Occurrence of Galβ(1å3)GalNAc-SerThr in the linkage region of polygalactosamine containing fungal glycoprotein from Cordyceps ophioglossoides

Kawaguchi, Noboru; Ohmori, Tai; Takeshita, Yasuyoshi; Kawanishi, Gosei; Katayama, Sumio; Yamada, Hideaki

doi:10.1016/0006-291x(86)91097-1

Cited by 16 publications

(5 citation statements)

References 7 publications

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“…4), and the following linkages were Most polysaccharides extracellularly produced by microorganisms are acidic or neutral. Polygalactosamine secreted by molds is a unique example of a microbial extracellular basic polysaccharide [24][25][26]. Gluconacetobacter xylinum ATCC 10245, which is well-known as a cellulose producer, synthesis cellulose-based glucose-coglucosamine and glucose-co-N-acetylglucosamine when it is grown on glucosamine and N-acetylglucosamine, respectively [27].…”

Section: Mnr Studiesmentioning

confidence: 99%

Structure of the polysaccharide isolated from the sheath of Sphaerotilus natans

Takeda

Nakamori

Hatta

et al. 2003

International Journal of Biological Macromolecules

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Section: Mnr Studiesmentioning

confidence: 99%

Structure of the polysaccharide isolated from the sheath of Sphaerotilus natans

Takeda

Nakamori

Hatta

et al. 2003

International Journal of Biological Macromolecules

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“…The observation that blood group A tetrasaccharide is also the best of the tested competitors for the Cgl-II binding site marks such fine specificity as an evolutionarily old characteristic of galectins and suggests that it might be functionally important. At least some fungi incorporate GalNAc into glycoproteins and polysaccharides (49), but there has not yet been enough structural characterization of fungal glycoconjugates to use this information to identify any candidate ligands. It is also possible that relevant ligands are not fungal, but perhaps animal, insect, or nematode glycoconjugates mediating, for instance, spore adhesion to those organisms (50).…”

Section: Figmentioning

confidence: 99%

Fungal Galectins, Sequence and Specificity of Two Isolectins from Coprinus cinereus

Cooper

Boulianne

Charlton

et al. 1997

Journal of Biological Chemistry

105

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Galectins are members of a genetically related family of ␤-galactoside-binding lectins. At least eight distinct mammalian galectins have been identified. More distantly related, but still conserving amino acid residues critical for carbohydrate-binding, are galectins in chicken, eel, frog, nematode, and sponge. Here we report that galectins are also expressed in a species of fungus, the inky cap mushroom, Coprinus cinereus. Two dimeric galectins are expressed during fruiting body formation which are 83% identical to each other in amino acid sequence and conserve all key residues shared by members of the galectin family. Unlike most galectins, these have no N-terminal post-translational modification and no cysteine residues. We expressed one of these as a recombinant protein and studied its carbohydrate-binding specificity using a novel nonradioactive assay. Binding specificity has been well studied for a number of other galectins, and like many of these, the recombinant C. cinereus galectin shows particular affinity for blood group A structures. These results demonstrate not only that the galectin gene family is evolutionarily much older than previously realized but also that fine specificity for complex saccharide structures has been conserved. Such conservation implies that galectins evolved to perform very basic cellular functions, presumably by interaction with glycoconjugates bearing complex lactoside carbohydrates resembling blood group A.Galectins are animal lectins that are related in amino acid sequence and specifically bind to ␤-galactoside carbohydrates such as lactose (1). Members of this gene family all include a conserved carbohydrate-binding domain but vary in inclusion of other domains and in tissue expression patterns. More distantly related, but conserving critical amino acid residues involved in carbohydrate-binding, are galectins in chicken, eel, frog, nematode, and sponge (2).Although galectins have been studied for 20 years now, physiological functions for these proteins have not yet been clearly established. Their affinity for oligosaccharides found on glycoconjugates on cell surfaces or in extracellular matrix has suggested that galectins function extracellularly by binding to such ligands. Indeed, certain galectins have particular affinity for specific glycoprotein ligands, such as polylactosamine chains on laminin (1, 3). When added to cells or overexpressed after transfection, galectins can have major effects on cell adhesion, proliferation, apoptosis, metastasis, and immune function (1-6). However, evidence has also been presented for intracellular functions of galectins, for instance in message splicing (7) or as nuclear proteins (8). Therefore, efforts are being directed at exploring the evolutionary origin of galectins in the hope that their functions will be easier to define in simple model organisms.Here we report that a species of fungus, the inky cap mushroom, Coprinus cinereus, expresses two lectins related in sequence and carbohydrate-binding specificity to other galectins. T...

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“…[53] Bioxanthracenes appear to be antimalarial, while the bioactivity data for glycoprotein containing N-acetylgalactosamine isolated from C. ophioglossoides are not available. [55,56,59] Chiou et al [132] observed a hypotensive effect of C. sinensis in anaesthetized rats and a vasorelaxant effect in isolated aorta. The fungus counteracted arrhythmia in rats and increased the dosage of ouabain required to produce arrhythmia in guinea-pigs.…”

Section: Other Bioactivitymentioning

confidence: 99%

The genus Cordyceps: a chemical and pharmacological review

Yue

Meng

Zhou

et al. 2013

Journal of Pharmacy and Pharmacology

202

128

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Objectives Natural remedies are becoming increasingly popular and important in the public and scientific communities. Historically, natural remedies have been shown to present interesting biological and pharmacological activity and are used as chemotherapeutic agents. For centuries Cordyceps, which is a genus of more than 400 species in the family Clavicipitaceae, has been used in traditional Chinese medicine. This study highlights the chemistry and pharmacology of Cordyceps, especially Cordyceps sinensis (Berk.) Sacc. and C. militaris (Fr.) L. Information was obtained from Google Scholar and the journal databases PubMed and Scopus. Key findings Many bioactive components of Cordyceps have been extracted, such as cordycepin, cordycepic acid, ergosterol, polysaccharides, nucleosides and peptides. Studies show that Cordyceps and its active principles possess a wide range of pharmacological actions, such as anti-inflammatory, antioxidant, antitumour, antihyperglycaemic, antiapoptosis, immunomodulatory, nephroprotective, and hepatoprotective. Summary More research is required to discover the full extent of the activity of Cordyceps.

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Occurrence of Galβ(1å3)GalNAc-SerThr in the linkage region of polygalactosamine containing fungal glycoprotein from Cordyceps ophioglossoides

Cited by 16 publications

References 7 publications

Structure of the polysaccharide isolated from the sheath of Sphaerotilus natans

Structure of the polysaccharide isolated from the sheath of Sphaerotilus natans

Fungal Galectins, Sequence and Specificity of Two Isolectins from Coprinus cinereus

The genus Cordyceps: a chemical and pharmacological review

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