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PubMed1996

Biliary excretion of biochemically active cyanobacteria (blue-green algae) hepatotoxins in fish.

Previous reports demonstrated that microcystin and related cyanobacteria polypeptides are rapidly cleared from plasma and accumulate in liver tissue. In the present study, we have used their ability to inhibit protein phosphatases to show that these cyanobacteria hepatotoxins are excreted into the bile of experimentally poisoned rainbow trout. At various times after oral administration of hepatotoxic Microcystis aeruginosa, bile samples were analysed for microcystin content by methanol extraction and protein phosphatase assays. An inhibitory principle that specifically suppressed protein phosphatase activity was detected in all bile samples removed between 1 and 72 h after oral exposure to toxic algae. These results indicate that biochemically active microcystin molecules are excreted into the biliary tract of poisoned fish.

Animals↗
PubMed1978

Some properties of allophycocyanin from a thermophilic blue-green alga.

Allophycocyanin was purified from the extremely thermophilic blue-green alga Synechococcus lividus. It was shown to be more stable to thermal or urea denaturation than allophycocyanin from a mesophilic organisms. Its amino acid composition and spectroscopic response to pH were investigated. An analysis was made of the relatively low fluorescence polarization of allophycocyanin compared to that of a comparable sized aggregate of the biliprotein, C-phycocyanin. A rather speculative conclusion was reached that suggests that the lower polarization of allophycocyanin may be caused by orientations or positioning of the chromophores that are more favorable for intra-protein energy transfer.

Journal Article↗
PubMed1978

Comparison of the stability of phycocyanins from thermophilic, mesophilic, psychrophilic and halophilic algae.

Protein unfolding of eight different phycocyanins was investigated utilizing circular dichroism and visible spectra. The phycocyanin samples were extracted from algae that are normally found in vastly different environments, and are classified as mesophilic, thermophilic, halophilic and psychrophilic. The ability of these proteins to resist the denaturant urea is in the order of thermophile greater than mesophile, halophile greater than psychrophile. Based on a two-state approximation the apparent free energies of protein unfolding at zero urea denaturant concentration, deltaGH2Oapp, were found to range from 2.4 to 8.8 kcal/mole for the eight phycocyanins at pH 6 and 25 degrees C. The proteins from the thermophile are generally more stable than those from the mesophile. An extra stability of the halophile is believed due to the specific interaction of the proteins and the ions in solution. A correction for deltaGH2Oapp due to minor amino acid differences reveals that the stability and the structural properties of these proteins are primarily affected by this minor difference in amino acid compositions.

Amino Acids↗
PubMed1991

Model for a self-repairing system of non-articulated coralline algae.

We propose a perspective for living systems, emphasizing that living systems are organized through the recognition of themselves and their surroundings. Oscillator functions in Brownian Algebra are introduced, supposing that the oscillation can be regarded as metabolism of the living state. We illustrate the idea of the self-repairing model in non-articulated coralline algae. Since various cells of this plant are assumed to be identified with the periodic sequence of oscillations, the individual periodic sequence characterizing a cell is supposed to be determined by a local-interaction rule which can be regarded as the process of self-organization through the recognition of local shape. Owing to accidental injury the rule characterizing a cell's own state can be transformed, and it entails another periodic sequence. We express the oscillator as state flow diagrams, and analyze the relationship between the transformation of the period and the injury which is represented by the removal of transient in flow diagrams.

Eukaryota↗
PubMed1989

Kinetic properties of a sn-glycerol-3-phosphate dehydrogenase purified from the unicellular alga Chlamydomonas reinhardtii.

A sn-glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase, EC 1.1.1.8) has been purified from the unicellular green alga Chlamydomonas reinhardtii 3400-fold to a specific activity of 34 mumol/mg protein per min by a simple procedure involving two chromatographic steps on affinity dyes. The pH optimum for reduction of dihydroxyacetone phosphate was 6.8 and for glycerol 3-phosphate oxidation it was 9.5. In the direction of dihydroxyacetone phosphate reduction, the enzyme showed Michaelis-Menten kinetics. The enzyme reacted specifically with NADH and dihydroxyacetone phosphate as substrates with affinity constants of 16 and 12 microM, respectively. Product inhibition as well as competitive inhibition pattern indicated a random-bi-bi reaction mechanism for sn-glycerol-3-phosphate dehydrogenase from C. reinhardtii. The effective control of dihydroxyacetone reduction catalysed via this enzyme by ATP, Pi and NAD gave evidence for a physiological role of the enzyme in plastidic glycolysis.

Chlamydomonas↗
PubMed1991

Regulation of molybdenum cofactor species in the green alga Chlamydomonas reinhardtii.

Molybdenum cofactor (MoCo) of molybdoenzymes is constitutively produced in cells of the green alga Chlamydomonas reinhardtii grown in ammonium media, under which conditions certain molybdoenzymes are not synthesized. In soluble form, MoCo was found to be present in several forms: (i) as a low Mr free species; (ii) bound to a MoCo-carrier protein of about 50 kDa that could release MoCo to directly reconstitute in vitro nitrate reductase activity in the nit-1 mutant of Neurospora crassa, but not to Thiol-Sepharose which, in contrast, bonded free MoCo; and (iii) bound to other proteins, putatively constitutive molybdoenzymes, which only released MoCo after a denaturing treatment. The amount of total MoCo (free, carrier-bound and heat releasable forms) was dependent on the growth phase of cell cultures. Constitutive levels of total MoCo in ammonium-grown cells markedly increased when cells were transferred to media lacking ammonium (nitrate, urea or nitrogen-free media). This increase did not require de novo protein synthesis and was stimulated by light. Levels of both total MoCo and free plus carrier-bound MoCo seemed to be unrelated to either nitrate reductase synthesis or functioning of nit-1 and nit-2 genes responsible for nitrate reductase structure and regulation, respectively. Results suggest that MoCo is continuously synthesized in C. reinhardtii and that its levels are regulated by ammonium in a way independent of nitrate reductase synthesis.

Ammonium Chloride↗
PubMed1982

Phylogeny and ontogeny of the phosphoglycerate mutases--IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals.

1. The distribution of the glycerate-2,3-P2 dependent and independent phosphoglycerate mutases (PGM) has been studied in more than eighty species. 2. PGM activity in the extracts has been measured in the presence and in the absence of glycerate-2,3-P2, at pH 7.5 and at pH 8.5. 3. All samples with glycerate-2,3-P2 dependent PGM possess higher activity at pH 7.5 than at pH 8.5. In contrast, samples with glycerate-2,3-P2 independent PGM possess lower activity at pH 7.5 than at pH 8.5. 4. In algae and fungi both glycerate-2,3-P2 dependent and independent PGM have been found. 5. In plants only glycerate-2,3-P2 independent PGM has been detected. 6. In animals both types of PGM are present. Independent PGM activity is present in sponges, coelenterates, myriapods, arachnids and echinoderms. Glycerate-2,3-P2 dependent PGM is present in platyhelminths, mollusks, annelids, crustaceans, insects and vertebrates.

2,3-Diphosphoglycerate↗
PubMed1989

A comparative study of animal erythrocyte agglutinins from marine algae.

1. Fifteen marine algal species were analyzed for agglutinins to rabbit, sheep and human A, B and O blood group erythrocytes. 2. Protein extracts from all marine algae agglutinated rabbit erythrocytes, whereas twelve and five extracts agglutinated sheep and human erythrocytes, respectively. 3. The highest agglutination titers were consistently observed with rabbit erythrocytes. 4. Dictyota dichotoma strongly agglutinated human B blood group erythrocytes relative to A and O group erythrocytes. 5. Agglutination titer of rabbit erythrocytes by six algal extracts was not inhibited by mono- or polysaccharides, yet was reduced by glycoproteins.

Animals↗
PubMed1992

A sulfated proteoglycan from the red alga Gracilaria verrucosa is a hemagglutinin.

1. A novel hemagglutinin was isolated from the red alga Gracilaria verrucosa and characterized as a sulfated proteoglycan with 92% carbohydrate content. 2. It is a dimer (MW 27,000 and MW 23,000); its molecular weight (MW) and isoelectric point are 49,000 and 3.8, respectively. 3. It agglutinates rabbit greater than horse greater than guinea pig greater than goose erythrocytes. 4. This activity is sensitive to heat, but insensitive to protease or periodate. It is not inhibited by simple sugars but by fetuin. 5. Since the periodate treatment of the rabbit erythrocyte lowers agglutination, this hemagglutinin is probably a lectin or a lectin-like molecule with complex saccharide specificity.

Animals↗
PubMed1989

Structure of the three beta-tubulin-encoding genes of the unicellular alga, Polytomella agilis.

The quadriflagellate, unicellular, colorless alga, Polytomella agilis, contains several distinct microtubule arrays. To study the genetic basis of microtubule heterogeneity in P. agilis, we characterized its tubulin(Tub)-encoding genes (tub). The three beta tub genes detected in blots of P. agilis DNA were isolated from a genomic library. The structure and organization of the genes were examined by restriction mapping and nucleotide (nt) sequencing. S1 nuclease protection studies showed that all three genes are expressed. The predicted amino acid (aa) sequences are more than 98% conserved with the Chlamydomonas reinhardtii and Volvox carteri beta-Tubs, underscoring the close phylogenetic relationship of these species. Evolutionary divergence among the P. agilis genes is demonstrated by differences in intron number, nt sequences in noncoding regions, and silent nt substitutions in the coding regions. However, the proteins encoded by the beta 1 and beta 3 tub genes are identical; the beta 2 gene product differs by one conservative aa substitution. These results are in striking contrast to the C-terminal aa diversity reported within beta tub gene families in animal, higher plant and fungal systems. The data support the hypothesis that those tub genes whose products assemble into axonemal microtubules are subject

Amino Acid Sequence↗
PubMed1992

Structure of a gene encoding heat-shock protein HSP70 from the unicellular alga Chlamydomonas reinhardtii.

The structure of a gene encoding a 70-kDa heat-shock protein (HSP70) from the unicellular alga, Chlamydomonas reinhardtii, is described. This gene shows a remarkable expression pattern, because it is inducible by light as well as by elevated temperature [von Gromoff et al., Mol. Cell. Biol. 9 (1989) 3911-3918]. As a first step in the investigation of trans-acting factors involved in environmentally controlled expression of this hsp70 gene, the nucleotide sequence of the entire gene, including its 5'- and 3'-flanking regions was determined. Although the deduced amino acid sequence exhibits a high degree of conservation to the HSP70 from higher plants, the C. reinhardtii gene has a unique structure among the members of the hsp70 gene family. While most hsp70 genes have only one or no intron, the coding region of the C. reinhardtii gene is interrupted by six introns. Besides putative TATA and CCAAT boxes, two heat-shock elements (HSE) were found in the promoter region, and a third HSE motif was located within the fourth intron. A computer search for regulatory cis-acting elements revealed a noted similarity of a 5'-upstream sequence motif to the G-box motif conserved in higher plants. A polyadenylation recognition sequence canonical for nuclear genes of C. reinhardtii is located downstream from the coding sequence.

Amino Acid Sequence↗
PubMed1994

Extensive sequence divergence in the 3' inverted repeat of the chloroplast rbcL gene in non-flowering land plants and algae.

A stem-loop region is present at the 3' terminus of the chloroplast rbcL mRNA in all taxa surveyed to date. In spinach, this structure has been shown by others to be involved in modulating transcript stability and correct 3' terminus processing, and is a conserved feature of other flowering plant rbcL mRNAs. In Chlamydomonas reinhardtii, an analogous structure has been shown by others to serve as a transcription terminator. Our sequencing data have shown that this region is highly divergent in several non-flowering land plants, as evidenced by representatives from the ferns, conifers, 'fern-allies' and liverworts. To extend our analysis, a computer-assisted survey of the stem-loop region of the 3' flanking region of published chloroplast rbcL genes was undertaken. The flowering plant rbcL inverted repeats (IR) were remarkably conserved in sequence, allowing for precise multiple alignments of both monocot and dicot sequences within a single matrix. Surprisingly, sequences obtained from non-flowering land plants, algae, photosynthetic protists and photosynthetic prokaryotes were extremely variant, in terms of both sequence composition and thermodynamic parameters.

Amino Acid Sequence↗
PubMed1994

A group-I self-splicing intron in the nuclear small subunit rRNA-encoding gene of the green alga, Chlorella ellipsoidea C-87.

We report the presence of a 442-bp group-I self-splicing intron in the nuclear small subunit (SSU) rRNA-encoding gene (rDNA) of the unicellular green alga, Chlorella ellipsoidea C-87 (C. saccharophila 211-1a). The intron was found to be inserted at a position within the highly conserved helix 48 that was close to the 3' terminus of the SSU rRNA. The position was exactly the same as previously identified for the Pneumocystis carinii intron. A secondary structure model for the C. ellipsoidea intron contained all P1-P10 motifs of the group-I introns. Although the overall secondary structure of the C. ellipsoidea intron was substantially different from that of the intron in the nuclear large subunit rDNA of Tetrahymena thermophila, the nucleotide (nt) sequences constituting the catalytic core were strikingly conserved between the two; only three of 48 nt were different. The C. ellipsoidea intron was autocatalytically excised from the transcript in vitro via the group-I mechanism under somewhat unique conditions. No SSU rDNA intron was found in six other Chlorella species, including C. fusca var. vacuolata, C. kessleri, C. minutissima, C. protothecoides, C. sorokiniana and C. vulgaris.

Animals↗
PubMed1996

A cDNA coding for glutathione S-transferase from the unicellular green algae Coccomyxa sp.

A cDNA coding for glutathione S-transferase (GST) was cloned and sequenced from the unicellular green algae Coccomyxa sp. The predicted 215 amino acid polypeptide (23.9 kDa, pI 5.3) is most similar to the theta-type GSTs found in a variety of different eukaryotic organisms. Within this sub-class, the Coccomyxa GST is 42% identical (63% similar) to the flatfish Pleuronectes platessa homologue, and 24 to 35% (49-57%) to other theta-type GST's.

Amino Acid Sequence↗
PubMed1988

Immunomodulation by a unicellular green algae (Chlorella pyrenoidosa) in tumor-bearing mice.

A unicellular algae, Chlorella pyrenoidosa, was used as a biological response modifier. In C57BL/6(B6), C3H/He and DDD/1 mice, both intraperitoneal or oral administrations of autoclaved Chlorella cells or heat-extracted substance were carried out every other day for 10 days before mouse mammary carcinoma (MM-2) or Ehrlich ascites cells were transplanted into the peritoneal cavity. In case of mouse leukemia cells (EL-4), subcutaneous transplantation was carried out. All control mice died within 20 days after each tumor cell transplantation, while 73.3-80% of the treated groups survived over 60 days in the combination of MM-2 vs. C3H/He and EL-4 vs. B6, respectively. The cytotoxic activities against tumor cells, that were abolished by treatment with anti-Thyl.2 monoclonal antibody plus complement, were evidenced in the experimental host. Since Chlorella cells and derivatives showed no indication of direct in vitro cytotoxicity to either tumor or mouse spleen cells, the antitumor effects documented may be mediated by host immune response.

Adjuvants, Immunologic↗
PubMed2005

Fucoidan a sulfated polysaccharide from brown algae is a potent modulator of connective tissue proteolysis.

Fucoidans are sulfated fucosylated polymers from brown algae cell wall that exhibit some heparin/heparan sulfate properties. We previously demonstrated that these polysaccharides were able in vitro to stimulate dermal fibroblast proliferation and extracellular matrix deposition. Here, we investigated the action of a 16kDa fucoidan fraction on parameters involved in connective tissue breakdown. This fucoidan is able to inhibit gelatinase A secretion and stromelysin 1 induction by interleukin-1beta on dermal fibroblasts in culture. Furthermore, we observed that fucoidan increases the rate of association of MMPs with their specific inhibitors namely TIMPs. Using tissue sections of human skin in ex vivo experiments, we evidenced that this polysaccharide was able to minimize human leukocyte elastase activity resulting in the protection of human skin elastic fiber network against the enzymatic proteolysis due to this serine proteinase. These results suggested that fucoidan could be used for treating some inflammatory pathologies in which uncontrolled extracellular matrix degradation takes place.

Cells, Cultured↗