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Light Dependent (light + dependent)
Selected AbstractsCytotoxic action mode of a novel porphyrin derivative isolated from harmful red tide dinoflagellate Heterocapsa circularisquamaJOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, Issue 3 2008Daekyung Kim Abstract Heterocapsa circularisquama is known to cause lethal effect on bivalves, but toxic effect on fish has not been reported yet. Recently, we have found that H. circularisquama has potent light-dependent hemolytic toxins. Based on the chemical structural analysis, one of the hemolytic toxins named H2-a was found to be a novel porphyrin derivative with similar structure to pyropheophorbide a methyl ester (PME), a well-known photoactive hemolytic agent (Miyazaki et al., Aquatic Toxicol. 2005;73:382--393). To clarify the cytotoxic action mode of H2-a, we examined the effects of H2-a on HeLa cells in comparison with PME. The cytotoxicities of both reagents were strictly light dependent, and no significant cytotoxic effects including cellular morphological changes were induced without light illumination. The dose response curves revealed that H2-a showed stronger cytotoxicity to HeLa cells than PME. Fluorescence microscopic observation suggested that H2-a tends to accumulate in the plasma membrane, whereas PME seems to distribute entire cytoplasm. Although PME induced typical apoptotic nuclear morphological changes and DNA fragmentation in HeLa cells, no such apoptosis-inducing ability of H2-a was observed. Among the radical scavengers, histidine significantly inhibited the cytotoxic activity of H2-a, suggesting the involvement of singlet oxygen in the cytotoxicity. These results suggest that the cytotoxic mechanism of H2-a is necrotic rather than apoptosis differing from PME, even though these are structurally quite similar to each other. The relatively high affinity of H2-a to the plasma membrane might result in the potent and quick cytotoxicity without induction of apoptotic signal transduction. © 2008 Wiley Periodicals, Inc. J Biochem Mol Toxicol 22:158,165, 2008; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20216 [source] Melting out of sea ice causes greater photosynthetic stress in algae than freezing in,JOURNAL OF PHYCOLOGY, Issue 5 2007Peter J. Ralph Sea ice is the dominant feature of polar oceans and contains significant quantities of microalgae. When sea ice forms and melts, the microalgal cells within the ice matrix are exposed to altered salinity and irradiance conditions, and subsequently, their photosynthetic apparatuses become stressed. To simulate the effect of ice formation and melting, samples of sea-ice algae from Cape Hallett (Antarctica) were exposed to altered salinity conditions and incubated under different levels of irradiance. The physiological condition of their photosynthetic apparatuses was monitored using fast and slow fluorescence-induction kinetics. Sea-ice algae exhibited the least photosynthetic stress when maintained in 35, and 51, salinity, whereas 16, 21, and 65, treatments resulted in significant photosynthetic stress. The greatest photosynthetic impact appeared on PSII, resulting in substantial closure of PSII reaction centers when exposed to extreme salinity treatments. Salinity stress to sea-ice algae was light dependent, such that incubated samples only suffered photosynthetic damage when irradiance was applied. Analysis of fast-induction curves showed reductions in J, I, and P transients (or steps) associated with combined salinity and irradiance stress. This stress manifests itself in the limited capacity for the reduction of the primary electron receptor, QA, and the plastoquinone pool, which ultimately inhibited effective quantum yield of PSII and electron transport rate. These results suggest that sea-ice algae undergo greater photosynthetic stress during the process of melting into the hyposaline meltwater lens at the ice edge during summer than do microalgae cells during their incorporation into the ice matrix during the process of freezing. [source] STRUCTURE-ACTIVITY RELATIONSHIPS OF OLIGOAGAR ELICITORS TOWARD GRACILARIA CONFERTA (RHODOPHYTA)JOURNAL OF PHYCOLOGY, Issue 3 2001Florian Weinberger Agar oligosaccharides in the neoagarobiose series were prepared by partial enzyme hydrolysis, separated on Biogel P2 and P4, and analyzed by high-performance anion exchange chromatography with pulsed amperometric detection, yielding neoagarosaccharide fractions with a disaccharide repetition degree ranging from 1 (neoagarobiose) to more than 8 (neoagarohexadecaose). These fractions were analyzed for their biological activity toward the marine red alga Gracilaria conferta (Schousboe ex Montagne) J. et G. Feldmann in terms of increase of oxygen consumption, release of hydrogen peroxide, elimination of epiphytic bacteria, and induction of thallus tip bleaching. The structure,activity and dose,response relationships of neoagarosaccharides were very similar in the respiratory and oxidative burst responses and in their bactericidal properties, with neoagarosaccharides consisting of 6 to 8 disaccharide repeating units being the most active. All these responses were competitively inhibited by the reduced form of neoagarohexaose, neoagarohexaitol. In contrast, the tip-bleaching response was light dependent, required much higher concentrations of neoagarosaccharides, and was not inhibited by neoagarohexaitol, suggesting that it is an unspecific oxidative stress reaction. Putative structural effects on the recognition of endogenous agar-oligosaccharide elicitors by G. conferta are discussed. [source] Photoinhibition and loss of photosystem II reaction centre proteins during senescence of soybean leaves.PHYSIOLOGIA PLANTARUM, Issue 3 2002Enhancement of photoinhibition by the, stay-green' mutation cytG The ,stay-green' mutation cytG in soybean (Glycine max) partially inhibits the degradation of the light-harvesting complex II (LHCII) and the associated chlorophyll during monocarpic senescence. cytG did not alter the breakdown of the cytochrome b6/f complex, thylakoid ATP synthase or components of Photosystem I. In contrast, cytG accelerated the loss of oxygen evolution activity and PSII reaction-centre proteins. These data suggest that LHCII and other thylakoid components are degraded by separate pathways. In leaves induced to senesce by darkness, cytG inhibited the breakdown of LHCII and chlorophyll, but it did not enhance the loss of PSII-core components, indicating that the accelerated degradation of PSII reaction centre proteins in cytG was light dependent. Illumination of mature and senescent leaves of wild-type soybean in the presence of an inhibitor (lincomycin) of chloroplast protein synthesis revealed that senescence per se did not affect the rate of photoinhibition in leaves. Likewise, mature leaves of the cytG mutant did not show more photoinhibition than wild-type leaves. However, in senescent cytG leaves, photoinhibition proceeded more rapidly than in the wild-type. We conclude that the cytG mutation enhances photoinhibition in senescing leaves, and photoinhibition causes the rapid loss of PSII reaction-centre proteins during senescence in cytG. [source] | ||||||||||