Scavenger System

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Gunnar Houen - One of the best experts on this subject based on the ideXlab platform.

  • large scale purification and characterization of non glycosylated gc globulin vitamin d binding protein from plasma fraction iv
    Biotechnology and Applied Biochemistry, 2006
    Co-Authors: Charlotte Svaerke Jorgensen, Maja Christiansen, Inga Laursen, Lisbeth B Krogsoe, Peter Hojrup, Lene Blou, Gunnar Houen
    Abstract:

    Gc globulin, also called vitamin D-binding protein, is a plasma protein involved in the extracellular actin-Scavenger System. Low levels of Gc globulin have been found to correlate with multiple organ failure and nonsurvival of patients with fulminant hepatic failure and trauma. Therefore substitution therapy with Gc globulin might be beneficial for such patients, increasing their chance of survival. In the present study, we describe a large-scale purification process for the production of a virus-safe human plasma-derived Gc globulin from Cohn fraction IV paste. The process includes three ion-exchange-chromatography steps, followed by a gel filtration, and two virus-reduction steps are implemented. The Gc globulin product was characterized with respect to purity, functional activity, glycosylation and, finally, with respect to content of endotoxin. From the results, it can be concluded that human Gc globulin purified from Cohn fraction IV is non-glycosylated. The purified Gc globulin is able to mask the presence of endotoxin by 20%.

  • gc globulin vitamin d binding protein levels an inhibition elisa assay for determination of the total concentration of gc globulin in plasma and serum
    Scandinavian Journal of Clinical & Laboratory Investigation, 2004
    Co-Authors: Charlotte Svaerke Jorgensen, Inga Laursen, Michael Christiansen, Bent Norgaardpedersen, E Ostergaard, F V Schiodt, Gunnar Houen
    Abstract:

    Gc globulin, also called vitamin D‐binding protein, is a plasma protein involved in the actin‐Scavenger System. In this study, the total Gc globulin concentration in serum or plasma samples was determined using a new, fast, solid‐phase inhibition assay. Included in the study were 228 healthy volunteers (131 M, 97 F), 22 pregnant women, 90 cancer patients and 9 patients with chronic liver disease. Moreover, the degree of complexing with actin was determined in selected samples using crossed immunoelectrophoresis. The Gc globulin level in healthy controls was in the range 176–623 mg/L, showing no age dependency. The median level was found to be significantly higher in women than in men. Gc globulin concentrations were raised during pregnancy, showing a median value of 541 mg/L in the first trimester, and slightly raised to 574 mg/L in the second trimester. Cancer patients showed no changes in Gc globulin level, and there was no sign of increased amounts of complexing with actin. Chronic liver patients showe...

Eero Kajantie - One of the best experts on this subject based on the ideXlab platform.

  • plasma heme Scavengers alpha l microglobulin and hemopexin as biomarkers in high risk pregnancies
    Frontiers in Physiology, 2019
    Co-Authors: Grigorios Kalapotharakos, Bo Åkerström, Katja Murtoniemi, Esa Hämäläinen, Eero Kajantie, Katri Räikkönen, Pia M Villa
    Abstract:

    Women with established preeclampsia (PE) have increased plasma concentration of free fetal hemoglobin. We measured two hemoglobin Scavenger System proteins, hemopexin (Hpx) and alpha-1-microglobulin (A1M) in maternal plasma using enzyme-linked immunosorbent assay during the late second trimester of pregnancy in women with high and low risk of developing PE. In total 142 women were included in nested case-control study: 42 women diagnosed with PE and 100 controls (49 randomly selected high-risk and 51 low-risk controls). The concentration of plasma A1M in high-risk controls was higher compared to low-risk controls. Women with severe PE had higher plasma A1M levels compared to women with non-severe PE. In conclusion, the concentration of plasma A1M is increased in the late second trimester in high-risk controls, suggesting activation of endogenous protective System against oxidative stress.

  • Table_1_Plasma Heme Scavengers Alpha-1-Microglobulin and Hemopexin as Biomarkers in High-Risk Pregnancies.docx
    2019
    Co-Authors: Grigorios Kalapotharakos, Bo Åkerström, Katja Murtoniemi, Esa Hämäläinen, Eero Kajantie, Katri Räikkönen, Pia Villa, Hannele Laivuori, Stefan R Hansson
    Abstract:

    Women with established preeclampsia (PE) have increased plasma concentration of free fetal hemoglobin. We measured two hemoglobin Scavenger System proteins, hemopexin (Hpx) and alpha-1-microglobulin (A1M) in maternal plasma using enzyme-linked immunosorbent assay during the late second trimester of pregnancy in women with high and low risk of developing PE. In total 142 women were included in nested case-control study: 42 women diagnosed with PE and 100 controls (49 randomly selected high-risk and 51 low-risk controls). The concentration of plasma A1M in high-risk controls was higher compared to low-risk controls. Women with severe PE had higher plasma A1M levels compared to women with non-severe PE. In conclusion, the concentration of plasma A1M is increased in the late second trimester in high-risk controls, suggesting activation of endogenous protective System against oxidative stress.

Charlotte Svaerke Jorgensen - One of the best experts on this subject based on the ideXlab platform.

  • large scale purification and characterization of non glycosylated gc globulin vitamin d binding protein from plasma fraction iv
    Biotechnology and Applied Biochemistry, 2006
    Co-Authors: Charlotte Svaerke Jorgensen, Maja Christiansen, Inga Laursen, Lisbeth B Krogsoe, Peter Hojrup, Lene Blou, Gunnar Houen
    Abstract:

    Gc globulin, also called vitamin D-binding protein, is a plasma protein involved in the extracellular actin-Scavenger System. Low levels of Gc globulin have been found to correlate with multiple organ failure and nonsurvival of patients with fulminant hepatic failure and trauma. Therefore substitution therapy with Gc globulin might be beneficial for such patients, increasing their chance of survival. In the present study, we describe a large-scale purification process for the production of a virus-safe human plasma-derived Gc globulin from Cohn fraction IV paste. The process includes three ion-exchange-chromatography steps, followed by a gel filtration, and two virus-reduction steps are implemented. The Gc globulin product was characterized with respect to purity, functional activity, glycosylation and, finally, with respect to content of endotoxin. From the results, it can be concluded that human Gc globulin purified from Cohn fraction IV is non-glycosylated. The purified Gc globulin is able to mask the presence of endotoxin by 20%.

  • gc globulin vitamin d binding protein levels an inhibition elisa assay for determination of the total concentration of gc globulin in plasma and serum
    Scandinavian Journal of Clinical & Laboratory Investigation, 2004
    Co-Authors: Charlotte Svaerke Jorgensen, Inga Laursen, Michael Christiansen, Bent Norgaardpedersen, E Ostergaard, F V Schiodt, Gunnar Houen
    Abstract:

    Gc globulin, also called vitamin D‐binding protein, is a plasma protein involved in the actin‐Scavenger System. In this study, the total Gc globulin concentration in serum or plasma samples was determined using a new, fast, solid‐phase inhibition assay. Included in the study were 228 healthy volunteers (131 M, 97 F), 22 pregnant women, 90 cancer patients and 9 patients with chronic liver disease. Moreover, the degree of complexing with actin was determined in selected samples using crossed immunoelectrophoresis. The Gc globulin level in healthy controls was in the range 176–623 mg/L, showing no age dependency. The median level was found to be significantly higher in women than in men. Gc globulin concentrations were raised during pregnancy, showing a median value of 541 mg/L in the first trimester, and slightly raised to 574 mg/L in the second trimester. Cancer patients showed no changes in Gc globulin level, and there was no sign of increased amounts of complexing with actin. Chronic liver patients showe...

Katja Murtoniemi - One of the best experts on this subject based on the ideXlab platform.

  • plasma heme Scavengers alpha l microglobulin and hemopexin as biomarkers in high risk pregnancies
    Frontiers in Physiology, 2019
    Co-Authors: Grigorios Kalapotharakos, Bo Åkerström, Katja Murtoniemi, Esa Hämäläinen, Eero Kajantie, Katri Räikkönen, Pia M Villa
    Abstract:

    Women with established preeclampsia (PE) have increased plasma concentration of free fetal hemoglobin. We measured two hemoglobin Scavenger System proteins, hemopexin (Hpx) and alpha-1-microglobulin (A1M) in maternal plasma using enzyme-linked immunosorbent assay during the late second trimester of pregnancy in women with high and low risk of developing PE. In total 142 women were included in nested case-control study: 42 women diagnosed with PE and 100 controls (49 randomly selected high-risk and 51 low-risk controls). The concentration of plasma A1M in high-risk controls was higher compared to low-risk controls. Women with severe PE had higher plasma A1M levels compared to women with non-severe PE. In conclusion, the concentration of plasma A1M is increased in the late second trimester in high-risk controls, suggesting activation of endogenous protective System against oxidative stress.

  • Table_1_Plasma Heme Scavengers Alpha-1-Microglobulin and Hemopexin as Biomarkers in High-Risk Pregnancies.docx
    2019
    Co-Authors: Grigorios Kalapotharakos, Bo Åkerström, Katja Murtoniemi, Esa Hämäläinen, Eero Kajantie, Katri Räikkönen, Pia Villa, Hannele Laivuori, Stefan R Hansson
    Abstract:

    Women with established preeclampsia (PE) have increased plasma concentration of free fetal hemoglobin. We measured two hemoglobin Scavenger System proteins, hemopexin (Hpx) and alpha-1-microglobulin (A1M) in maternal plasma using enzyme-linked immunosorbent assay during the late second trimester of pregnancy in women with high and low risk of developing PE. In total 142 women were included in nested case-control study: 42 women diagnosed with PE and 100 controls (49 randomly selected high-risk and 51 low-risk controls). The concentration of plasma A1M in high-risk controls was higher compared to low-risk controls. Women with severe PE had higher plasma A1M levels compared to women with non-severe PE. In conclusion, the concentration of plasma A1M is increased in the late second trimester in high-risk controls, suggesting activation of endogenous protective System against oxidative stress.

Roberto Dominguez - One of the best experts on this subject based on the ideXlab platform.

  • crystal structures of the vitamin d binding protein and its complex with actin structural basis of the actin Scavenger System
    Proceedings of the National Academy of Sciences of the United States of America, 2002
    Co-Authors: Ludovic R Otterbein, Christophe Cosio, Philip Graceffa, Roberto Dominguez
    Abstract:

    Actin is the most abundant protein in eukaryotic cells, but its release from cells into blood vessels can be lethal, being associated with clinical situations including hepatic necrosis and septic shock. A homeostatic mechanism, termed the actin-Scavenger System, is responsible for the depolymerization and removal of actin from the circulation. During the first phase of this mechanism, gelsolin severs the actin filaments. In the second phase, the vitamin D-binding protein (DBP) traps the actin monomers, which accelerates their clearance. We have determined the crystal structures of DBP by itself and complexed with actin to 2.1 A resolution. Similar to its homologue serum albumin, DBP consists of three related domains. Yet, in DBP a strikingly different organization of the domains gives rise to a large actin-binding cavity. After complex formation the three domains of DBP move slightly to "clamp" onto actin subdomain 3 and to a lesser extent subdomain 1. Contacts between actin and DBP throughout their extensive 3,454-A(2) intermolecular interface involve a mixture of hydrophobic, electrostatic, and solvent-mediated interactions. The area of actin covered by DBP within the complex approximately equals the sum of those covered by gelsolin and profilin. Moreover, certain interactions of DBP with actin mirror those observed in the actin-gelsolin complex, which may explain how DBP can compete effectively with gelsolin for actin binding. Formation of the strong actin-DBP complex proceeds with limited conformational changes to both proteins, demonstrating how DBP has evolved to become an effective actin-Scavenger protein.