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Journal ArticleDOI

Agrocybe cylindracea lectin is a member of the galectin family.

01 Oct 2001-Glycoconjugate Journal (Kluwer Academic Publishers-Plenum Publishers)-Vol. 18, Iss: 10, pp 745-749
TL;DR: The complete amino acid sequence of Agrocybe cylindracea lectin was determined from the peptides obtained by chemical cleavages and enzymatic hydrolyses and several insertions suggest that β-strands S2, F3, and S4 and the loop structures between β-Strands F2 & S3 and F5 & S2 are different from those of galectins reported so far.
Abstract: The complete amino acid sequence of Agrocybe cylindracea lectin was determined from the peptides obtained by chemical cleavages and enzymatic hydrolyses. The sequence shows 19.1% and 36.8% identity with those of human galectin-1 and Coprinus lectin-1, a fungal galectin, respectively. Seven residues, which are commonly found in carbohydrate recognizing domain (CRD) of galectins, were conserved. However, several insertions in the sequence, compared with those of human galectin-1 and Coprinus lectin-1, suggest that β-strands S2, F3, and S4 and the loop structures between β-strands F2 & S3 and F5 & S2 are different from those of galectins reported so far.
Citations
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Journal ArticleDOI
TL;DR: An attempt has been made to collate the information on mushroom lectins, their blood group and sugar specificities, with an emphasis on their biomedical potential and future perspectives.
Abstract: Lectins are nonimmune proteins or glycoproteins that bind specifically to cell surface carbohydrates, culminating in cell agglutination. These are known to play key roles in host defense system and also in metastasis. Many new sources have been explored for the occurrence of lectins during the last few years. Numerous novel lectins with unique specificities and exploitable properties have been discovered. Mushrooms have attracted a number of researchers in food and pharmaceuticals. Many species have long been used in traditional Chinese medicines or functional foods in Japan and other Asian countries. A number of bioactive constituents have been isolated from mushrooms including polysaccharides, polysaccharopeptides, polysaccharide–protein complexes, proteases, ribonucleases, ribosome inactivating proteins, antifungal proteins, immunomodulatory proteins, enzymes, lectins, etc. Mushroom lectins are endowed with mitogenic, antiproliferative, antitumor, antiviral, and immunestimulating potential. In this review, an attempt has been made to collate the information on mushroom lectins, their blood group and sugar specificities, with an emphasis on their biomedical potential and future perspectives.

120 citations


Cites background from "Agrocybe cylindracea lectin is a me..."

  • ...Panellus serotinus Late Fall-oyster/Olive oysterling F Yagi et al. (2000)...

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  • ...Coltricia cinnamomea Shiny cinnamon polypore F Yagi et al. (2000)...

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  • ...Agaricus abruptibulbus Abruptly-bulbous agaricus F Yagi et al. (2000)...

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  • ...Cryptoporus volvatus Veiled polypore F Yagi et al. (2000)...

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  • ...A. cylindracea exhibits a unique carbohydrate binding specificity among the known galectins with resistance to the substitution of 3’O of galactosyl moiety and shows a strong affinity to NeuAcα2,3Lac (Yagi, Hiroyama, and Kodama, 2001)....

    [...]

Journal ArticleDOI
TL;DR: This review provides an up-to-date summary on the biochemical, molecular and structural properties of mushroom lectins, as well as their versatile applications specifically focusing on mushroom lectin bioactivity.
Abstract: Lectins are non-immunoglobulin proteins that bind diverse sugar structures with a high degree of selectivity. Lectins play crucial role in various biological processes such as cellular signaling, scavenging of glycoproteins from the circulatory system, cell–cell interactions in the immune system, differentiation and protein targeting to cellular compartments, as well as in host defence mechanisms, inflammation, and cancer. Among all the sources of lectins, plants have been most extensively studied. However, more recently fungal lectins have attracted considerable attention due to their antitumor, antiproliferative and immunomodulatory activities. Given that only 10% of mushroom species are known and have been taxonomically classified, mushrooms represent an enormous unexplored source of potentially useful and novel lectins. In this review we provide an up-to-date summary on the biochemical, molecular and structural properties of mushroom lectins, as well as their versatile applications specifically focusing on mushroom lectin bioactivity.

110 citations

Journal ArticleDOI
TL;DR: The results demonstrate that, similar to the legume lectin fold, the galectin fold represents a conserved structural framework upon which dramatically altered specificities can be grafted by few alterations in the binding site and that, in consequence, many metazoan galECTin-related proteins may represent lectins with novel carbohydrate-binding specificities.

56 citations

Journal ArticleDOI
TL;DR: This review summarizes current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin- type lectins and beta-propeller-type Lectins, as well as mycospin and mycocypin families of protease inhibitors.
Abstract: Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

54 citations


Additional excerpts

  • ...Besides these proteins from C. cinerea, galectins from two different Agrocybe species: ACG from Agrocybe cylindracea and AAG from Agrocybe aegerita, have been characterized (Yagi et al. 2001; Yang et al. 2009) (Table 1)....

    [...]

  • ...cinerea, galectins from two different Agrocybe species: ACG from Agrocybe cylindracea and AAG from Agrocybe aegerita, have been characterized (Yagi et al. 2001; Yang et al. 2009) (Table 1)....

    [...]

Journal ArticleDOI
TL;DR: The refined structure shows that ACG is a "proto"-type galectin composed of a beta-sandwich of two antiparallel sheets, each with six strands, in contrast to the five and six strands in animal galectins, which is among the "layer"-type.

52 citations

References
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Journal ArticleDOI
TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.

11,290 citations

Journal ArticleDOI
TL;DR: Small amounts of myoglobin, beta-lactoglobulin, and other proteins and peptides can be spotted or electroblotted onto polyvinylidene difluoride membranes, stained with Coomassie Blue, and sequenced directly, suggesting that PVDF membranes are superior supports for sequence analysis of picomole quantities of proteins purified by gel electrophoresis.

4,869 citations

Journal ArticleDOI
TL;DR: All amino acids, including proline, are converted quantitatively to phenylthiocarbamyl compounds and these are stable enough to eliminate any need for in-line derivatization, providing results comparable in sensitivity and precision to those obtained by state-of-the-art ion-exchange analyzers.

1,516 citations

Journal ArticleDOI
TL;DR: It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates and a consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era.
Abstract: Animal metal-independent beta-galactoside-binding lectins were initially found in vertebrates, but they have recently been isolated from much lower invertebrates, such as nematode and sponge, as well. Further, an eosinophilic lysophospholipase associated with various inflammatory reactions was very recently found to be a new member of this protein family. It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates. From the viewpoints of protein architecture, the superfamily members can be subdivided into three types; i.e. 'proto type' (the relatively well-studied 14 kDa lectins), 'chimera type' (29-35 kDa lectins also known as epsilon BP/CBP35/Mac2/laminin-binding protein) and 'tandem-repeat type' (a newly found nematode 32 kDa lectin). Comparison of their amino acid sequences and mutagenesis studies have suggested the functional importance of some conservative hydrophilic residues (His44, Asn46, Arg48, Glu71 and Arg73 of human 14 kDa lectin). Several non-charged residues (Gly14, Phe45, Pro47, Phe49, Val59, Trp68, Pro78 and Phe79) are also well conserved, and are probably important to maintain the structural framework of these proteins. A consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era. Ubiquitous occurrence of these homologous lectins with shared sugar specificity suggests that they are involved in 'essential minimum' functions of multicellular animals, possibly in cooperation with their partner glycoconjugates.

487 citations

Journal ArticleDOI
TL;DR: Crystallographic studies revealed that galectins and legume lectins such as concanavalin A have a common topology in spite of the absence of sequence homology, which suggests a possible relationship between animal and plant lectins, and the existence of a lectin super family.
Abstract: Galectins, animal lectins exhibiting specificity for galactosides, are now known to be widely distributed from lower invertebrates, such as sponges and nematodes, to higher vertebrates. The origin of the family can be traced back to the Precambrian era. They are classified into proto-, chimera-, and tandem-repeat types on the basis of protein architecture. The molecular functions of these types should be different because they can cross-link pairs of biomolecules of different combinations. Their biological significance, however, is not yet fully understood because they are involved in too many phenomena, such as differentiation, morphogenesis, metastasis, etc., and too many problems remain unsolved, such as those regarding their controversial cellular localization, mechanism of externalization, etc. Nevertheless, such difficulties seem to indicate their importance as household equipment and their common roles throughout the animal kingdom. They are likely to be responsible for recognizing the N-acetyllactosamine (LacNAc) structure, which is included in various glycoconjugates and considered to be an important glycocode, and then carry out appropriate tasks under given circumstances. Recently, crystallographic studies revealed that galectins and legume lectins such as concanavalin A have a common topology in spite of the absence of sequence homology. This suggests a possible relationship between animal and plant lectins, and the existence of a lectin super family. Studies on the galectin family are becoming increasingly important for glycobiology.

473 citations