Retention and photodynamic effects of haematoporphyrin derivative in cells after prolonged cultivation in the presence of porphyrin

Christensen, Terje; Sandquist, T.; Feren, Kari; Waksvik, Helga; Moan, Johan Emelian

doi:10.1038/bjc.1983.154

Cited by 56 publications

(17 citation statements)

References 19 publications

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“…Migration of porphyrins within the cell as a function of incubation time is indicated by reports that porphyrins photosensitize at different cellular loci, as a function of time prior to irradiation (Kessel and Kohn, 1980;Christensen et al, 1983a;Moan et al, 1983). In our laboratory (unpublished data) we have found that DHE initially binds to very hydrophobic loci, perhaps representing lipid-rich membrane domains, then slowly migrates to more hydrophilic intracellular regions.…”

Section: Porphyrin Transportmentioning

confidence: 57%

HEMATOPORPHYRIN and HPD: PHOTOPHYSICS, PHOTOCHEMISTRY and PHOTOTHERAPY

Kessel

1984

Photochem & Photobiology

258

116

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Section: Porphyrin Transportmentioning

confidence: 57%

HEMATOPORPHYRIN and HPD: PHOTOPHYSICS, PHOTOCHEMISTRY and PHOTOTHERAPY

Kessel

1984

Photochem & Photobiology

258

116

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“…The absorbance peak corresponding to the heme Sorret band (387.5 mm) was quantitated by comparing to an external standard (hemin, Sigma) (24).…”

Section: Methodsmentioning

confidence: 99%

Heme Oxygenase-mediated Resistance to Oxygen Toxicity in Hamster Fibroblasts

Dennery

Sridhar

Lee

et al. 1997

Journal of Biological Chemistry

129

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The role of heme oxygenase (HO)-1 was evaluated in the oxygen-resistant hamster fibroblast cell line, O 2 R95, which moderately overexpress HO when compared with the parental cell line, HA-1. To suppress HO-1 expression, O 2 R95 were transfected with HO-1 antisense oligonucleotide or treated with tin-mesoporphyrin (SnMP). To increase HO-1 expression, cells were transfected with HO-1 cDNA in a pRC/cytomegalovirus (CMV) vector. All cells were challenged with a 48-h exposure to 95% O 2 (hyperoxia). When HO activity was suppressed, O 2 R95 cells had significantly decreased cell viability, increased susceptibility to lipid peroxidation, and increased protein oxidation in hyperoxia. In contrast, further overexpression of HO-1 did not improve resistance to oxygen toxicity. Antisense-transfected cells and SnMP-treated cells with lowered HO activity showed increased levels of cellular heme compared with controls. In the HO-1 cDNA-transfected O 2 R95 cells, cellular heme was lowered compared with controls; however, cellular redox active iron levels were increased. We conclude that HO mediates cytoprotection to oxygen toxicity within a narrow range of expression. We speculate that this protective effect may be mediated in part through increased metabolism of the pro-oxidant heme but that higher levels of HO activity obviate protection by increased redox active iron release.Heme oxygenase (HO-1), 1 the rate-limiting enzyme in the conversion of heme to bilirubin, is known to be induced by various oxidant stresses. However, it is not clear whether HO serves in protection against hyperoxia and, if so, by which mechanisms. HO-1 antisense transfection experiments have shown that higher HO-1 protein levels were associated with protection against UVA radiation (1). Furthermore, transfection of coronary vessel endothelial cells with an overexpression vector containing HO-1 cDNA resulted in resistance against hemoglobin-induced injury (2). We have previously shown that HA-1 hamster fibroblasts made stably resistant to oxygen toxicity (O 2 R95) had 1.8-fold higher HO activity (3), suggesting that moderate increases in HO activity may be beneficial in resistance to oxygen toxicity. However, O 2 R95 cells have increases in other antioxidants that may also contribute to their resistance to oxygen toxicity (4), and no direct evidence currently exists linking HO to resistance to oxygen toxicity.Investigators have hypothesized that HO may serve a role in protection against oxidative injury by forming the antioxidant molecules biliverdin and bilirubin (5, 6). Additionally, induction of ferritin with enhanced HO activity has been observed (1). This could lead to sequestration of redox active iron, thereby conferring protection against oxidative stress (7). Another possible antioxidant mechanism of HO could involve the destruction of heme itself. Heme and hemoproteins have been shown by several investigators to be instrumental in exacerbating oxidative injury (8, 9). This has lead to the hypothesis that reduction of the cellular heme pool by ...

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“…The mechanisms for cell inactivation seem to some extent to depend on the photosensitizer concentration and on the incubation time with the photosensitizer (Fritsch et al, 1976;Kessel, 1981;Christensen et al, 1983). Photoactivation of porphyrin after incubation for a short time (1 h) has been reported to damage the membrane to a relatively greater degree than photoactivation of porphyrin after a long (22h) incubation, using light doses inactivating the same number of cells (Christensen et al, 1983;. A number of intracellular effects have been reported after photoactivation of porphyrins over short and long incubations.…”

mentioning

confidence: 99%

Relationship between changes in antigen expression and protein synthesis in human melanoma cells after hyperthermia and photodynamic treatment

Cl¹,

Ranheim²,

Malik³

et al. 1988

Br J Cancer

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Summary Hyperthermia and photoactivated hematoporphyrin derivative induce a dose-dependent reduction in the expression of the p250 surface melanoma-associated antigen on the human FME cell line. Expression of this glycoprotein antigen was quantitated by immunofluorescence flow cytometry based on the monoclonal antibody 9.2.27. Decrease in antigen expression was followed by a transient increase above the level for untreated cells, before normalization occurred about one week after treatment.These treatment-induced changes in antigen expression could partly be explained by changes in protein synthesis. This conclusion was based on the following observations: Hyperthermia and photoactivated hematoporphyrin derivative both inhibited protein synthesis. The latter increased again rapidly to rates above normal until antigen expression reached normal level, whereupon the protein synthesis rate decreased to normal.Inhibition of protein synthesis by cycloheximide 1 day after heating, prevented the recovery of antigen expression, demonstrating that protein synthesis is necessary for resumption of normal antigen expression.The changes in both antigen expression and protein synthesis were dose-dependent, and the magnitude and duration of the changes increased with increasing dose. The time courses of the changes in protein synthesis after two different treatments which both inactivated two logs of cells were almost identical, as were the time courses after two lower heat doses inactivating one log of cells. These similarities were reflected in the changes in antigen expression.At the same time as protein synthesis reached its maximum and antigen expression resumed normal level, an increase in the Golgi apparatus was observed ultrastructurally, indicating an increased synthesis rate and transportation of glycoproteins to the cell surface.

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Retention and photodynamic effects of haematoporphyrin derivative in cells after prolonged cultivation in the presence of porphyrin

Cited by 56 publications

References 19 publications

HEMATOPORPHYRIN and HPD: PHOTOPHYSICS, PHOTOCHEMISTRY and PHOTOTHERAPY

HEMATOPORPHYRIN and HPD: PHOTOPHYSICS, PHOTOCHEMISTRY and PHOTOTHERAPY

Heme Oxygenase-mediated Resistance to Oxygen Toxicity in Hamster Fibroblasts

Relationship between changes in antigen expression and protein synthesis in human melanoma cells after hyperthermia and photodynamic treatment

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