PortalPublikationenMetalloporphyrins inactivate caspase-3 and -8.

Metalloporphyrins inactivate caspase-3 and -8.

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Metalloporphyrins inactivate caspase-3 and -8. / Blumenthal, Signe B; Kiemer, Alexandra K; Tiegs, Gisa; Seyfried, Stefan; Höltje, Monika; Brandt, Birte; Höltje, Hans-Dieter; Zahler, Stefan; Vollmar, Angelika M.

in: FASEB J, Jahrgang 19, Nr. 10, 10, 2005, S. 1272-1279.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Blumenthal, SB, Kiemer, AK, Tiegs, G, Seyfried, S, Höltje, M, Brandt, B, Höltje, H-D, Zahler, S & Vollmar, AM 2005, 'Metalloporphyrins inactivate caspase-3 and -8.', FASEB J, Jg. 19, Nr. 10, 10, S. 1272-1279. <http://www.ncbi.nlm.nih.gov/pubmed/16051694?dopt=Citation>

APA

Blumenthal, S. B., Kiemer, A. K., Tiegs, G., Seyfried, S., Höltje, M., Brandt, B., Höltje, H-D., Zahler, S., & Vollmar, A. M. (2005). Metalloporphyrins inactivate caspase-3 and -8. FASEB J, 19(10), 1272-1279. [10]. http://www.ncbi.nlm.nih.gov/pubmed/16051694?dopt=Citation

Vancouver

Blumenthal SB, Kiemer AK, Tiegs G, Seyfried S, Höltje M, Brandt B et al. Metalloporphyrins inactivate caspase-3 and -8. FASEB J. 2005;19(10):1272-1279. 10.

Bibtex

@article{60b74de7853f42cdbe6fde6705d0bc71,
title = "Metalloporphyrins inactivate caspase-3 and -8.",
abstract = "Activation of caspases represents one of the earliest biochemical indicators for apoptotic cell death. Therefore, measurement of caspase activity is a widely used and generally accepted method to determine apoptosis in a wide range of in vivo and in vitro settings. Numerous publications characterize the role of the heme-catabolizing enzyme heme oxygenase-1 (HO-1) in regulating apoptotic processes. Different metalloporphyrins representing inducers and inhibitors of this enzyme are often used, followed by assessment of apoptotic cell death. In the present work, we found that caspase-3-like activity, as well as activity of caspase-8 measured in either Fas (CD95) ligand-treated Jurkat T-lymphocytes or by the use of recombinant caspase-3 or -8, was inhibited by different metalloporphyrins (cobalt(III) protoporphyrin IX, tin and zinc(II) protoporphyrin-IX). Moreover, employing the mouse model of Fas-induced liver apoptosis these properties of porphyrins could also be demonstrated in vivo. The metalloporphyrins were shown to inhibit caspase-3-mediated PARP cleavage. Molecular modeling studies demonstrated that porphyrins can occupy the active site of caspase-3 in an energetically favorable manner and in a binding mode similar to that of known inhibitors. The data shown here introduce metalloporphyrins as direct inhibitors of caspase activity. This finding points to the need for careful employment of metalloporphyrins as modulators of HO-1.",
keywords = "Animals, Humans, Mice, Mice, Inbred BALB C, Apoptosis, Models, Molecular, Jurkat Cells, Caspase 3, Caspase 8, Caspases/*antagonists & inhibitors/chemistry/metabolism, Enzyme Inhibitors/*pharmacology, Fas Ligand Protein, Heme Oxygenase-1/*physiology, Membrane Glycoproteins/pharmacology, Metalloporphyrins/*pharmacology, Poly(ADP-ribose) Polymerases/metabolism, Tumor Necrosis Factors/pharmacology, Animals, Humans, Mice, Mice, Inbred BALB C, Apoptosis, Models, Molecular, Jurkat Cells, Caspase 3, Caspase 8, Caspases/*antagonists & inhibitors/chemistry/metabolism, Enzyme Inhibitors/*pharmacology, Fas Ligand Protein, Heme Oxygenase-1/*physiology, Membrane Glycoproteins/pharmacology, Metalloporphyrins/*pharmacology, Poly(ADP-ribose) Polymerases/metabolism, Tumor Necrosis Factors/pharmacology",
author = "Blumenthal, {Signe B} and Kiemer, {Alexandra K} and Gisa Tiegs and Stefan Seyfried and Monika H{\"o}ltje and Birte Brandt and Hans-Dieter H{\"o}ltje and Stefan Zahler and Vollmar, {Angelika M}",
year = "2005",
language = "English",
volume = "19",
pages = "1272--1279",
journal = "FASEB J",
issn = "0892-6638",
publisher = "FASEB",
number = "10",

}

RIS

TY - JOUR

T1 - Metalloporphyrins inactivate caspase-3 and -8.

AU - Blumenthal, Signe B

AU - Kiemer, Alexandra K

AU - Tiegs, Gisa

AU - Seyfried, Stefan

AU - Höltje, Monika

AU - Brandt, Birte

AU - Höltje, Hans-Dieter

AU - Zahler, Stefan

AU - Vollmar, Angelika M

PY - 2005

Y1 - 2005

N2 - Activation of caspases represents one of the earliest biochemical indicators for apoptotic cell death. Therefore, measurement of caspase activity is a widely used and generally accepted method to determine apoptosis in a wide range of in vivo and in vitro settings. Numerous publications characterize the role of the heme-catabolizing enzyme heme oxygenase-1 (HO-1) in regulating apoptotic processes. Different metalloporphyrins representing inducers and inhibitors of this enzyme are often used, followed by assessment of apoptotic cell death. In the present work, we found that caspase-3-like activity, as well as activity of caspase-8 measured in either Fas (CD95) ligand-treated Jurkat T-lymphocytes or by the use of recombinant caspase-3 or -8, was inhibited by different metalloporphyrins (cobalt(III) protoporphyrin IX, tin and zinc(II) protoporphyrin-IX). Moreover, employing the mouse model of Fas-induced liver apoptosis these properties of porphyrins could also be demonstrated in vivo. The metalloporphyrins were shown to inhibit caspase-3-mediated PARP cleavage. Molecular modeling studies demonstrated that porphyrins can occupy the active site of caspase-3 in an energetically favorable manner and in a binding mode similar to that of known inhibitors. The data shown here introduce metalloporphyrins as direct inhibitors of caspase activity. This finding points to the need for careful employment of metalloporphyrins as modulators of HO-1.

AB - Activation of caspases represents one of the earliest biochemical indicators for apoptotic cell death. Therefore, measurement of caspase activity is a widely used and generally accepted method to determine apoptosis in a wide range of in vivo and in vitro settings. Numerous publications characterize the role of the heme-catabolizing enzyme heme oxygenase-1 (HO-1) in regulating apoptotic processes. Different metalloporphyrins representing inducers and inhibitors of this enzyme are often used, followed by assessment of apoptotic cell death. In the present work, we found that caspase-3-like activity, as well as activity of caspase-8 measured in either Fas (CD95) ligand-treated Jurkat T-lymphocytes or by the use of recombinant caspase-3 or -8, was inhibited by different metalloporphyrins (cobalt(III) protoporphyrin IX, tin and zinc(II) protoporphyrin-IX). Moreover, employing the mouse model of Fas-induced liver apoptosis these properties of porphyrins could also be demonstrated in vivo. The metalloporphyrins were shown to inhibit caspase-3-mediated PARP cleavage. Molecular modeling studies demonstrated that porphyrins can occupy the active site of caspase-3 in an energetically favorable manner and in a binding mode similar to that of known inhibitors. The data shown here introduce metalloporphyrins as direct inhibitors of caspase activity. This finding points to the need for careful employment of metalloporphyrins as modulators of HO-1.

KW - Animals

KW - Humans

KW - Mice

KW - Mice, Inbred BALB C

KW - Apoptosis

KW - Models, Molecular

KW - Jurkat Cells

KW - Caspase 3

KW - Caspase 8

KW - Caspases/antagonists & inhibitors/chemistry/metabolism

KW - Enzyme Inhibitors/pharmacology

KW - Fas Ligand Protein

KW - Heme Oxygenase-1/physiology

KW - Membrane Glycoproteins/pharmacology

KW - Metalloporphyrins/pharmacology

KW - Poly(ADP-ribose) Polymerases/metabolism

KW - Tumor Necrosis Factors/pharmacology

KW - Animals

KW - Humans

KW - Mice

KW - Mice, Inbred BALB C

KW - Apoptosis

KW - Models, Molecular

KW - Jurkat Cells

KW - Caspase 3

KW - Caspase 8

KW - Caspases/antagonists & inhibitors/chemistry/metabolism

KW - Enzyme Inhibitors/pharmacology

KW - Fas Ligand Protein

KW - Heme Oxygenase-1/physiology

KW - Membrane Glycoproteins/pharmacology

KW - Metalloporphyrins/pharmacology

KW - Poly(ADP-ribose) Polymerases/metabolism

KW - Tumor Necrosis Factors/pharmacology

M3 - SCORING: Journal article

VL - 19

SP - 1272

EP - 1279

JO - FASEB J

JF - FASEB J

SN - 0892-6638

IS - 10

M1 - 10

ER -