The DOI matches its Crossref record.
The cytotoxic activity of hematoheme: Evidence for two different mechanisms
Abstract
Hematoheme displays a potent cytolytic activity toward erythrocytes either in the presence of hydrogen peroxide and a halide ion (system I) or in the presence of oxygen and a reducing agent (system II). In system I it resembles the cytotoxic activity of various peroxidases, whereas in system II it resembles the destructive activity of bleomycin and a variety of metal complexes. Both types of reactions presumably involve the generation of active oxygen species, which are responsible for the damaging effects. In a first attempt to compare the chemical mechanisms of the two types of reactions we used various traps and scavengers of active oxygen species. Tryptophan as well as tyrosine and uric acid were found to be potent inhibitors of the hematoheme-H2O2-halide reaction but do not significantly inhibit the hematoheme-O2-ascorbate reaction. Pyridine, on the other hand, inhibits the oxygen-mediated reaction, but does not affect the peroxide-halide-mediated activity. The cytolytic activity of photoactivated hematoporphyrin, which involves the generation of singlet oxygen, is activated by pyridine and is strongly inhibited by diphenylisobenzofuran. The latter compound is a weak activator of both hematoheme reactions. We conclude that the two hematoheme reactions proceed by two different mechanisms and probably generate different toxic intermediates. The results further suggest that the toxic intermediate generated by photoactivated hematoporphyrin (singlet oxygen) does not play a d…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Other eukaryotic cells do not undergo lysis in the presence of heme, although in vitro , endothelial cells are susceptible to heme toxicity by either the peroxidase-like or monooxygenase-like activities of heme (63).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [63]
In the citing paper
“The main cause of bacterial heme toxicity is not due to the release of free iron by cellular monooxygenases or by the peroxidase-like activity of heme (55, 63, 111).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [63]
In the citing paper
“Based on what has been reported, a likely cause of bacterial heme toxicity is its ability to damage DNA; however, the two have not been directly correlated (63).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [63]
In the citing paper
“The monooxygenase-like reactivity of heme is the cause of heme-mediated DNA and protein damage in vitro and is most likely the mechanism of heme toxicity in metazoans (1, 2, 63).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [63]
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 44
- Edelson, 1973, J. Exp. Med, 138, 318, 10.1084/jem.138.1.318 · DOI
- Clark, 1975, Blood, 45, 161, 10.1182/blood.V45.2.161.161 · DOI
- Clark, 1977, Blood, 50, 65, 10.1182/blood.V50.1.65.65 · DOI
- Jaques, 1975, Arch. Int. Physiol. Biochem, 83, 976
- Stadhouders, 1962, Neth. Milk Dairy J, 16, 96
- Jago, 1962, 111, 585
- Wallace, 1982, J. Biol. Chem, 257, 4966, 10.1016/S0021-9258(18)34620-9 · DOI
- Eaton, 1982, Science, 215, 691, 10.1126/science.7036344 · DOI
- Rosen, 1977, J. Biol. Chem, 252, 4803, 10.1016/S0021-9258(17)40127-X · DOI
- Klebanoff, 1974, J. Biol. Chem, 249, 3724, 10.1016/S0021-9258(19)42533-7 · DOI
- Chan, 1971, J. Amer. Chem. Soc, 93, 4632, 10.1021/ja00747a071 · DOI
- Piatt, 1977, FEBS Lett, 74, 251, 10.1016/0014-5793(77)80857-0 · DOI
- Khan, 1983, 80, 5195
- Shiga, 1973, Arch. Biochem. Biophys, 154, 540, 10.1016/0003-9861(73)90006-4 · DOI
- Weiss, 1980, J. Biol. Chem, 255, 9912, 10.1016/S0021-9258(18)43479-5 · DOI
- Aft, 1983, J. Biol. Chem, 258, 12069, 10.1016/S0021-9258(17)44341-9 · DOI · Paper page
- Sausville, 1979, Biochemistry, 17, 2746, 10.1021/bi00607a008 · DOI
- Myers, 1982, Biochemistry, 21, 1707, 10.1021/bi00537a001 · DOI
- Mohindru, 1983, Biochemistry, 22, 30A, 10.1021/bi00270a005 · DOI
- Gutteridge, 1982, Biochem. Pharmacol, 31, 2801, 10.1016/0006-2952(82)90136-8 · DOI
- Cederbaum, 1980, Biochemistry, 19, 3698, 10.1021/bi00557a010 · DOI
- Floyd, 1983, Biochemistry, 22, 2645, 10.1021/bi00280a008 · DOI
- Oberley, 1979, FEBS Lett, 97, 47, 10.1016/0014-5793(79)80049-6 · DOI
- Drath, 1974, Infect. Immun, 10, 1077, 10.1128/iai.10.5.1077-1083.1974 · DOI
- Bachur, 1978, Cancer Res, 38, 1745
- Kanovsky, 1984, J. Biol. Chem, 259, 5596, 10.1016/S0021-9258(18)91055-0 · DOI
- Harrison, 1978, FEBS Lett, 92, 327, 10.1016/0014-5793(78)80780-7 · DOI
- Albrich, 1981, 78, 210
- Rodriguez, 1982, Biochem. Biophys. Res. Commun, 104, 1470, 10.1016/0006-291X(82)91416-4 · DOI
- Burger, 1981, J. Biol. Chem, 256, 11636, 10.1016/S0021-9258(19)68452-8 · DOI
- Kaplan, 1960, Science, 131, 392, 10.1126/science.131.3398.392 · DOI
- Fine, 1963, Biochemistry, 2, 116, 10.1021/bi00901a020 · DOI
- Pesce, 1964, J. Biol. Chem, 239, 1753, 10.1016/S0021-9258(18)91253-6 · DOI
- Kaplan, 1964, 17, 131
- Inubushi, 1981, Vol. 76, 88
- Lamson, 1973, Anal. Biochem, 52, 647, 10.1016/0003-2697(73)90074-2 · DOI
- McFaul, 1986, Vol. 132, 491
- McFaul, 1985, 179, 331
- McFaul, 1986, 183, 244
- Lin, 1986, Biochem. Med. Metab. Biol, 36, 60, 10.1016/0885-4505(86)90107-6 · DOI
- Adams, 1972, Adv. Radiat. Chem, 3, 125
- Packer, 1968, Chem. Commun, 15, 826
- Simon, 1964, Arch. Biochem. Biophys, 105, 197, 10.1016/0003-9861(64)90253-X · DOI
- Ames, 1981, 78, 6858
Cited by
Sorted by citations
The Toxicities of Native and Modified Hemoglobins
Everse, J., & Hsia, N. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00499-6 · Cited by 346
Self-citationOvercoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
Anzaldi, L. L., & Skaar, E. P. (2010) · Infection and Immunity · doi:10.1128/iai.00613-10 · Cited by 295
Metadata
- Authors
- Lin, H., & Everse, J.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1987-03
- Volume
- 161
- Issue
- 2
- Pages
- 323-331
- ISSN
- 0003-2697
- Cited by
- 15
- References
- 0
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
