TY  - JOUR
AU  - Pajic, I
AU  - Kljajic, Z
AU  - Dogovic, N
AU  - Sladić, Dušan
AU  - Juranić, Z.
AU  - Gasic, MJ
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/501
AB  - A lectin from the Adriatic sponge Haliclona cratera was purified by ion-exchange and gel chromatography The molecular mass of the lectin is approximately 29 kDa. Purified lectin is rich in hydrophobic and basic amino acids and has an isoelectric point at pH 8.6. H. cratera lectin is relatively heat- and pH-stable. It agglutinates native and trypsinized, papainized and neuraminidase-treated human A, B, O, AB and sheep erythrocytes, and the hemagglutinating activity is independent of Ca2+, Mn2+ and Mg2+ ions; D-galactose and N-acetyl-D-galactosamine are found to be moderate inhibitors of the activity. H. cratera lectin displays cytotoxic effect on HeLa and FemX cells and weak mitogenic effect on human T-lymphocytes pretreated with phytohemagglutinin (PHA). (C) 2002 Elsevier Science Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology
T1  - A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity
VL  - 132
IS  - 2
SP  - 213
EP  - 221
DO  - 10.1016/S1532-0456(02)00068-6
ER  - 

@article{
author = "Pajic, I and Kljajic, Z and Dogovic, N and Sladić, Dušan and Juranić, Z. and Gasic, MJ",
year = "2002",
abstract = "A lectin from the Adriatic sponge Haliclona cratera was purified by ion-exchange and gel chromatography The molecular mass of the lectin is approximately 29 kDa. Purified lectin is rich in hydrophobic and basic amino acids and has an isoelectric point at pH 8.6. H. cratera lectin is relatively heat- and pH-stable. It agglutinates native and trypsinized, papainized and neuraminidase-treated human A, B, O, AB and sheep erythrocytes, and the hemagglutinating activity is independent of Ca2+, Mn2+ and Mg2+ ions; D-galactose and N-acetyl-D-galactosamine are found to be moderate inhibitors of the activity. H. cratera lectin displays cytotoxic effect on HeLa and FemX cells and weak mitogenic effect on human T-lymphocytes pretreated with phytohemagglutinin (PHA). (C) 2002 Elsevier Science Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology",
title = "A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity",
volume = "132",
number = "2",
pages = "213-221",
doi = "10.1016/S1532-0456(02)00068-6"
}

Pajic, I., Kljajic, Z., Dogovic, N., Sladić, D., Juranić, Z.,& Gasic, M.. (2002). A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity. in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology
Elsevier Science Inc, New York., 132(2), 213-221.
https://doi.org/10.1016/S1532-0456(02)00068-6

Pajic I, Kljajic Z, Dogovic N, Sladić D, Juranić Z, Gasic M. A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity. in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology. 2002;132(2):213-221.
doi:10.1016/S1532-0456(02)00068-6 .

Pajic, I, Kljajic, Z, Dogovic, N, Sladić, Dušan, Juranić, Z., Gasic, MJ, "A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity" in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology, 132, no. 2 (2002):213-221,
https://doi.org/10.1016/S1532-0456(02)00068-6 . .

TY  - JOUR
AU  - Muller, W.E.G.
AU  - Sladić, Dušan
AU  - Zahn, R.K.
AU  - Bassler, K.-H.
AU  - Dogovic, N.
AU  - Gerner, H.
AU  - Gasic, M.J.
AU  - Schroder, H.C.
PY  - 1987
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/13
AB  - The hydroquinone-containing cytostatic compound avarol inhibits predominantly growth of those cell lines which have a low level of superoxide dismutase. The substrate of this enzyme, the superoxide anion, was found to be formed during the in vitro oxidation reaction of avarol to its semiquinone radical in the presence of oxygen. Under the same incubation conditions plasmid DNA (pBR322) was converted from the fully supercoiled circular form mainly to the nicked circular form, indicating that the compound causes primarily single-strand breaks. Using Friend erythroleukemia cells (FLC) it was found that avarol induces a dose-dependent DNA damage; the maximum number of DNA strand breaks was observed at 5 h after addition of the compound to the cells. Removal of avarol resulted in a rapid DNA rejoining with biphasic repair kinetics [first half-time, 8 min (90% of the breaks) and a second half-time, 40 min (10% of the breaks)]. When the degree of avarol-induced DNA damage in FLC was compared with the drug-caused inhibition of cell growth a close correlation was established. Avarol displayed no effect on dimethyl sulfoxide-induced erythrodifferentiation of FLC as determined by the benzidine reaction and by dot blot hybridization experiments. From incubation studies of FLC with [3H]avarol no hint was obtained for the formation of an adduct between DNA and the compound. The subcellular distribution of [3H]avarol was studied in liver cells after i.v. application of the compound. The predominant amount of the compound was present in the cytosolic fraction; little avarol was associated with plasma membranes, nuclei, and mitochondria. Using (a) oxidative phosphorylation and (b) oxygen uptake as parameters for mitochondrial function, no effect of the compound on the activity of this organelle was determined. These results suggest that avarol forms superoxide anions (and in consequence possibly also hydroxyl radicals) especially in those cells which have low levels of superoxide dismutase. Moreover, evidence is provided that the active oxygen species cause DNA damage resulting in the observed cytotoxic effect.
T2  - Cancer Research
T1  - Avarol-induced DNA strand breakage in vitro and in Friend erythroleukemia cells
VL  - 47
IS  - 24 I
SP  - 6565
EP  - 6571
UR  - https://hdl.handle.net/21.15107/rcub_cherry_13
ER  - 

@article{
author = "Muller, W.E.G. and Sladić, Dušan and Zahn, R.K. and Bassler, K.-H. and Dogovic, N. and Gerner, H. and Gasic, M.J. and Schroder, H.C.",
year = "1987",
abstract = "The hydroquinone-containing cytostatic compound avarol inhibits predominantly growth of those cell lines which have a low level of superoxide dismutase. The substrate of this enzyme, the superoxide anion, was found to be formed during the in vitro oxidation reaction of avarol to its semiquinone radical in the presence of oxygen. Under the same incubation conditions plasmid DNA (pBR322) was converted from the fully supercoiled circular form mainly to the nicked circular form, indicating that the compound causes primarily single-strand breaks. Using Friend erythroleukemia cells (FLC) it was found that avarol induces a dose-dependent DNA damage; the maximum number of DNA strand breaks was observed at 5 h after addition of the compound to the cells. Removal of avarol resulted in a rapid DNA rejoining with biphasic repair kinetics [first half-time, 8 min (90% of the breaks) and a second half-time, 40 min (10% of the breaks)]. When the degree of avarol-induced DNA damage in FLC was compared with the drug-caused inhibition of cell growth a close correlation was established. Avarol displayed no effect on dimethyl sulfoxide-induced erythrodifferentiation of FLC as determined by the benzidine reaction and by dot blot hybridization experiments. From incubation studies of FLC with [3H]avarol no hint was obtained for the formation of an adduct between DNA and the compound. The subcellular distribution of [3H]avarol was studied in liver cells after i.v. application of the compound. The predominant amount of the compound was present in the cytosolic fraction; little avarol was associated with plasma membranes, nuclei, and mitochondria. Using (a) oxidative phosphorylation and (b) oxygen uptake as parameters for mitochondrial function, no effect of the compound on the activity of this organelle was determined. These results suggest that avarol forms superoxide anions (and in consequence possibly also hydroxyl radicals) especially in those cells which have low levels of superoxide dismutase. Moreover, evidence is provided that the active oxygen species cause DNA damage resulting in the observed cytotoxic effect.",
journal = "Cancer Research",
title = "Avarol-induced DNA strand breakage in vitro and in Friend erythroleukemia cells",
volume = "47",
number = "24 I",
pages = "6565-6571",
url = "https://hdl.handle.net/21.15107/rcub_cherry_13"
}

Muller, W.E.G., Sladić, D., Zahn, R.K., Bassler, K.-H., Dogovic, N., Gerner, H., Gasic, M.J.,& Schroder, H.C.. (1987). Avarol-induced DNA strand breakage in vitro and in Friend erythroleukemia cells. in Cancer Research, 47(24 I), 6565-6571.
https://hdl.handle.net/21.15107/rcub_cherry_13

Muller W, Sladić D, Zahn R, Bassler K, Dogovic N, Gerner H, Gasic M, Schroder H. Avarol-induced DNA strand breakage in vitro and in Friend erythroleukemia cells. in Cancer Research. 1987;47(24 I):6565-6571.
https://hdl.handle.net/21.15107/rcub_cherry_13 .

Muller, W.E.G., Sladić, Dušan, Zahn, R.K., Bassler, K.-H., Dogovic, N., Gerner, H., Gasic, M.J., Schroder, H.C., "Avarol-induced DNA strand breakage in vitro and in Friend erythroleukemia cells" in Cancer Research, 47, no. 24 I (1987):6565-6571,
https://hdl.handle.net/21.15107/rcub_cherry_13 .