Protein Information

Name catalase
Synonyms CAT; Catalase; Erythrocyte derived growth promoting factor; Carnitine O acetyltransferase; Carnitine acetylase; Carnitine acetyltransferase; CAT; Catalases…

Compound Information

Name acrolein
CAS 2-propenal

Reference List

PubMed Abstract RScore(About this table)
7728738 Subramaniam S, Subramaniam S, Shyamala Devi CS: Erythrocyte antioxidant enzyme activity in CMF treated breast cancer patients. Cancer Biochem Biophys. 1994 Oct;14(3):177-82.

Acrolein and phosphoramide mustard are the metabolites of cyclophosphamide which are among the causative agents which reduce the activity of superoxide dismultase, catalase, glutathione peroxidase, glutathione reductase, glutathione-S-transferase and glucose-6-phosphate dehydrogenase in erythrocytes of CMF treated breast cancer patients.
81(1,1,1,1) Details
19596284 Roy J, Pallepati P, Bettaieb A, Tanel A, Averill-Bates DA: Acrolein induces a cellular stress response and triggers mitochondrial apoptosis in A549 cells. Chem Biol Interact. 2009 Oct 7;181(2):154-67. Epub 2009 Jul 9.

Inhibition by the antioxidants catalase, polyethylene glycol-catalase, sodium pyruvate and MnTBAP showed that acrolein-induced reactive oxygen species were responsible for mitochondrial membrane hyperpolarisation.
62(0,2,2,2) Details
9567773 Arumugam N, Sivakumar V, Thanislass J, Devaraj H: Effects of acrolein on rat liver antioxidant defense system. Indian J Exp Biol. 1997 Dec;35(12):1373-4.

Following 45 days of acrolein exposure, the levels of glutathione, ascorbic acid and the activity of catalase were decreased whereas the activities of superoxide dismutase and glutathione peroxidase were increased.
6(0,0,1,1) Details
18501200 Ansari MA, Roberts KN, Scheff SW: Oxidative stress and modification of synaptic proteins in hippocampus after traumatic brain injury. Free Radic Biol Med. 2008 Aug 15;45(4):443-52. Epub 2008 May 3.

At various times post-TBI, animals were killed and the hippocampus was analyzed for antioxidants (GSH, GSSG, glutathione peroxidase, glutathione reductase, glutathione-S-transferase, glucose-6-phosphate dehydrogenase, superoxide dismutase, and catalase) and oxidants (acrolein, 4-hydroxynonenal, protein carbonyl, and 3-nitrotyrosine).
6(0,0,1,1) Details
18607771 Zhu H, Jia Z, Strobl JS, Ehrich M, Misra HP, Li Y: Potent induction of total cellular and mitochondrial antioxidants and phase 2 enzymes by cruciferous sulforaphane in rat aortic smooth muscle cells: cytoprotection against oxidative and electrophilic stress. Cardiovasc Toxicol. 2008 Fall;8(3):115-25. Epub 2008 Jul 8.

Here we report that incubation of rat aortic smooth muscle A10 cells with sulforaphane (0.25-5 microM) resulted in concentration-dependent induction of a spectrum of important cellular antioxidants and phase 2 enzymes, including superoxide dismutase (SOD), catalase, the reduced form of glutathione (GSH), glutathione peroxidase, glutathione reductase (GR), glutathione S-transferase (GST), and NAD (P) H:quinone oxidoreductase 1 (NQO1).
Pretreatment with sulforaphane (0.5, 1, and 5 microM) protected aortic smooth muscle cells from oxidative and electrophilic cytotoxicity induced by xanthine oxidase (XO)/xanthine, H2O2, SIN-1-derived peroxynitrite, 4-hydroxy-2-nonenal, and acrolein.
3(0,0,0,3) Details
19032949 Yoshida M, Tomitori H, Machi Y, Hagihara M, Higashi K, Goda H, Ohya T, Niitsu M, Kashiwagi K, Igarashi K: Acrolein toxicity: Comparison with reactive oxygen species. Biochem Biophys Res Commun. 2009 Jan 9;378(2):313-8. Epub 2008 Nov 24.

Toxicity of H (2) O (2) was prevented by glutathione peroxidase plus N-acetyl-l-cysteine, pyruvate, catalase, and reduced by polyphenol, and toxicity of () OH was prevented by glutathione peroxidase plus N-acetyl-l-cysteine, pyruvate, catalase and reduced by N-acetyl-l-cysteine.
1(0,0,0,1) Details
8430435 Awasthi S, Boor PJ: Semicarbazide protection from in vivo oxidant injury of vascular tissue by allylamine. Toxicol Lett. 1993 Feb;66(2):157-63.

Previous studies showed that allylamine-induced chronic lesions are markedly reduced by semicarbazide, an inhibitor of semicarbazide-sensitive amine oxidase (SSAO), and that allylamine is metabolized to the aldehyde, acrolein, by SSAO.
Aorta, epicardium, and endocardium were assayed for SSAO, glutathione peroxidase, catalase, thiol status and lipid peroxidation.
1(0,0,0,1) Details
18367636 Zhu H, Jia Z, Zhang L, Yamamoto M, Misra HP, Trush MA, Li Y: Antioxidants and phase 2 enzymes in macrophages: regulation by Nrf2 signaling and protection against oxidative and electrophilic stress. Exp Biol Med. 2008 Apr;233(4):463-74.

As compared with wild-type cells, Nrf2 (- /-) macrophages were much more susceptible to cell injury induced by reactive oxygen/nitrogen species, as well as two known macrophage toxins, acrolein and cadmium.
Incubation of wild-type macrophages with 3H-1,2-dithiole-3-thione (D3T) led to significant induction of various antioxidants and phase 2 enzymes, including catalase, glutathione, glutathione peroxidase (GPx), glutathione reductase, glutathione S-transferase, and NAD (P) H:quinone oxidoreductase 1.
1(0,0,0,1) Details
8721611 Agostinelli E, Przybytkowski E, Averill-Bates DA: Glucose, glutathione, and cellular response to spermine oxidation products. Free Radic Biol Med. 1996;20(5):649-56.

When catalase was present, cytotoxicity is attributed to spermine-derived aldehyde (s).
Glucose did not protect cells against cytotoxicity induced by spermine-derived aldehyde (s), nor by the aldehyde acrolein.
1(0,0,0,1) Details
9022075 Anderson MM, Hazen SL, Hsu FF, Heinecke JW: Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. J Clin Invest. 1997 Feb 1;99(3):424-32.

Aldehyde generation required neutrophil activation and a free hydroxy-amino acid; it was inhibited by catalase and heme poisons, implicating H202 and myeloperoxidase in the cellular reaction.
1(0,0,0,1) Details
8068243 Averill-Bates DA, Agostinelli E, Przybytkowski E, Mondovi B: Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells. Biochem Cell Biol. 1994 Jan-Feb;72(1-2):36-42.

It has been suggested that the dialdehyde produced during the oxidation of spermine subsequently undergoes spontaneous beta-elimination to form acrolein.
The inhibition patterns of NAD-dependent aldehyde dehydrogenase and catalase against cytotoxicity of bovine serum amine oxidase were determined in Chinese hamster ovary cells at 37 degrees C.
4(0,0,0,4) Details
7945412 Agostinelli E, Przybytkowski E, Mondovi B, Averill-Bates DA: Heat enhancement of cytotoxicity induced by oxidation products of spermine in Chinese hamster ovary cells. Biochem Pharmacol. 1994 Sep 15;48(6):1181-6.

Heat also increased the individual cytotoxicity of both exogenous H2O2 and the exogenous aldehyde acrolein.
The effect of temperature was especially marked in the presence of exogenous catalase.
3(0,0,0,3) Details
2842890 Ramos K, Grossman SL, Cox LR: Allylamine-induced vascular toxicity in vitro: prevention by semicarbazide-sensitive amine oxidase inhibitors. Toxicol Appl Pharmacol. 1988 Aug;95(1):61-71.

Single cell suspensions of VEC or SMC formed acrolein (ACR) when incubated in the presence of AAM.
The effect of catalase, a hydrogen peroxide scavenger, on AAM-induced cytotoxicity was also evaluated.
2(0,0,0,2) Details
16828947 Bhatia K, Kaur M, Atif F, Ali M, Rehman H, Rahman S, Raisuddin S: Aqueous extract of Trigonella foenum-graecum L. ameliorates additive urotoxicity of buthionine sulfoximine and cyclophosphamide in mice. Food Chem Toxicol. 2006 Oct;44(10):1744-50. Epub 2006 Jun 3.

Cyclophosphamide (CP) is a commonly used anti-cancer drug which causes toxicity by its reactive metabolites such as acrolein and phosphoramide mustard.
CP-treated animals exhibited a significant decrease in the activities of glutathione S-transferase (GST), glutathione reductase (GR), glutathione peroxidase (GP) and catalase (CAT) when compared to the controls.
1(0,0,0,1) Details
8784495 Johnson WC, Cluff CW, Goff WL, Wyatt CR: Reactive oxygen and nitrogen intermediates and products from polyamine degradation are Babesiacidal in vitro. Ann N Y Acad Sci. 1996 Jul 23;791:136-47.

Polyamines are degraded into acrolein which has also been shown to be toxic to Plasmodium spp.
The toxicity was partially reversed by the addition of the ROI scavenger catalase.
1(0,0,0,1) Details
10079053 Arumugam N, Sivakumar V, Thanislass J, Pillai KS, Devaraj SN, Devaraj H: Acute pulmonary toxicity of acrolein in rats--underlying mechanism. . Toxicol Lett. 1999 Feb 22;104(3):189-94.

The activities of catalase and glutathione peroxidase were reduced whereas an increase in the activities of superoxide dismutase was observed.
1(0,0,0,1) Details
12763045 Kwak MK, Kensler TW, Casero RA Jr: Induction of phase 2 enzymes by serum oxidized polyamines through activation of Nrf2: effect of the polyamine metabolite acrolein. Biochem Biophys Res Commun. 2003 Jun 6;305(3):662-70.

0(0,0,0,0) Details
11263996 Sharmin S, Sakata K, Kashiwagi K, Ueda S, Iwasaki S, Shirahata A, Igarashi K: Polyamine cytotoxicity in the presence of bovine serum amine oxidase. . Biochem Biophys Res Commun. 2001 Mar 23;282(1):228-35.


Amine oxidase in fetal calf serum produces aminodialdehyde generating acrolein spontaneously, H (2) O (2), and ammonia from spermine.
0(0,0,0,0) Details
2264722 Levitz SM, DiBenedetto DJ, Diamond RD: Inhibition and killing of fungi by the polyamine oxidase-polyamine system. Antonie Van Leeuwenhoek. 1990 Aug;58(2):107-14.


Two putative end products of the system, hydrogen peroxide and acrolein, both killed C. neoformans at concentrations attainable with the whole system.
0(0,0,0,0) Details