Browse our Hemopexin Proteins (HPX)

Human Hemopexin (HPX) interaction partners

1. Data suggest that apo (show C9orf3 Proteins)-hemopexin isolated from plasma exchibits low endogenous levels of tyrosine nitration in the peptide YYCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and rat hemopexins; heme binding by hemopexin declined as tyrosine nitration proceeded in vitro.

2. There were significantly higher serum concentrations of fetal hemoglobin (show HBB Proteins) and alpha1-microglobulin and significantly lower first trimester serum concentrations of hemopexin in patients who later developed preeclampsia.

3. HPX is upregulated in non-small cell lung cancer patients compared to those with benign lung disease or no lung disease.

4. Plasma hemopexin levels were decreased or markedly decreased in patients with burns or sepsis and in premature infants.

5. Data show that HPX, POTEE and ApoA1 (show APOA1 Proteins) are deregulated in breast tumors suggesting un important role in breast tumorigenesis.

6. The Bach1 (show BACH1 Proteins)-dependent repression of the HO-1 (show HMOX1 Proteins) expression is under the control of the Hemopexin-dependent uptake of extracellular he

7. Hemopexin is overexpressed in the RPE (show RPE Proteins) of diabetic patients with DME and induces the breakdown of RPE (show RPE Proteins) cells in vitro.

8. activated hemopexin might be considered as a factor mediating ang II (show AGT Proteins) effects upon blood pressure by modulating AT1-R (show AGTR1 Proteins) availability

9. hemopexin will be neuroprotective after traumatic brain injury, with heme release in the CNS, and during the ensuing inflammation.

10. In sum, these data indicated that AKI-associated hepatic stress generates Hpx, which gains renal tubule access.

Cow (Bovine) Hemopexin (HPX) interaction partners

1. two glycoproteins, AHSG (show AHSG Proteins) and HPX, represent a pivotal glycoprotein of the cytoprotective activity for WN1316, showing a concrete evidence for the novel glycan-independent function of serum glycoproteins in neuroprotective drug efficacy.

Mouse (Murine) Hemopexin (HPX) interaction partners

1. this study shows that hemopexin counteracts systolic dysfunction induced by heme-driven oxidative stress

2. Hemopexin plays a novel protective role in alleviating heme-induced oxidative stress, improving inflammatory properties of high-density lipoprotein, macrophage phenotype and function, and inhibiting the development of atherosclerosis in apoE (show APOE Proteins)(-/-) mice.

3. This study demonstrated that Deletion of the hemopexin aggravates brain injury following stroma-free hemoglobin-induced intracerebral hemorrhage

4. In models for sepsis or burns, mean plasma hemopexin levels were increased above baseline.

5. The findings suggest that hemopexin can modulate the role of hemoglobin in sterile and infectious inflammation

6. results demonstrate that hemopexin decreases the accumulation and catabolism of exogenous hemin by neural cells. Its beneficial effect in stroke models is unlikely to be mediated by increased production of cytoprotective heme breakdown products

7. Hemopexin deficiency, which is often associated with sickle cell disease, may worsen outcome after intracerebral hemorrhage

8. haptoglobin (show HP Proteins) and hemopexin together are essential for protection from splenomegaly and liver fibrosis resulting from intravascular hemolysis

9. the importance of hemopexin in heme detoxification, thus suggesting that drugs mimicking hemopexin activity might be useful to prevent endothelial damage in patients suffering from hemolytic disorders.

10. hemopexin, by controlling heme-iron availability in lymphocytes, modulates responsiveness to IFN-gamma (show IFNG Proteins) and, hence, autoimmune responses

Rabbit Hemopexin (HPX) interaction partners

1. Data suggest that apo (show C9orf3 Proteins)-hemopexin isolated from plasma exchibits low endogenous levels of tyrosine nitration in the peptide YYCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and rat hemopexins; heme binding by hemopexin declined as tyrosine nitration proceeded in vitro.