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Wyszukujesz frazę "heme" wg kryterium: Temat


Wyświetlanie 1-11 z 11
Tytuł:
Heme oxygenase-1 expression in disease states.
Autorzy:
Deshane, Jessy
Wright, Marcienne
Agarwal, Anupam
Powiązania:
https://bibliotekanauki.pl/articles/1041399.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
heme oxygenase-1
heme
cytoprotection
polymorphisms
disease
Opis:
Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase. The biological effects exerted by the products of this enzymatic reaction have gained much attention. The anti-oxidant, anti-inflammatory and cytoprotective functions associated with HO-1 are attributable to one or more of its degradation products. Induction of HO-1 occurs as an adaptive and beneficial response to several injurious stimuli including heme and this inducible nature of HO-1 signifies its importance in several pathophysiological disease states. The beneficial role of HO-1 has been implicated in several clinically relevant disease states involving multiple organ systems as well as significant biological processes such as ischemia-reperfusion injury, inflammation/immune dysfunction and transplantation. HO-1 has thus emerged as a key target molecule with therapeutic implications.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 273-284
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis.
Autorzy:
Simpson, Waltena
Olczak, Teresa
Genco, Caroline
Powiązania:
https://bibliotekanauki.pl/articles/1043355.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Kgp
heme
Porphyromonas gingivalis
HmuR
gingipain
Opis:
We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological significance of the HmuR-Kgp complex in heme utilization in P. gingivalis through the construction and characterization of a defined kgp mutant and a hmuR kgp double mutant in P. gingivalis A7436. The P. gingivalis kgp mutant exhibited a decreased ability to bind both hemin and hemoglobin. Growth of this strain with hemoglobin was delayed and its ability to utilize hemin as a sole iron source was diminished as compared to the wild type strain. Inactivation of both the hmuR and kgp genes resulted in further decreased ability of P. gingivalis to bind hemoglobin and hemin, as well as diminished ability to utilize either hemin or hemoglobin as a sole iron source. Collectively, these in vivo results further confirmed that both HmuR and Kgp are involved in the utilization of hemin and hemoglobin in P. gingivalis A7436.
Źródło:
Acta Biochimica Polonica; 2004, 51, 1; 253-262
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Evaluation of the activity of thermostable DNA polymerases in the presence of heme, as a key inhibitor in the real time PCR method in diagnostics of sepsis
Autorzy:
Gosiewski, Tomasz
Brzychczy-Włoch, Monika
Pietrzyk, Agata
Sroka, Agnieszka
Bulanda, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/1039451.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
polymerase inhibitor
heme
real time PCR
sepsis
Opis:
The study aim was evaluation of the usefulness of several thermostable DNA polymerases in real time PCR conducted in the presence of the heme. Our study had the advantage of testing several different polymerases, one of which proved to be the least sensitive to heme activity. We also found that there is no need of supplementing the reaction mixture with protective substances like BSA. Selection of the appropriate polymerase can increase the efficiency of the PCR reaction which is very important for diagnosis of sepsis and for other analyses performed on DNA template isolated from the blood.
Źródło:
Acta Biochimica Polonica; 2013, 60, 4; 603-606
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Heme iron in meat as the main source of iron in the human diet
Autorzy:
Buzala, M.
Slomka, A.
Janicki, B.
Powiązania:
https://bibliotekanauki.pl/articles/1189787.pdf
Data publikacji:
2016
Wydawca:
Uniwersytet Warmińsko-Mazurski w Olsztynie / Polskie Towarzystwo Magnezologiczne im. Prof. Juliana Aleksandrowicza
Tematy:
heme iron
iron
meat
iron source
human diet
human nutrition
Opis:
Iron is a trace element involved in many cardinal metabolic processes of almost all living organisms. It is well known that iron participates in oxygen transport as well as it is a cofactor in many fundamental enzymatic and nonenzymatic processes. Accordingly, disturbances of iron homeostasis can cause serious clinical consequences. In humans, dietary iron can enter the body in two main forms: heme and nonheme. The former is a component of many hemoproteins (including myoglobin, hemoglobin, cytochromes b and c) and is easily absorbed in the duodenal enterocytes. Red meat is an excellent source of heme iron, while the less bioavailable nonheme form is found in large amounts in milk products and vegetables. For this reason, consumers of meat have a better iron status than vegetarians and vegans. The aim of this paper was to discuss the role of heme iron in the human diet. Heme iron found in muscle protein should be supplied to humans to prevent iron deficiency, which can lead to anemia. It is easily absorbed by the human body and its main source is red meat. In addition, heme iron, which is mainly found in myoglobin in meat, contributes to the desirable bright red color and to the most undesirable brown color of meat. Both heme and nonheme iron are catalysts of lipid oxidation in meat. This process lowers the nutritive value through oxidation of polyunsaturated fatty acids, which produces an undesirable flavor and aroma. The present review is focused on the role of heme iron, which is mainly found in meat and is the principal source of iron in the human diet.
Źródło:
Journal of Elementology; 2016, 21, 1; 303-314
1644-2296
Pojawia się w:
Journal of Elementology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Heme iron in meat as the main source of iron in the human diet
Autorzy:
Buzala, M.
Slomka, A.
Janicki, B.
Powiązania:
https://bibliotekanauki.pl/articles/962737.pdf
Data publikacji:
2016
Wydawca:
Uniwersytet Warmińsko-Mazurski w Olsztynie / Polskie Towarzystwo Magnezologiczne im. Prof. Juliana Aleksandrowicza
Tematy:
heme iron
iron
meat
iron source
human diet
human nutrition
Opis:
Iron is a trace element involved in many cardinal metabolic processes of almost all living organisms. It is well known that iron participates in oxygen transport as well as it is a cofactor in many fundamental enzymatic and nonenzymatic processes. Accordingly, disturbances of iron homeostasis can cause serious clinical consequences. In humans, dietary iron can enter the body in two main forms: heme and nonheme. The former is a component of many hemoproteins (including myoglobin, hemoglobin, cytochromes b and c) and is easily absorbed in the duodenal enterocytes. Red meat is an excellent source of heme iron, while the less bioavailable nonheme form is found in large amounts in milk products and vegetables. For this reason, consumers of meat have a better iron status than vegetarians and vegans. The aim of this paper was to discuss the role of heme iron in the human diet. Heme iron found in muscle protein should be supplied to humans to prevent iron deficiency, which can lead to anemia. It is easily absorbed by the human body and its main source is red meat. In addition, heme iron, which is mainly found in myoglobin in meat, contributes to the desirable bright red color and to the most undesirable brown color of meat. Both heme and nonheme iron are catalysts of lipid oxidation in meat. This process lowers the nutritive value through oxidation of polyunsaturated fatty acids, which produces an undesirable flavor and aroma. The present review is focused on the role of heme iron, which is mainly found in meat and is the principal source of iron in the human diet.
Źródło:
Journal of Elementology; 2016, 21, 1
1644-2296
Pojawia się w:
Journal of Elementology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effects of protoporphyrins on production of nitric oxide and expression of vascular endothelial growth factor in vascular smooth muscle cells and macrophages.
Autorzy:
Józkowicz, Alicja
Dulak, Józef
Powiązania:
https://bibliotekanauki.pl/articles/1043649.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cell viability
metalloporphyrins
vascular endothelial growth factor
nitric oxide
heme oxygenase
Opis:
Heme oxygenase-1 (HO-1), an inducible enzyme degrading heme to biliverdin, iron and carbon monoxide, is involved in regulation of inflammation and angiogenesis. Tin protoporphyrin (SnPPIX) and zinc protoporphyrin (ZnPPIX) are commonly used as competitive inhibitors of HO-1. We aimed to compare the effects of SnPPIX and ZnPPIX on the production of vascular endothelial growth factor (VEGF), activity of inducible nitric oxide synthase (iNOS) and cell viability. All experiments were performed on rat vascular smooth muscle cells and murine RAW264.7 macrophages treated with 3-10 μM protoporphyrins. Some cells were additionally stimulated with IL-1β or with lipopolysaccharide. After a 24 h incubation period SnPPIX and ZnPPIX significantly reduced the generation of VEGF in vascular smooth muscle cells and RAW264.7, both in resting and stimulated cells. The inhibitory potentials of both protoporphyrins on VEGF synthesis were very similar. In contrast, analysis of iNOS activity revealed that results obtained with different HO-1 inhibitors are discrepant. Generation of nitric oxide by iNOS was significantly increased by SnPPIX but strongly decreased by ZnPPIX. Similar differences were observed when cell viability was compared. SnPPIX improved the cell survival rate, whereas the same doses of ZnPPIX exerted some cytotoxic effects. In summary, SnPPIX and ZnPPIX can be used as HO-1 inhibitors in some experimental models. However, these compounds produce also HO-independent effects, which can make the interpretation of experiments very uncertain. Thus the involvement of the HO-1 pathway should be always confirmed by more specific methods.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 69-79
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Hem12, an enzyme of heme biosynthesis pathway, is monoubiquitinated by Rsp5 ubiquitin ligase in yeast cells
Autorzy:
Chelstowska, Anna
Jastrzebska, Zaneta
Kaminska, Joanna
Sadurska, Anna
Plochocka, Danuta
Rytka, Joanna
Zoladek, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1038993.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
yeast
heme biosynthesis
Hem12
ubiquitination
Rsp5 ligase
protein degradation
Opis:
Heme biosynthesis pathway is conserved in yeast and humans and hem12 yeast mutants mimic porphyria cutanea tarda (PCT), a hereditary human disease caused by mutations in the UROD gene. Even though mutations in other genes also affect UROD activity and predispose to sporadic PCT, the regulation of UROD is unknown. Here, we used yeast as a model to study regulation of Hem12 by ubiquitination and involvement of Rsp5 ubiquitin ligase in this process. We found that Hem12 is monoubiquitinated in vivo by Rsp5. Hem12 contains three conserved lysine residues located on the protein surface that can potentially be ubiquitinated and lysine K8 is close to the 36-LPEY-39 (PY) motif which binds WW domains of the Rsp5 ligase. The hem12-K8A mutation results in a defect in cell growth on a glycerol medium at 38°C but it does not affect the level of Hem12. The hem12-L36A,P37A mutations which destroy the PY motif result in a more profound growth defect on both, glycerol and glucose-containing media. However, after several passages on the glucose medium, the hem12-L36A,P37A cells adapt to the growth medium owing to higher expression of hem12-L36A,P37A gene and higher stability of the mutant Hem12-L36A,P37A protein. The Hem12 protein is downregulated upon heat stress in a Rsp5-independent way. Thus, Rsp5-dependent Hem12 monoubiquitination is important for its functioning, but not required for its degradation. Since Rsp5 has homologs among the Nedd4 family of ubiquitin ligases in humans, a similar regulation by ubiquitination might be also important for functioning of the human UROD.
Źródło:
Acta Biochimica Polonica; 2015, 62, 3; 509-515
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Pharmacological versus genetic inhibition of heme oxygenase-1 - the comparison of metalloporphyrins, shRNA and CRISPR/Cas9 system
Autorzy:
Mucha, Olga
Podkalicka, Paulina
Czarnek, Maria
Biela, Anna
Mieczkowski, Mateusz
Kachamakova-Trojanowska, Neli
Stepniewski, Jacek
Jozkowicz, Alicja
Dulak, Jozef
Loboda, Agnieszka
Powiązania:
https://bibliotekanauki.pl/articles/1038402.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
CRISPR/Cas9
shRNA
inhibitors
heme oxygenase-1
HO-1
off-target
Opis:
Inhibition of heme oxygenase-1 (HO-1, encoded by HMOX1), a cytoprotective, anti-apoptotic and anti-inflammatory enzyme, may serve as a valuable therapy in various pathophysiological processes, including tumorigenesis. We compared the effect of chemical inhibitors - metalloporphyrins, with genetic tools - shRNA and CRISPR/Cas9 systems, to knock-down (KD)/knock-out (KO) HO-1 expression/activity. 293T cells were incubated with metalloporphyrins, tin and zinc protoporphyrins (SnPPIX and ZnPPIX, respectively) or were either transduced with lentiviral vectors encoding different shRNA sequences against HO-1 or were modified by CRISPR/Cas9 system targeting HMOX1. Metalloporphyrins decreased HO activity but concomitantly strongly induced HO-1 mRNA and protein in 293T cells. On the other hand, only slight basal HO-1 inhibition in shRNA KD 293T cell lines was confirmed on mRNA and protein level with no significant effect on enzyme activity. Nevertheless, silencing effect was much stronger when CRISPR/Cas9-mediated knock-out was performed. Most of the clones harboring mutations within HMOX1 locus did not express HO-1 protein and failed to increase bilirubin concentration after hemin stimulation. Furthermore, CRISPR/Cas9-mediated HO-1 depletion decreased 293T viability, growth, clonogenic potential and increased sensitivity to H2O2 treatment. In summary, we have shown that not all technologies can be used for inhibition of HO activity in vitro with the same efficiency. In our hands, the most potent and comprehensible results can be obtained using genetic tools, especially CRISPR/Cas9 approach.
Źródło:
Acta Biochimica Polonica; 2018, 65, 2; 277-286
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
HIF-1: the knowns and unknowns of hypoxia sensing.
Autorzy:
Zagórska, Anna
Dulak, Józef
Powiązania:
https://bibliotekanauki.pl/articles/1041533.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
angiogenesis
prolyl and asparaginyl hydroxylases
hypoxia inducible factor-1
carbon monoxide
reactive oxygen species
nitric oxide
heme oxygenase
Opis:
Hypoxia-inducible factor-1 (HIF-1) is a transcriptional activator that functions as a master regulator of cellular and systemic oxygen homeostasis. It consists of two constitutively produced subunits: HIF-1α and HIF-1β. Under normoxic conditions HIF-1α undergoes hydroxylation at specific prolyl residues which leads to an immediate ubiquitination and subsequent proteasomal degradation of the α subunit. Additionally, hydroxylation of an asparaginyl residue blocks the transcriptional activity of HIF-1 due to inhibition of its interaction with co-activators. In contrast, under hypoxic conditions, abolition of prolyl hydroxylation results in HIF-1α stabilization, whereas the lack of asparaginyl hydroxylation allows the transcriptional activity. Additionally, the transcriptional activity may be modulated by phosphorylation or redox modification of HIF-1. Despite its name, HIF-1 is induced not only in response to reduced oxygen availability but also by other stimulants, such as nitric oxide, various growth factors, or direct inhibitors of prolyl and asparaginyl hydroxylases. Therefore, it seems to be a crucial transcription factor elicited by a wide range of stresses such as impaired oxygenation, inflammation, energy deprivation, or intensive proliferation. However, the mechanisms of normoxic activation, as well as of oxygen sensing, are not yet fully known. Further understanding of the processes that control HIF-1 activity will be crucial for the development of new diagnostic and therapeutic strategies.
Źródło:
Acta Biochimica Polonica; 2004, 51, 3; 563-585
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Adult stem cells: hopes and hypes of regenerative medicine
Autorzy:
Dulak, Józef
Szade, Krzysztof
Szade, Agata
Nowak, Witold
Józkowicz, Alicja
Powiązania:
https://bibliotekanauki.pl/articles/1038957.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
embryonic stem cells
induced pluripotent stem cells
myocardial infarction
very small embryonic-like stem cells
heme oxygenase-1
Opis:
Stem cells are self-renewing cells that can differentiate into specialized cell type(s). Pluripotent stem cells, i.e. embryonic stem cells (ESC) or induced pluripotent stem cells (iPSC) differentiate into cells of all three embryonic lineages. Multipotent stem cells, like hematopoietic stem cells (HSC), can develop into multiple specialized cells in a specific tissue. Unipotent cells differentiate only into one cell type, like e.g. satellite cells of skeletal muscle. There are many examples of successful clinical applications of stem cells. Over million patients worldwide have benefited from bone marrow transplantations performed for treatment of leukemias, anemias or immunodeficiencies. Skin stem cells are used to heal severe burns, while limbal stem cells can regenerate the damaged cornea. Pluripotent stem cells, especially the patient-specific iPSC, have a tremendous therapeutic potential, but their clinical application will require overcoming numerous drawbacks. Therefore, the use of adult stem cells, which are multipotent or unipotent, can be at present a more achievable strategy. Noteworthy, some studies ascribed particular adult stem cells as pluripotent. However, despite efforts, the postulated pluripotency of such events like "spore-like cells", "very small embryonic-like stem cells" or "multipotent adult progenitor cells" have not been confirmed in stringent independent studies. Also plasticity of the bone marrow-derived cells which were suggested to differentiate e.g. into cardiomyocytes, has not been positively verified, and their therapeutic effect, if observed, results rather from the paracrine activity. Here we discuss the examples of recent studies on adult stem cells in the light of current understanding of stem cell biology.
Źródło:
Acta Biochimica Polonica; 2015, 62, 3; 329-337
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Therapeutic potential of heme oxygenase-1 in cardiovascular disease
Autorzy:
Jazwa, A.
Florczyk, U.
Stepniewski, J.
Jozkowicz, A.
Dulak, J.
Powiązania:
https://bibliotekanauki.pl/articles/80176.pdf
Data publikacji:
2011
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
angiogenesis
angiogenic factor
antiapoptotic effect
antiinflammatory effect
antioxidant effect
carbon monoxide
cardiovascular disease
cytoprotection
endothelial cell
ferrous iron
heme oxygenase-1
hypoxia
iron
stem cell
stromal cell
therapeutic potential
vascular endothelial growth factor-A
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2011, 92, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-11 z 11

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