERPINA1) decreases p(HGNC:PRTN3) View Subject | View Object

The main function of A1AT is to inhibit neutrophil elastase and proteinase 3. PubMed:28716864

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Cell Ontology (CL)
neutrophil
MeSH
Serum
MeSH
Malaria
Text Location
Discussion

p(HGNC:SERPINA1) decreases path(MESH:Inflammation) View Subject | View Object

However A1AT has broader functions [26, 27], abrogating inflammation via both enzyme-inhibitory and noninhibitory mechanisms [47]. PubMed:28716864

Appears in Networks:
Annotations
Cell Ontology (CL)
neutrophil
MeSH
Serum
MeSH
Malaria
Text Location
Discussion

p(HGNC:SERPINA1) decreases p(PFAM:"Pkinase_C", pmod(Ph)) View Subject | View Object

Along with this, A1AT inhibited hemin to induce PKC phosphorylation, which is an essential step for the production of ROS [9]. PubMed:28716864

Appears in Networks:
Annotations
Cell Ontology (CL)
neutrophil
MeSH
Serum
MeSH
Malaria
Text Location
Discussion

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.