Comparison of the Multiple Agglutinins of the Acorn Barnacle,<i>Megabalanus rosa</i>

Muramoto, Koji; Ogata, Kyoko; Kamiya, Hisao

doi:10.1080/00021369.1985.10866675

Cited by 3 publications

(4 citation statements)

References 8 publications

(9 reference statements)

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“…BRA were isolated from the hemolymph of M. rosa , and were labeled with fluorerscein isothiocyanate‐I (FITC), as previously described 30 . A D‐galactose (Gal)‐binding lectin, named BRL, was prepared from the hemolymph of Balanus rostratus , as described elsewhere 31 .…”

Section: Methodsmentioning

confidence: 99%

Modulating effect of acorn barnacle C-type lectins on the crystallization of calcium carbonate

et al. 2008

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The modulating effect of invertebrate C‐type lectins on the crystallization of calcium carbonate was investigated. The multiple C‐type lectins, named BRA‐1, ‐2 and ‐3, isolated from the acorn barnacle Megabalanus rosa inhibited the nucleation and growth of calcium carbonate crystals. Among BRA, BRA‐2 most efficiently inhibited the crystal nucleation of aragonite and calcite at the concentrations of > 3.3 and > 26 μg/mL, respectively. The inhibitory activities of BRA were enhanced by the addition of various biomolecules such as D‐glucosamine, D‐galactosamine, chitosan oligosaccharides, L‐arginine and L‐aspartic acid. Although the crystals of aragonite and calcite were formed in the presence of lower concentrations of BRA, the shape and size of the crystals were changed. These results further indicate the participation of the lectins in biomineralization.

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Section: Methodsmentioning

confidence: 99%

Modulating effect of acorn barnacle C-type lectins on the crystallization of calcium carbonate

et al. 2008

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“…Tel/Fax: +81-22-717-8807; E-mail: muramoto@biochem.tohoku.ac.jp Abbreviations: BRA, Megabalanus rosa lectin; BRL, Balanus rostatus lectin; FAC, frontal affinity chromatography; PA, pyridylaminated; pNP, p-nitrophenyl molecular forms with respect to molecular weight, designated BRA-1, BRA-2, and BRA-3. 18) On the other hand, only one C-type lectin, designated BRL, has been isolated from the hemolymph of the acorn barnacle Balanus rostratus.…”

Section: )mentioning

confidence: 99%

“…The binding of the lectins to rabbit erythrocyte ghosts is inhibited by various simple sugars, including D-galactose, D-galactosamine, N-acetyl-D-galactosamine, and N-acetylneuraminic acid, indicating that they have wide sugar-binding specificities and can function as recognition factors for a variety of foreign substances. 18) Inhibition assay of hemagglutination with simple sugars has been used to examine the sugar-binding specificities of most lectins, because no simple method is available to do this with a large repertoire of oligosaccharides. To investigate the detailed sugar-binding specificities of lectins, the frontal affinity chromatography (FAC) system was recently reinforced by an efficient combination of the advantages of high-performance liquid chromatography (HPLC) and a large repertoire of pyridylaminated (PA)-oligosaccharides.…”

Section: )mentioning

confidence: 99%

Diverse Sugar-Binding Specificities of Marine Invertebrate C-Type Lectins

Matsubara¹,

Nakamura‐Tsuruta²,

Hirabayashi³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Scavenging of foreign cells, e.g. sheep erythrocytes introduced into the hemocoel as a model, of invading foreign substances such as lipopolysaccharides and (in the course of normal development) of tissue constituents no longer required, is counted among the functional roles of invertebrate C-type lectins (Muramoto et al, 1985;Takahashi et al, 1985Takahashi et al, , 1986Giga et al, 1987;Suzuki et al, 1990;Inoue et al, 1991;Jomori and Natori, 1991;Kotani et al, 1995;Haq et al, 1996;Hatakeyama et al, 1996). In snake venoms, the appearance of C-type Iectins has been interpreted in a more aggressive mode for the benefit of the predator as strong agglutinins and inhibitors of coagulation or inflammatory responses (Atoda et al, 1991 ;Hirabayshi et al, 1991;Inoue et al, 1991).…”

Section: C-type Lectinsmentioning

confidence: 99%

Animal Lectins

Gabius

1997

European Journal of Biochemistry

435

342

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Protein and lipid glycosylation is no longer considered as a topic whose appeal is restricted to a limited number of analytical experts perseveringly pursuing the comprehensive cataloguing of structural variants. It is in fact arousing curiosity in various areas of basic and applied bioscience. Well founded by the conspicuous coding potential of the sugar part of cellular glycoconjugates which surpasses the storage capacity of oligonucleotide-or oligopeptide-based code systems, recognition of distinct oligosaccharide ligands by endogenous receptors, i.e. lectins and sugar-binding enzymes or antibodies, is increasingly being discovered to play salient roles in animal physiology. Having inevitably started with a descriptive stage, research on animal lectins has now undubitably reached maturity. Besides listing the current categories for lectin classification and providing presentations of the individual families and their presently delineated physiological significance, this review places special emphasis on tracing common structural and functional themes which appear to reverberate in nominally separated lectin and animal categories as well as lines of research which may come to fruition for medical sciences.Keywords: lectin ; glycoprotein; glycolipid; cell adhesion ; molecular recognition ; inflammation; infection ; fertilization ; signal transduction ; tumor biology.The putative multiplicity of functional implications for protein and lipid glycosylation has fueled vigorous and prolific research activities in the last decade. Although glycobiologists continue to be afflicted with the problem of precisely defining the physiological significance of the puzzling variability and complex pattern of carrier-attached saccharide chains, the notion of inherent ligand properties for recognitive protein-carbohydrate interactions is already well established

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Comparison of the Multiple Agglutinins of the Acorn Barnacle,Megabalanus rosa

Cited by 3 publications

References 8 publications

Modulating effect of acorn barnacle C-type lectins on the crystallization of calcium carbonate

Modulating effect of acorn barnacle C-type lectins on the crystallization of calcium carbonate

Diverse Sugar-Binding Specificities of Marine Invertebrate C-Type Lectins

Animal Lectins

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